|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
862-1942 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1410.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 862 SRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDL 941
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 942 EARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDR 1021
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1022 IAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK 1101
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1102 KEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1181
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1182 LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGK 1261
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1262 GDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1341
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1342 NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQR 1421
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1422 HEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALS 1501
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1502 LARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 1581
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1582 NLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQL 1661
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1662 RKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1741
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1742 LEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGT 1821
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1822 VKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLE 1901
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 2550219468 1902 EAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1942
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1345.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKD---QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 332 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepVDRIIGLDQVAGMSET 651
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD---------------------VDRIVGLDQVTGMTET 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 652 ALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 731
Cdd:cd14920 540 AFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 732 RVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14920 620 RIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
95-785 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1336.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKD----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKEsgkkKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYR-FLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 330 GIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 410 ADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 490 EEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPK-FQKPKQLKDKADF 568
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTQRayfyhrfpilhlepvdriigldqvagm 648
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGG--------------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 649 setalPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQG 728
Cdd:cd01377 531 -----GGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKG 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 729 FPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd01377 606 FPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1329.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 335 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14919 241 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14919 321 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 495 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYA 574
Cdd:cd14919 401 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 575 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepVDRIIGLDQVAGMSETALP 654
Cdd:cd14919 481 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD---------------------VDRIIGLDQVAGMSETALP 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 655 GAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 734
Cdd:cd14919 540 GAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 735 FQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14919 620 FQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1293.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepVDRIIGLDQVAG 647
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD---------------------VDRIVGLDKVAG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 648 MSEtALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQ 727
Cdd:cd14932 540 MGE-SLHGAFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQ 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 728 GFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14932 619 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-785 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1236.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepVDRIIGLDQVAG 647
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD---------------------VDRIVGLDKVSG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 648 MSEtaLPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQ 727
Cdd:cd15896 540 MSE--MPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQ 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 728 GFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd15896 618 GFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1193.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 332 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepVDRIIGLDQVAGMSET 651
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD---------------------VDRIVGLDQMAKMTES 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 652 ALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 731
Cdd:cd14921 540 SLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 732 RVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14921 620 RIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1140.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASShKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 241
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 242 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 321
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 322 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 482 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKpKQ 561
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 562 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEmqstqrayfyhrfpilhlepvdRIIG 641
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDA----------------------EIVG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 642 LDQVAgMSETALpGAfKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 721
Cdd:cd14911 534 MAQQA-LTDTQF-GA-RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEG 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 722 IRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14911 611 IRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1116.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGI 331
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 332 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepVDRIIGLDQVAGMSET 651
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD---------------------VEGIVGLEQVSSLGDG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 652 alPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 731
Cdd:cd14930 539 --PPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPN 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 732 RVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14930 617 RILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
83-785 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1111.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 83 VEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM 162
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 163 QDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 242
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 243 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQE 321
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEEFKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 322 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:pfam00063 240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:pfam00063 320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 482 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQ 561
Cdd:pfam00063 400 HHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 562 lKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEmqstqrayfyhrfpilhlepvdriiG 641
Cdd:pfam00063 477 -QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDY-------------------------E 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 642 LDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 721
Cdd:pfam00063 531 TAESAAANESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEG 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 722 IRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:pfam00063 611 IRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
76-797 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1018.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 76 NPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITD 155
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 156 TAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqGELERQLLQANPILEAFGNAKTVKNDNSSRF 235
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---GSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 236 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQ 314
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGcLTVDGID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 315 DKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNT-AAQKVSHLLGINVTDFTRGILTPR 393
Cdd:smart00242 238 DAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALTKRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:smart00242 318 IKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCINYAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTH 553
Cdd:smart00242 397 EKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECRFPKGTDQTFLEKLNQHHKKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 554 PKFQKPKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQStqrayfyhrfpilhl 633
Cdd:smart00242 474 PHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN--------------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 634 epvdriigldqvagmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQL 713
Cdd:smart00242 538 ------------------------AGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQL 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 714 RCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLE 793
Cdd:smart00242 594 RYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELE 673
|
....
gi 2550219468 794 EERD 797
Cdd:smart00242 674 ELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1172 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 905.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 32 VWVPSDKSGFEPASLKEEVGEEAIVEL---VENGKKVKVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKERYY 106
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 107 SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKK 186
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 187 VIQYLAYVASSHKSkkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIR 266
Cdd:COG5022 172 IMQYLASVTSSSTV--EISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 267 QAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT-IPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISG 345
Cdd:COG5022 250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 346 VLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERM 425
Cdd:COG5022 330 ILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 426 FRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFg 505
Cdd:COG5022 409 FDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 506 LDLQPCIDLIEKpAGPPGILALLDEECWFPKATDKSFVEKVMQ--EQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADE 583
Cdd:COG5022 487 FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYDVEG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 584 WLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQstqrayfyhrfpilhlepvdriigldqvagmsetalpgafKTRKGM 663
Cdd:COG5022 564 FLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN----------------------------------------IESKGR 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 664 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 743
Cdd:COG5022 604 FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYR 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 744 ILTPNS----IPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERDLKITDVIIGFQACCRGYLARKA 819
Cdd:COG5022 684 ILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRR 763
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 820 FAKRQQQLTAMKVLQRNCAAYLKLRNWQWWRLFTKVKPLLQVSRQEEEMMAKEEElvkVREKQLAAENRLTEMETLQSQL 899
Cdd:COG5022 764 YLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLAC---IIKLQKTIKREKKLRETEEVEF 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 900 MAEKLQLQEQLqaetelcAEAEELRAR-LTAKKQELEEIChdlEARVEEEEERCQHLQAEKKKMQQniqeleeqleeeeS 978
Cdd:COG5022 841 SLKAEVLIQKF-------GRSLKAKKRfSLLKKETIYLQS---AQRVELAERQLQELKIDVKSISS-------------L 897
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 979 ARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLL------EDRIAEFTTNLTEEE--EKSKSLAKLKNKHEAMI 1050
Cdd:COG5022 898 KLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLnnidleEGPSIEYVKLPELNKlhEVESKLKETSEEYEDLL 977
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1051 TDLEERLRREEKQRQELEKTRRKLegdsTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVEEEAAQKNMaLKKIREL 1130
Cdd:COG5022 978 KKSTILVREGNKANSELKNFKKEL----AELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTELSI-LKPLQKL 1051
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|..
gi 2550219468 1131 ESQISELQEDLEseraSRNKAEKQKRDLGEELEALKTELEDT 1172
Cdd:COG5022 1052 KGLLLLENNQLQ----ARYKALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
95-785 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 873.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLAYVASSHKSKKD--QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL-----SNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNT--DQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQ-GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 484 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLK 563
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 564 DKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdemqstqrayfyhrfpilhlepvdriigld 643
Cdd:cd00124 478 KLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ-------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 644 qvagmsetalpgafktrkgmfrtvgqlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 723
Cdd:cd00124 519 ---------------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVR 571
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 724 ICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd00124 572 IRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 781.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVAS---------SHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 245
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 246 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETM 323
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVsmNPYD-YHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 324 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 403
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 404 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 484 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKP--- 559
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 560 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTQRAyfyhrfpilhlepvdri 639
Cdd:cd14927 476 KKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTE----------------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 640 iglDQVAGMSETalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVL 719
Cdd:cd14927 539 ---DPKSGVKEK------RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVL 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 720 EGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK-GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14927 610 EGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
96-785 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 755.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVASS-----HKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLIttNPYD-YPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 329 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKA 566
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 567 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepvdriigldq 644
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT------------------------------ 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 645 VAGMSETALPGAFKTRKG-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 723
Cdd:cd14913 526 FATADADSGKKKVAKKKGsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIR 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 724 ICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14913 606 ICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 749.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKD-QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDgKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNK-YRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKeYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 333 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 493 QREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK---ADF 568
Cdd:cd14934 400 KREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdKFVSELWKDEmqstqrayfyhrfpilhlepvdriigldqvagm 648
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFKE--------------------------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 649 sETALPGAFKTRKG-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQ 727
Cdd:cd14934 523 -EEAPAGSKKQKRGsSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRK 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 728 GFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14934 602 GFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 748.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAkskGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL-EPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMG 330
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 331 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 411 DFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 491 EYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLK---DKA 566
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMqstqrayfyhrfpilhlepvdriiglDQVA 646
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHA--------------------------GQSG 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 647 GMSETAlpGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICR 726
Cdd:cd14909 531 GGEQAK--GGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICR 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2550219468 727 QGFPNRVVFQEFRQRYEILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14909 609 KGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
95-785 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 724.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDILGFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 333 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14929 239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14929 319 AVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 493 QREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK--ADFC 569
Cdd:cd14929 398 RKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMqstqrayfyhrfpilhlepvdriigldqvagMS 649
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYI-------------------------------ST 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 650 ETALPGAFKTRK--GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQ 727
Cdd:cd14929 524 DSAIQFGEKKRKkgASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICRE 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2550219468 728 GFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14929 604 GFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
96-785 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 708.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSG-LIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKKdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET---QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFA 413
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 414 IEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd01380 319 RDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 493 QREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPK--FQKPKQLKDKadFCI 570
Cdd:cd01380 399 VKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA--FIV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwkdemqstqrayfyhrfpilhlepvdriigldqvagmse 650
Cdd:cd01380 473 KHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS----------------------------------------------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 651 talpgafKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 730
Cdd:cd01380 506 -------KNRK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFP 575
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 731 NRVVFQEFRQRYEILTPNSIPKGfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd01380 576 SRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
96-785 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 706.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVAS-SHKSKKDQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQtpgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 329 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK- 565
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 566 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepvdriigldq 644
Cdd:cd14917 476 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN------------------------------ 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 645 VAGMSETALPGAFKTRKG-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 723
Cdd:cd14917 526 YAGADAPIEKGKGKAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIR 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 724 ICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14917 606 ICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
96-785 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 687.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVAS-SHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtnNPYD-YAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK 565
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 566 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEmqstqrayfyhrfpilhlepvdriigld 643
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---------------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 644 QVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 723
Cdd:cd14916 528 ASADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIR 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 724 ICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14916 608 ICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-785 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 686.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVASSHKSKKD------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLkTDLLLEPYNKYR--FLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDK 565
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 566 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTqrayfyhrfpilhlepvdriigld 643
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAE------------------------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 644 qvAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 723
Cdd:cd14923 532 --AGDSGGSKKGG-KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIR 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 724 ICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14923 609 ICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
97-785 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 684.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 176
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 177 GAGKTENTKKVIQYLAYVASSHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 330 GIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 408
Cdd:cd14918 242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 409 QADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 489 QEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 568 --FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWkdemqSTQRAyfyhrfpilhlepvdriigldqv 645
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-----STYAS----------------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 646 AGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIC 725
Cdd:cd14918 529 AEADSGAKKGA-KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIC 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 726 RQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14918 608 RKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-785 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 676.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKD 564
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQStqrayfyhrfpilhlepvdriigl 642
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTA------------------------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 643 dQVAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 722
Cdd:cd14912 532 -EGASAGGGAKKGG-KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 723 RICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14912 610 RICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-785 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 675.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 565 K--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTQRAyfyhrfpilhlepvdriiGL 642
Cdd:cd14910 476 KveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEE------------------GG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 643 DQVAGmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 722
Cdd:cd14910 538 GKKGG----------KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 723 RICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14910 608 RICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
96-785 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 668.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVASSHKskkdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--HLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 333 EEEQMGLLRVISGVLQLGNIVFKK-ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14883 236 EEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEAR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14883 316 DNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 492 YQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTQRAyfyhrfpilhlepVDRIIGLDQVAGMSET 651
Cdd:cd14883 472 HYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTG-------------LSISLGGDTTSRGTSK 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 652 ALPgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 731
Cdd:cd14883 539 GKP-----------TVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPI 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 732 RVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14883 608 HLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-785 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 665.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLIttNPYD-FAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepvdriigl 642
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG---------------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 643 DQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 722
Cdd:cd14915 528 GQTAEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGI 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 723 RICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14915 608 RICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
96-785 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 646.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVASshkskkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 335 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd01383 234 DQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd01383 314 DALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 495 EGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPkqlKDKAdFCIIHYA 574
Cdd:cd01383 394 DGIDWTKVDF-EDNQECLDLIEKK--PLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RGGA-FTIRHYA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 575 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVselwkdemqstqrayfyHRFPILHLEPVDRIigldqvagmsetALP 654
Cdd:cd01383 467 GEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLP-----------------QLFASKMLDASRKA------------LPL 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 655 GAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 734
Cdd:cd01383 518 TKASGSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMT 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 735 FQEFRQRYEILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd01383 598 HQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
96-785 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 645.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVasshkSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGA 252
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV-----SGGSESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 332 PEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG---RDYVQKAQTKE 408
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFVEKVMQEQGTHPKFQKPKQLKD--K 565
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEEK--PPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 566 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTQRayfyhRFPIlhlepvdriigldqv 645
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSK-----KRPP--------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 646 agmsetalpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIC 725
Cdd:cd01378 533 --------------------TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVR 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 726 RQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd01378 593 RAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
95-785 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 629.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLAYVASshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDVVGIS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 333 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPD---NTAAQKVSHLLGINVTDFTRGiLTPRIKVGRD-YVQKAQTKE 408
Cdd:cd01384 239 EEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgIITKPLDPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 409 QADFAIEALAKATYERMFRWLVLRINKAL--DKTKRqgaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd01384 318 AATLSRDALAKTIYSRLFDWLVDKINRSIgqDPNSK---RLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEKpaGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKqlKDKA 566
Cdd:cd01384 395 MEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSRT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdemqstqrayfyhrFPILHLEpvdriigldqva 646
Cdd:cd01384 470 DFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGL----------------FPPLPRE------------ 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 647 gmsetalpgafKTRKGM-FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIC 725
Cdd:cd01384 522 -----------GTSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRIS 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 726 RQGFPNRVVFQEFRQRYEILTPNsIPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 785
Cdd:cd01384 591 CAGYPTRKPFEEFLDRFGLLAPE-VLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
95-785 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 611.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHSW------IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLMFTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 334 EEQMGLLRVISGVLQLGNIVFKK--ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd01381 235 EEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGAS--FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01381 315 DVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 490 EEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAdF 568
Cdd:cd01381 395 EEYDKEGINWQHIEF-VDNQDVLDLIaLKPM---NIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTS-F 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMqstqrayfyhrfpilhlepvdriigldqvAGM 648
Cdd:cd01381 470 GINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI-----------------------------SMG 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 649 SETAlpgafKTRKgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQG 728
Cdd:cd01381 521 SETR-----KKSP----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAG 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 729 FPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd01381 592 YPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-785 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 591.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLAYVASSHkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG-----AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01382 156 VSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL---------------KDPLLDDVGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 334 EEQMGLLRVISGVLQLGNIVFKKERNT-------DQASMPDNTAAqkvSHLLGINVTDF-----TRGILTPRIKVGRDYV 401
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYA---AELLGLDQDELrvsltTRVMQTTRGGAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 482 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKP-- 559
Cdd:cd01382 376 ERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPrk 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 560 ------KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdemqstqrayfyhrFPILHL 633
Cdd:cd01382 453 sklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSL----------------FESSTN 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 634 EPVDRiiglDQVAGmsetalpgafktrKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQL 713
Cdd:cd01382 517 NNKDS----KQKAG-------------KLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQL 579
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 714 RCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd01382 580 QCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
95-785 |
1.62e-180 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 562.09 E-value: 1.62e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASShkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAgeHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQAS---MPDNTAAQKVSHLLGINVTDFTRGILTPRIKV-GRDYVQKAQTKEQ 409
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 410 ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 490 EEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFC 569
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKK--QPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTEFI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdemqstqrayfyhrFPILHlepvdriigldqvagms 649
Cdd:cd14872 470 VKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVL----------------FPPSE----------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 650 etalpGAFKTRKGmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGF 729
Cdd:cd14872 517 -----GDQKTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGY 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 730 PNRVVFQEFRQRYEILtPNSIPKGFM-DGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14872 589 PFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
95-785 |
1.40e-177 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 554.75 E-value: 1.40e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVAsshksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-----QRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAIT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01387 155 SQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQ---ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd01387 235 EEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd01387 315 LDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 491 EYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlkDKADFCI 570
Cdd:cd01387 394 EYIREQIDWTEIAF-ADNQPVINLISKK--PVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPEFTI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdemqstqrayfyhrfpilhlepvdriigldQVAGMSE 650
Cdd:cd01387 469 KHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS------------------------------SHRAQTD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 651 TALP----GAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICR 726
Cdd:cd01387 519 KAPPrlgkGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRK 598
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 727 QGFPNRVVFQEFRQRYEILTPNSIPKGfMDGKQACVLMIKALELD-SNLYRIGQSKVFFR 785
Cdd:cd01387 599 EGYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
95-785 |
1.26e-175 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 549.76 E-value: 1.26e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQ----DREDQS 169
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 170 ILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------------GELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 237 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 317 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmpDNTAAQKVSH---LLGINVTDFTRGILTPR 393
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-KPAGPPGILALLDeECWFPKAT--DKSFVEKVMQEQ 550
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 551 GT-------------HPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvselwkdemq 617
Cdd:cd14890 476 GRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 618 STQRayfyhrfpilhlepvdriigldqvaGMSetalpgafktrkgmfrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNH 697
Cdd:cd14890 542 RSIR-------------------------EVS-----------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNE 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 698 EKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSipkgfMDGKQACVLMIKALELDSNLYRI 777
Cdd:cd14890 580 TKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQI 654
|
....*...
gi 2550219468 778 GQSKVFFR 785
Cdd:cd14890 655 GSSKIFLK 662
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-785 |
3.48e-173 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 543.89 E-value: 3.48e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVasshkSKKDQGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL-----SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHvTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01385 156 VEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCY-TLEGEDEKYEFERLKQAMEMVGF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 332 PEEEQMGLLRVISGVLQLGNIVFKKER-NTDQASMPDNTAAQK-VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01385 235 LPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKLPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 410 ADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd01385 315 AIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 486 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPkQLKDK 565
Cdd:cd01385 394 KLEQEEYKKEGISWHNIEY-TDNTGCLQLISKK--PTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVMEP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 566 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL----------WKdEMQSTQRAYFyhrfpILHLEP 635
Cdd:cd01385 470 A-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrWA-VLRAFFRAMA-----AFREAG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 636 VDRIIGLDQVAGM----SETALPGAFKTRKGMfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLD 711
Cdd:cd01385 543 RRRAQRTAGHSLTlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLR 620
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 712 QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnsIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd01385 621 QLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
95-783 |
3.29e-171 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 537.45 E-value: 3.29e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY------KGKKRHEMPPHIYAITDTAYRSMMQDRE-- 166
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 167 --DQSILCTGESGAGKTENTKKVIQYLAYVASshKSKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKFI 239
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS--ATTHGQNATERenvrdRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 240 RINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKD 317
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 318 MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-KKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKV 396
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 397 GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAS-FIGILDIAGFEIFDLNSFEQLCINYTNEK 475
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 476 LQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQG 551
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 552 THPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdemqstqrayfyhrfpil 631
Cdd:cd14901 472 KHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS--------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 632 hlepvdriigldqvagmsetalpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLD 711
Cdd:cd14901 531 ----------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLE 576
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 712 QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNL-----YRIGQSKVF 783
Cdd:cd14901 577 QLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
95-785 |
4.74e-170 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 534.36 E-value: 4.74e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLAYVAsshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLsgAGEHLKTDLLLEPYNKYRFL-SNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 329 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASM--PDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14903 230 IGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14903 310 KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVMqeqGTHPKFQK----PKQl 562
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPRT- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 563 kDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepvdrIIGL 642
Cdd:cd14903 461 -SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE------------------------KVES 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 643 DQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 722
Cdd:cd14903 516 PAAASTSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAI 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 723 RICRQGFPNRVVFQEFRQRYEILTPNSiPKGFMDGKQACVLMIKALELDS-NLYRIGQSKVFFR 785
Cdd:cd14903 596 RISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
96-785 |
1.48e-168 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 529.16 E-value: 1.48e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVasshkSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSNGHVTIPG----QQDKDMFQETMEAMRIMG 330
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDivnnSGNREKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 331 IPEEEQMGLLRVISGVLQLGNIVFK---KERNTDQASM-PDNTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQ 405
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADEL-QEALTSHSVVTRgETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 406 TKEQADFAIEALAKATYERMFRWLVLRINKAL--DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd01379 316 TVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 484 MFILEQEEYQREGIEWNFIDFGlDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPkFQKPKql 562
Cdd:cd01379 396 IFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVselwkdemQSTQRAYFyhRFPILHLepvdriigl 642
Cdd:cd01379 469 SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV--------RQTVATYF--RYSLMDL--------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 643 dqvagmsetalpgafktrkgmfrtvgqlykeqLAKLMATLrntnPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 722
Cdd:cd01379 530 --------------------------------LSKMVVGQ----PHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETT 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 723 RICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 785
Cdd:cd01379 574 RIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
95-785 |
1.89e-167 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 526.57 E-value: 1.89e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKK-RHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLayvasSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14897 81 GESGAGKTESTKYMIKHL-----MKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD-------KDMFQETMEAM 326
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLTNIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14897 236 KLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 407 KEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14897 316 LRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKql 562
Cdd:cd14897 396 YVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFKK--PLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASP-- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdemqstqrAYFyhrfpilhlepvdriigl 642
Cdd:cd14897 471 GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT--------SYF------------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 643 dqvagmsetalpgafktrkgmfrtvgqlyKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 722
Cdd:cd14897 525 -----------------------------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIA 575
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 723 RICRQGFPNRVVFQEFRQRYEILTPNSiPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 785
Cdd:cd14897 576 KIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
95-747 |
2.55e-165 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 521.95 E-value: 2.55e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD--------- 244
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL--VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN------------------- 305
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGAdakpisidmssfephlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 306 -----GHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQ---KVSHL 377
Cdd:cd14888 238 yltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 378 LGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFE 457
Cdd:cd14888 318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKA 537
Cdd:cd14888 398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFVPGG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 538 TDKSFVEKVMQEQGTHPKFQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdemq 617
Cdd:cd14888 475 KDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS---- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 618 stqrAYFyhrfpilhlepvDRIIGLdqvagmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNH 697
Cdd:cd14888 549 ----AYL------------RRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2550219468 698 EKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 747
Cdd:cd14888 598 QNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
95-785 |
2.30e-164 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 518.58 E-value: 2.30e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLAYVASSH---KSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 330 GIPEEEQMGLLRVISGVLQLGNIVFKkerNTDQASMPDNTAAQKVSHLLGINVTDFTRgILTPRIKVGR-DYVQKAQTKE 408
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTD-ALTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 409 QADFAIEALAKATYERMFRWLVLRINKALdkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDkaDF 568
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWkdemqstqrayfyhrfpilhlepvdriiglDQVAGM 648
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF------------------------------EHVSSR 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 649 SETALPGAFKTRKGmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQG 728
Cdd:cd14873 519 NNQDTLKCGSKHRR--PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAG 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 729 FPNRVVFQEFRQRYEILTPNSIPKGFMDGKqaCVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14873 597 YAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-785 |
9.76e-163 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 514.31 E-value: 9.76e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEM---PPHIYAITDTAYRSMMQDR----ED 167
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 168 QSILCTGESGAGKTENTKKVIQYLA----YVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMF 319
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 320 QETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFkkERNTDQ----ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIK 395
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 396 VGRDYV-QKAQTKEQADFAIEALAKATYERMFRWLVLRINKAldkTKRQG------------ASFIGILDIAGFEIFDLN 462
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINAC---HKQQTsgvtggaasptfSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 463 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKS 541
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 542 FVEKVMQEQ-GTHPKFQKPKQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdemqstq 620
Cdd:cd14892 473 LLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK--------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 621 rayfyhrfpilhlepvdriigldqvagmsetalpgafktrkgmFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKK 700
Cdd:cd14892 536 -------------------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKF 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 701 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS-IPKGFMDGKQACVLMIKALE-----LDSNL 774
Cdd:cd14892 566 PGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNKaGVAASPDACDATTARKKCEEivaraLEREN 645
|
730
....*....|.
gi 2550219468 775 YRIGQSKVFFR 785
Cdd:cd14892 646 FQLGRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
97-785 |
1.17e-151 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 484.03 E-value: 1.17e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM----QDREDQSILC 172
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 173 TGESGAGKTENTKKVIQYLAYVAsshkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGA 252
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHvtipGQQD-----KDMFQETMEAMR 327
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA----GCKRevqywKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKkerntdqasmPDNTAAQKVSH-------------------LLG--INVTDFT 386
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFE----------MDDDEALKVENdsngwlkaaagqfgvseedLLKtlTCTVTFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 387 RGiltprikvgrDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQG--ASFIGILDIAGFEIFDLNSF 464
Cdd:cd14889 302 RG----------EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIekPAGPPGILALLDEECWFPKATDKSFVE 544
Cdd:cd14889 372 EQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 545 KVMQEQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTQRayf 624
Cdd:cd14889 449 KLNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGT--- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 625 yhrfpilhLEPVDRIIGLDQVAGMSetalpgafkTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKL 704
Cdd:cd14889 524 --------LMPRAKLPQAGSDNFNS---------TRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQL 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 705 DPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL--TPNsIPKgfmdGKQACVLMIKALELDSnlYRIGQSKV 782
Cdd:cd14889 584 DSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRL 656
|
...
gi 2550219468 783 FFR 785
Cdd:cd14889 657 FFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
95-748 |
5.30e-148 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 474.13 E-value: 5.30e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH--------EMPPHIYAITDTAYRSMMQDR 165
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 166 EDQSILCTGESGAGKTENTKKVIQYL--------------AYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsqqeqnseevlTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 232 SSRFGKFIRINFD-VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLS---NG 306
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYlkkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 307 HVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQA--SMPDNTAAQKVSHLLGINVTD 384
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 385 FTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------DKTKRQGASFIGILDIAGFE 457
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP 535
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 536 KATDKSFVEKVMQEQGTHPKFQKPKQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDE 615
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 616 MQSTQRAYFYhrfpilhlepvdriigldqvagmsetalpgaFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIP 695
Cdd:cd14907 557 DGSQQQNQSK-------------------------------QKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKP 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 696 NHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 748
Cdd:cd14907 606 NEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
96-751 |
1.51e-143 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 460.54 E-value: 1.51e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY-----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 164 ----DREDQSILCTGESGAGKTENTKKVIQYLAYV-----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 235 FGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlktdlllepynkyrflsnghvtipGQQ 314
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------------AAR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 315 DKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD-QASMPDNTAAQKV------SHLLGINVTDFTR 387
Cdd:cd14900 217 KRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 388 GILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGAS-FIGILDIAGFEIFDLNS 463
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 464 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFV 543
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 544 EKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndniatllhqssdkfvselwkdemqstqray 623
Cdd:cd14900 454 SKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------------------------------- 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 624 fyhrfpILHLEPVDriigldqvagmsetalpgafktrkgMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGK 703
Cdd:cd14900 501 ------VLHQEAVD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGI 548
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2550219468 704 LDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIP 751
Cdd:cd14900 549 YERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
95-785 |
1.07e-141 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 456.04 E-value: 1.07e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERyySGLI----YTYSGLFCVVINPYKNLPiysEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE---D 167
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 168 QSILCTGESGAGKTENTKKVIQYL------------AYVASSHKSKKDQG-ELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttravggkkasgQDIEQSSKKRKLSVtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 235 FGKFIRINFDVNGY-IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPG 312
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 313 QQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKK----ERNTDQASMPDNTAAQKVSHLLGINVTDFTRG 388
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 389 ILTPRIkVGRDYVQKAQ-TKEQADFAIEALAKATYERMFRWLVLRINKALDKtKRQGASFIGILDIAGFEIFDL-NSFEQ 466
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 467 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKV 546
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 547 MQEQGTHPKFQKPKQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHqSSDKFVselwkDEMQStqrayfy 625
Cdd:cd14891 471 HKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKFS-----DQMQE------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 626 hrfpilhlepvdriigldqvagmsetalpgafktrkgmfrtvgqlykeqlakLMATLRNTNPNFVRCIIPNHEKKAGKLD 705
Cdd:cd14891 537 ----------------------------------------------------LVDTLEATRCNFIRCIKPNAAMKVGVFD 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 706 PHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIK-ALELDSNLYRIGQSKVFF 784
Cdd:cd14891 565 NRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFF 644
|
.
gi 2550219468 785 R 785
Cdd:cd14891 645 R 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
95-785 |
5.95e-139 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 448.62 E-value: 5.95e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14904 156 CETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 332 PEEEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQTKEQA 410
Cdd:cd14904 236 DNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRI-EEALCNRSVVTRnESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 491 EYQREGIEWNFIDFGlDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKPKQlkDKAD 567
Cdd:cd14904 394 EYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV--KRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWkdemqstqrayfyhrfpilhlepvdriiglDQVAG 647
Cdd:cd14904 468 FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF------------------------------GSSEA 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 648 MSETALPGAFKTRKGMfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQ 727
Cdd:cd14904 518 PSETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRS 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2550219468 728 GFPNRVVFQEFRQRYEILTPNSIPKGfmDGKQACVLMIKALELDSNL-YRIGQSKVFFR 785
Cdd:cd14904 597 GYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
95-785 |
4.00e-137 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 443.07 E-value: 4.00e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLayvaSSHKSKKDQGELeRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL----SSLYQDQTEDRL-RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQ--ASMPDNTAAQKVSHLLGINvTDFTRGILTPRIKV-GRDYVQKAQTKEQA 410
Cdd:cd14896 235 EELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPVEGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14896 314 IDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 490 EEYQREGIEWNFIDfGLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlkDKADFC 569
Cdd:cd14896 394 EECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLPVFT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWkdemQSTQRAYfyhrfpilhlepvdriiGLDQVAGms 649
Cdd:cd14896 469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF----QEAEPQY-----------------GLGQGKP-- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 650 etalpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGF 729
Cdd:cd14896 526 ----------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGF 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 730 PNRVVFQEFRQRYEILTPNSIPkGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14896 590 PVRVPFQAFLARFGALGSERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
95-768 |
1.05e-135 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 441.64 E-value: 1.05e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYK--------GKKRHEMPPHIYAITDTAYRSMMQ-D 164
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 165 REDQSILCTGESGAGKTENTKKVIQYLAYV----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT---IPGQQDKD 317
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSfarKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 318 --MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKE-RNTDQASMPDNTAAQ--KVSHLLGINVTDFTRGILTP 392
Cdd:cd14902 241 aqLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 393 RIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD--------KTKRQGASFIGILDIAGFEIFDLNSF 464
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVE 544
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDK--SNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 545 KVMQEQGThpkfqkpkqlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSelwkdemqstqrayf 624
Cdd:cd14902 478 KFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV--------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 625 yhrfpilhlepvdrIIGLDQVAGMSETALPGAFKTRKGMFRT--VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAG 702
Cdd:cd14902 531 --------------AIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPG 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 703 KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL-----TPNSIPK-GFMDGKQA--CVLMIKAL 768
Cdd:cd14902 597 IFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFkcflsTRDRAAKmNNHDLAQAlvTVLMDRVL 670
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
95-785 |
7.88e-132 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 429.71 E-value: 7.88e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK--GKKRHE-------MPPHIYAITDTAYRSMMQD- 164
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 165 REDQSILCTGESGAGKTENTKKVIQYLAYVASSHK-SKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKF 238
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgAPNEGEELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 239 IRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--------HLKTDLLLEPYNKYRFLSNGHVTI 310
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 311 PGQ-QDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQK----VSHLLGINVTDF 385
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 386 TRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSF 464
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFV 543
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 544 EKVM--------QEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLM-KNmdplndniatllhqssdkfvselwKD 614
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKN------------------------KD 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 615 EmqstqrayfyhrfpilhlepvdriigldqvagmsetaLPgafKTRKGMFRTvGQLYKEQLAKLMATLRNTNPNFVRCII 694
Cdd:cd14908 533 E-------------------------------------IP---LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIK 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 695 PNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnSIPK----GFMDGKQACVLMIKALEL 770
Cdd:cd14908 572 PNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCK 650
|
730 740 750
....*....|....*....|....*....|..
gi 2550219468 771 DSNLYR-----------------IGQSKVFFR 785
Cdd:cd14908 651 DLVKGVlspamvsmknipedtmqLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
93-828 |
1.07e-129 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 428.29 E-value: 1.07e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 93 NEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHE-MPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 172 CTGESGAGKTENTKKVIQYLAYVASSHKSKKDQgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFASSKSGNMDLKIQ----NAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:PTZ00014 264 GSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 332 PEEEQMGLLRVISGVLQLGNIVF--KKERNTDQASM--PDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:PTZ00014 344 SESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:PTZ00014 424 KDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDK 565
Cdd:PTZ00014 503 RESKLYKDEGISTEELEY-TSNESVIDLLcGKGK---SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 566 aDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD-EMQSTQRAyfyhrfpilhlepvdriigldq 644
Cdd:PTZ00014 579 -NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGvEVEKGKLA---------------------- 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 645 vagmsetalpgafktrKGMFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 724
Cdd:PTZ00014 636 ----------------KGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQL 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 725 CRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR---AGVLAHLEEERDLKIT 801
Cdd:PTZ00014 698 RQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWE 777
|
730 740
....*....|....*....|....*..
gi 2550219468 802 DVIIGFQACCRGYLARKAFAKRQQQLT 828
Cdd:PTZ00014 778 PLVSVLEALILKIKKKRKVRKNIKSLV 804
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
96-785 |
2.10e-128 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 420.90 E-value: 2.10e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPiyseeivEMYKGKKRHE-------MPPHIYAITDTAYRSMMQ----- 163
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 164 --DREDQSILCTGESGAGKTENTKKVIQYLAYVASSHK----SKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 237
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTatssSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 238 FIRINF-----DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNG--HV 308
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGqcYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 309 TIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD---------------QASMPDNTAAQK 373
Cdd:cd14895 235 RNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 374 ---VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTK--------- 441
Cdd:cd14895 315 ldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 442 -RQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEkpAG 520
Cdd:cd14895 395 nKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE--QR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 521 PPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIAT 598
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 599 LLHQSSDKFVSELWKDEMQSTQRAYFYHRFPILHLEPVDRIIGLdqvagmsetalpgafktrkgmfrtvGQLYKEQLAKL 678
Cdd:cd14895 550 VLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVGI-------------------------GSQFKQQLASL 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 679 MATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGK 758
Cdd:cd14895 605 LDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASA 684
|
730 740
....*....|....*....|....*..
gi 2550219468 759 QACVLMIKALELdsnlyriGQSKVFFR 785
Cdd:cd14895 685 LIETLKVDHAEL-------GKTRVFLR 704
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
95-785 |
3.70e-123 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 405.15 E-value: 3.70e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKyrflSNGHVTIPGQQDKDM------FQETMEAMR 327
Cdd:cd01386 156 IQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAAMK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGI------------LTPRIK 395
Cdd:cd01386 232 TLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 396 VGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEifdlN----------SFE 465
Cdd:cd01386 312 ESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGFQ----NpahsgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 466 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAG------------PPGILALLDEECW 533
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 534 FPKATDKSFVEKVMQEQG--THPKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNIATLLHQSSDKF 607
Cdd:cd01386 467 YPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 608 vselwkdemqstqrayfyhrfpilhlepvdriigldqvagmsetalpgAFKTRKGMFRTVgqlyKEQLAKLMATLRNTNP 687
Cdd:cd01386 547 ------------------------------------------------AAVKRKSPCLQI----KFQVDALIDTLRRTGL 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 688 NFVRCIIPNHE------KKAGKLDPHLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGF- 754
Cdd:cd01386 575 HFVHCLLPQHNagkderSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGl 654
|
730 740 750
....*....|....*....|....*....|....*
gi 2550219468 755 ----MDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd01386 655 nsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
95-783 |
7.62e-121 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 397.44 E-value: 7.62e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDLRIQ----TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLsNGHVT-IPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFL-NPKCLdVPGIDDVADFEEVLESLKSMGLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 333 EEEQMGLLRVISGVLQLGNIVFKKErntDQASMPDntAA----------QKVSHLLGINVTDFTRGILTPRIKVGRDYVQ 402
Cdd:cd14876 236 EEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 483 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFqKPKQL 562
Cdd:cd14876 390 IVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlEPVDRiiGl 642
Cdd:cd14876 466 DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-------------------VVVEK--G- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 643 dqvagmsetalpgafKTRKGMFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 722
Cdd:cd14876 524 ---------------KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEAL 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 723 RICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVF 783
Cdd:cd14876 587 QLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
95-783 |
2.18e-120 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 396.53 E-value: 2.18e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDRE--DQSI 170
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 171 LCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERieqRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIpgqqDKDMFQETMEAMR 327
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS---HLLGINVTDFTRGILTPRIKVGRDYV--Q 402
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRtsaLLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQL 562
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdemqstqrayfyhrFPIlhlEPVDRiigl 642
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKL----------------FPA---NPEEK---- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 643 DQVAGMSETALPGAfktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 722
Cdd:cd14880 531 TQEEPSGQSRAPVL---------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETI 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 723 RICRQGFPNRVVFQEFRQRYEILTPN--SIPKGFMDGKQAcvlmikalELDSNLYRIGQSKVF 783
Cdd:cd14880 602 HISAAGFPIRVSHQNFVERYKLLRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
95-781 |
1.67e-118 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 392.81 E-value: 1.67e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDREDQSILC 172
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 173 TGESGAGKTENTKKVIQYLAYVASSHKSKK-----DQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRsSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 247 GYIVGANIETYLLEKSR-AIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP-YNKYRFL--------------SNGHVTI 310
Cdd:cd14906 161 GKIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 311 PGQQDKD-MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQAS--MPDNTAA-QKVSHLLGINVTDFT 386
Cdd:cd14906 241 NNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 387 RGILTPRIKV-GRDYVQ-KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDK----------TKRQGASFIGILDIA 454
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 455 GFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWF 534
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 535 PKATDKSFVEKVMQEQGTHPKFQkpKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKd 614
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYY--QRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 615 emqstqrayfyhrfpilhlepvdriigldqvagMSETALPGAFKTRKGMFRTVGQlYKEQLAKLMATLRNTNPNFVRCII 694
Cdd:cd14906 555 ---------------------------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIK 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 695 PNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNL 774
Cdd:cd14906 601 PNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKT 680
|
....*..
gi 2550219468 775 YRIGQSK 781
Cdd:cd14906 681 MGISNNK 687
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
95-785 |
3.30e-112 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 372.99 E-value: 3.30e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYS-GLIYTYSGLFCVVINPYKNLPIYSEEIVEMY-KGKKRHEMPPHIYAITDTAYRSM-MQDREDQSIL 171
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 172 CTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQ----LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKidenLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLSNGHVTI----PGQ--QDKDMF 319
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVrrgvDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 320 QETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILtprIKVGRD 399
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 400 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD-KTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQ 478
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 479 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQE-QGTHPKFQ 557
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKSPYFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 558 KPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTQRAyfyhrfpilhlepvd 637
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK--------------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 638 riigldqvagmsetalpgafktrkgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 717
Cdd:cd14875 538 ---------------------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAG 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 718 VLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGK--QACVLMI----KALELDSNLYRIGQSKVFFR 785
Cdd:cd14875 591 VLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLayyqRLYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-785 |
5.50e-108 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 360.36 E-value: 5.50e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH-----EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 169 SILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-----VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMR 327
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 328 IMgIPEEEQMGLLRVISGVLQLGNIVFKKERN--TDQASMPDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTM 484
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 485 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPAgpPGILALLDEECWFPKATDKSFVE---KVMQEQGTHPKfqKPKQ 561
Cdd:cd14886 394 FKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPN--LSIFSFLEEQCLIQTGSSEKFTSsckSKIKNNSFIPG--KGSQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 562 LKdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepvdriig 641
Cdd:cd14886 469 CN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD--------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 642 ldqvagmsetaLPGAFKTRKGMFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 721
Cdd:cd14886 518 -----------IPNEDGNMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFES 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 722 IRICRQGFPNRVVFQEFRQRYEILT--PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14886 585 IQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
95-742 |
4.96e-105 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 354.02 E-value: 4.96e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 164 DREDQSILCTGESGAGKTENTKKVIQYLA------------YVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 232 SSRFGKFIRINF-DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-----AGEHLKTDLLLEPYNKYRFLSN 305
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 306 GHVTI--PGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-----KKERNT--DQASMPDNTAA----- 371
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 372 QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------------- 437
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 438 DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEK 517
Cdd:cd14899 401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 518 PagPPGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 594
Cdd:cd14899 480 R--PIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 595 NIATLLHQSSDKFVSELWKDEMQSTQRAYfyhrfpilhlEPVDRIIGLDQVAGMSETALPgafktrkgmfrTVGQLYKEQ 674
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSNDEDANGD----------SELDGFGGRTRRRAKSAIAAV-----------SVGTQFKIQ 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 675 LAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 742
Cdd:cd14899 617 LNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
95-785 |
1.69e-98 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 335.46 E-value: 1.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYS--------GLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 167 DQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 246
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG-LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvtiPGQQDKDMF--QETME 324
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDPESTdlRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 325 AMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTA--------AQKVSHLL-------GINVTDFTRGI 389
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 390 LT--------PRIKVGRDYV------------QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR------- 442
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 443 ------QGASFIGILDIAGFEIF---DLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQPC 511
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 512 IDLIEKPA---------------------GPPGILALLDE------ECWFPKATDKSFVEKVMQEQGTHPKFQK--PKQL 562
Cdd:cd14887 463 STLTSSPSstspfsptpsfrsssafatspSLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvselwkdemqstqraYFYhrfpilhlepvdRIIGL 642
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACS------------------TYT------------RLVGS 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 643 DQVAGMSetalpgAFKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 722
Cdd:cd14887 593 KKNSGVR------AISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLL 663
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 723 RICRQGFPNRVVFQEFRQRYEILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 785
Cdd:cd14887 664 RVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
92-784 |
1.27e-94 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 321.42 E-value: 1.27e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 92 LNEASVLHNLKERYYSGLIYTY---SGLfcVVINPYKNLPIYSEEIVEMYK-------GKKRHEMPPHIYAITDTAYRSM 161
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 162 MQDREDQSILCTGESGAGKTENTKKVI-QYLAYVASSHKSKKdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK----LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVT--IPGQQDK 316
Cdd:cd14879 155 LQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHPLplGPGSDDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 317 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF--KKERNTDQASMpDNTAA-QKVSHLLGINVTDFtRGILTPR 393
Cdd:cd14879 235 EGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSLTYK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 394 IK-VGRD----YVQKAQTKEQADfaieALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFD---LNSFE 465
Cdd:cd14879 313 TKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRSstgGNSLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 466 QLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIEKPAGppGILALLDEEC-WFPKATD 539
Cdd:cd14879 389 QFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGKPG--GLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 540 KSFVEKVMQEQGTHPKF---QKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLndniatllhqSSDkFVSelwkdem 616
Cdd:cd14879 461 EQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 617 qstqrayfyhrfpilhlepvdriigldqvagmsetalpgafktrkgMFRTVGQLyKEQLAKLMATLRNTNPNFVRCIIPN 696
Cdd:cd14879 523 ----------------------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 697 HEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgFMDGKQACVLMIKALELDSNLYR 776
Cdd:cd14879 556 DSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYV 629
|
....*...
gi 2550219468 777 IGQSKVFF 784
Cdd:cd14879 630 LGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
96-747 |
3.45e-94 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 317.99 E-value: 3.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNlpIYSEEIVEMYKGKKRHeMPPHIYAITDTAYRSMMQdREDQSILCTGE 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvnGYIVGANIE 255
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDlllepYNKYRF-LSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSEKYKMTCSAMKSLGIANFKSI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 335 EQMGLlrvisGVLQLGNIVFKKERNTDQASmpdNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14898 225 EDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 415 EALAKATYERMFRWLVLRINKALDKTkrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 495 EGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKvMQEQGTHpkfqkpkQLKDKADFCII--H 572
Cdd:cd14898 374 EGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVK-IKKYLNG-------FINTKARDKIKvsH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 573 YAGKVDYKADEWLMKNMDPLNDNIatllhqssdkFVSELWKDEmqstqrayfyhrfpilhlepvdriigldqvagmseta 652
Cdd:cd14898 442 YAGDVEYDLRDFLDKNREKGQLLI----------FKNLLINDE------------------------------------- 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 653 lpgafktrkGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 732
Cdd:cd14898 475 ---------GSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQE 545
|
650
....*....|....*
gi 2550219468 733 VVFQEFRQRYEILTP 747
Cdd:cd14898 546 IPKDRFEERYRILGI 560
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
95-785 |
8.85e-93 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 315.80 E-value: 8.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEivemYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYlaYVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14937 77 ESGSGKTEASKLVIKY--YLSGV----KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd14937 151 EIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMHDM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 335 EQmGLLRVISGVLQLGNIVFK---KERNTDQASMPDNT--AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd14937 231 KD-DLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 410 ADFAIEALAKATYERMFRWLVLRINKALDKTKrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14937 310 SVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKET 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 490 EEYQREGIEWNFIDFGLDlQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKaDFC 569
Cdd:cd14937 389 ELYKAEDILIESVKYTTN-ESIIDLLR---GKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK-NFV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDemqstqrayfyhrfpilhlepvdriigldqvAGMS 649
Cdd:cd14937 464 IKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-------------------------------VEVS 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 650 ETAlpgafkTRKGMfrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIcRQGF 729
Cdd:cd14937 513 ESL------GRKNL---ITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFF 582
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 730 PNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKAlELDSNLYRIGQSKVFFR 785
Cdd:cd14937 583 QYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
95-785 |
4.76e-91 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 311.36 E-value: 4.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 172 CTGESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 250
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-----FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH----VTIPGQQDKDMFQETMEAM 326
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 407 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14878 316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 484 MFILEQEEYQREGIEWNFIDFGLDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKP 559
Cdd:cd14878 396 LFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPS---GFLSLLDEESQMIWSVEPNLPKKLqslLESSNTNAVYSPM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 560 KQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQstqrayfyhrfpilh 632
Cdd:cd14878 473 KDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLV--------------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 633 lepvdriigldqvagmsetalpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQ 712
Cdd:cd14878 538 ---------------------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQ 584
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 713 LRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 785
Cdd:cd14878 585 LQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
95-737 |
4.37e-79 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 277.17 E-value: 4.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHE-------MPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 167 DQSILCTGESGAGKTENTKKVIQYLAYVasshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-- 244
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEev 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 245 -------VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSN----------G 306
Cdd:cd14884 157 entqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPdeshqkrsvkG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 307 HVTIPG----------QQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKkerntdqasmpdntaaqKVSH 376
Cdd:cd14884 237 TLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------AAAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 377 LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA----------- 445
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysine 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 446 SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKpagppgIL 525
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK------IF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 526 ALLDE-----ECWFPKATDKSFV-----EKVMQEQGTH------PKFQK---PKQLKDKADFCIIHYAGKVDYKADEWLM 586
Cdd:cd14884 453 RRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINNWID 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 587 KNMDPLNDNIATLLHQSSDKFVSElwkdemqstqrayfyhrfpilhlepvdriigldqvagmsetalpGAFKTRKGMFRT 666
Cdd:cd14884 533 KNSDKIETSIETLISCSSNRFLRE--------------------------------------------ANNGGNKGNFLS 568
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 667 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 737
Cdd:cd14884 569 VSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
96-771 |
5.95e-79 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 275.07 E-value: 5.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYknlpiyseeiveMYKGKKRH-------EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 169 SILCTGESGAGKTENTKKVIQYLAYVASshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFd 244
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQET 322
Cdd:cd14881 141 TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 323 MEAMRIMGIPeeeQMGLLRVISGVLQLGNIVFKkERNTDQASMPDNTAAQKVSHLLGINVTDFTRGiLTPRIK-VGRDYV 401
Cdd:cd14881 221 KACLGILGIP---FLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKaldkTKRQGAS--------FIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14881 296 KSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 474 EKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIEkpAGPPGILALLDEECwFPKATDKSFVEKVMQEQGT 552
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 553 HPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdemqstqrayfyhrfpilh 632
Cdd:cd14881 448 NPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 633 lepvdriigldqvagmsetalpgAFKTRKGMFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQ 712
Cdd:cd14881 502 -----------------------GFATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQ 551
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 713 LRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQAC--VLMIKALELD 771
Cdd:cd14881 552 IRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQP 612
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
96-738 |
3.19e-69 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 247.70 E-value: 3.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASShKSKKdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLS-RSKY----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 334 EEQMGLLRVISGVLQLGNIVFKKERNtdQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAqtkeqadfa 413
Cdd:cd14905 235 EKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 414 iEALAKATYERMFRWLVLRINKALDKTkrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQ 493
Cdd:cd14905 304 -DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 494 REGIEW-NFIDFGlDLQPCIDLIEKpagppgILALLDEECWFPKATDKSFVEKVMQEQGTHPKF-QKPKQlkdkadFCII 571
Cdd:cd14905 381 TERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------FGIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKF-------------VSELwkDEMQSTQRAYFYHRFPILHLEPVDR 638
Cdd:cd14905 448 HYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAEL--NQMFDAKNTAKKSPLSIVKVLLSCG 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 639 IIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPN--FVRCIIPNHEKKAGKLDPHLVLDQLRCN 716
Cdd:cd14905 526 SNNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIKSL 605
|
650 660
....*....|....*....|....*.
gi 2550219468 717 GVLEGIRICRQGFP----NRVVFQEF 738
Cdd:cd14905 606 CLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
95-750 |
3.49e-68 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 243.62 E-value: 3.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYkgkkrhemppHIYAITDTAYRSMMQDRED-QSILCT 173
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDVNgYIVGAN 253
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 254 IE-TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14874 143 LKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 333 EEEQMGLLRVISGVLQLGNIVFKKERNTD---QASMPDNTAAQK-VSHLLGINVTDFTRgILTPRIKVGrdyvqKAQTKE 408
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLVN-FLLPKSEDG-----TTIDLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 489 QEEYQREGIEWNF-IDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlKDKAD 567
Cdd:cd14874 375 LVDYAKDGISVDYkVPNSIENGKTVELLFKK--PYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KERLE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTQrayfyhrfpilhlepvDRIIgldqvag 647
Cdd:cd14874 452 FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTS----------------DMIV------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 648 msetalpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQ 727
Cdd:cd14874 509 ------------------SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIK 570
|
650 660
....*....|....*....|...
gi 2550219468 728 GFPNRVVFQEFRQRYEILTPNSI 750
Cdd:cd14874 571 GYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
98-743 |
1.03e-65 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 239.10 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 98 LHNLKERYYSGLIYTYSGLFCVVINPYKNLPIY----------SEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRED 167
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 168 QSILCTGESGAGKTENTKKVIQYLAYVASS----HKSKKDQGELE---RQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAgEH---LKTDLLL-EPYNKYRFLSN-----GHVTIP 311
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadplaTNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 312 GQQDKDMfqetMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-------KKERNTDQASMPDNTA------AQ--KVSH 376
Cdd:cd14893 243 ARDYRDL----MSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 377 LLGIN--VTD---FTRGILTpriKVGRDYVQ--KAQTKEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKR--- 442
Cdd:cd14893 319 LLEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKsni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 443 ----QGasfIGILDIAGFEIFD--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQ 509
Cdd:cd14893 396 vinsQG---VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 510 PCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAD------------FCIIHYAGKV 577
Cdd:cd14893 473 KCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 578 DYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEMQSTQRAyfyhrfpilhlepvdriigldqvAGMSETALPGAF 657
Cdd:cd14893 551 TYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSE-----------------------KAAKQTEERGST 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 658 --KTRKGMFR----------TVGQLYKEQLAKLMAtLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIC 725
Cdd:cd14893 608 ssKFRKSASSaresknitdsAATDVYNQADALLHA-LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQAS 686
|
730
....*....|....*...
gi 2550219468 726 RQGFPNRVVFQEFRQRYE 743
Cdd:cd14893 687 RSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
96-785 |
1.68e-65 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 235.79 E-value: 1.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 176 SGAGKTENTKKVIQYLAYVAsshksKKDQGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-----DGNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG--AGEHLKtDLLLEPYNKYRFLSNGHVTIPG---------QQDKDMFQETME 324
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSklkyrrddpEGNVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 325 AMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKerNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqgASF-----IGILDIAGFEIFDLNSFEQLCINYTNEKLQQL 479
Cdd:cd14882 313 HTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 480 FNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciDLIEKPAgppGILALLDEECwfPKATDKSFV-EKVMQEQGTHPK 555
Cdd:cd14882 390 YNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYImDRIKEKHSQFVK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 556 fqkpkqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDEmqstqrayfyhrfpilhlep 635
Cdd:cd14882 462 ------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNS-------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 636 vdriigldQVAGMsetalpgafKTRKGMFRTVGQlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 715
Cdd:cd14882 516 --------QVRNM---------RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRA 575
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 716 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 785
Cdd:cd14882 576 LAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
117-248 |
8.80e-59 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 200.26 E-value: 8.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 117 FCVVINPYKNLPIYSEEIV-EMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVA 195
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 196 SSHKSKKD----------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd01363 81 FNGINKGEtegwvylteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-783 |
5.57e-56 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 209.31 E-value: 5.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK-GKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 175 ESGAGKTENTKKVIQYLAYVASSHKS------------------KKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRlptnlndqeednihneenTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 237 KFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 317 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNI-----VFKKE---------------------RNTDQASMPDNTA 370
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 371 AQKV-SHLLGINVTDFTRGILTPRIkVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR--QGASF 447
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 448 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgpPGILAL 527
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPT--EGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 528 LDEECWFPKATDKS-FVEKVMQEQGTHPKFQKPKQLK-DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 605
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 606 KFvselwkdeMQSTQRAYFYhrfpilhlepvdriiglDQVAGMSET----ALPGAFKTRKGMFRTVGQ----LYKEQLAK 677
Cdd:cd14938 558 EY--------MRQFCMFYNY-----------------DNSGNIVEEkrrySIQSALKLFKRRYDTKNQmavsLLRNNLTE 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 678 LMATLRNTNPNFVRCIIPNHEKKA-GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgfmD 756
Cdd:cd14938 613 LEKLQETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------D 684
|
730 740
....*....|....*....|....*..
gi 2550219468 757 GKQACVLMIKALELDSNLYRIGQSKVF 783
Cdd:cd14938 685 LKEKVEALIKSYQISNYEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
954-1851 |
8.41e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 142.89 E-value: 8.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 954 HLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1033
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEELRE-----ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1034 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARV 1113
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE-------AQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1114 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtlDSTAAQQELRSKREQEvniL 1193
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQQEIEEL---L 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1194 KKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnevkvllqgkgdSEHKRKKVEA 1273
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA------------QLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1274 QLQELQVKFNEGERvrteladKVTKLQVELDNVTGLLSQSDSKSSKLTKdfsALESQLQDT-QELLQEENRQKLSLSTKL 1352
Cdd:TIGR02168 496 RLQENLEGFSEGVK-------ALLKNQSGLSGILGVLSELISVDEGYEA---AIEAALGGRlQAVVVENLNAAKKAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1353 KQVEDEKNSFREQLEEEEeakhnlekqiATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLE--------------GL 1418
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKG----------TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldnAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1419 SQRHEEK-----VAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR 1493
Cdd:TIGR02168 636 ELAKKLRpgyriVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1494 EKETKALSLARALEEAMEQKAELERlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATE 1573
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEA-------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1574 DAKLRLEVNLQAMKAQFeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKN 1653
Cdd:TIGR02168 789 AQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1654 RDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN 1733
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1734 ssgKGALALEEKRRLEARIAqleeeleeeqGNTELINDRLKKANLQIDQINTdlnlershaqKNENARQQLERQNKELKV 1813
Cdd:TIGR02168 948 ---EYSLTLEEAEALENKIE----------DDEEEARRRLKRLENKIKELGP----------VNLAAIEEYEELKERYDF 1004
|
890 900 910
....*....|....*....|....*....|....*...
gi 2550219468 1814 KLQEMEGTVKSKYKasitaLEAKIaqleEQLDNETKER 1851
Cdd:TIGR02168 1005 LTAQKEDLTEAKET-----LEEAI----EEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
879-1637 |
2.02e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 138.27 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 879 REKQLA-AENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAE----ELRARLTAKKQELEEICHDLEA---RVEEEEE 950
Cdd:TIGR02168 223 RELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEELQKELYAlanEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 951 RCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLT 1030
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1031 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLsdQIAELQAQIAELKMQLAKKEEELQAAL 1110
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1111 ARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEAlKTELEDTLDSTAAQQELRSKREQEV 1190
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLSGILGVLSELISVDEGYEAAI 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1191 NI-----LKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSE 1265
Cdd:TIGR02168 540 EAalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1266 HKRKKV-----EAQLQELQVKFNEGERVRTELADKVTK-----------------LQVELDNVTGLLSQSDSKSSKLTKD 1323
Cdd:TIGR02168 620 YLLGGVlvvddLDNALELAKKLRPGYRIVTLDGDLVRPggvitggsaktnssileRRREIEELEEKIEELEEKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1324 FSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLET 1403
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1404 AEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDldhQRQSACNLEKKQKKFDQLLAEEKTISakyaE 1483
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELS----E 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1484 ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLE 1563
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1564 ELEDELQATEDaKLRLEVNLQAMKA-QFERDLQGRDEQSEEKKKQLVRQVREM---------EAELEDER-----KQRSM 1628
Cdd:TIGR02168 933 GLEVRIDNLQE-RLSEEYSLTLEEAeALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieEYEELKERydfltAQKED 1011
|
....*....
gi 2550219468 1629 AVAARKKLE 1637
Cdd:TIGR02168 1012 LTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1056-1900 |
2.78e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 134.80 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1056 RLRREEKQRQeLEKTRRKLEgdstDLSDQIAELQAQIAELKMQlAKKEEELQAAlaRVEEEAAQKNMALKKIRELESQIS 1135
Cdd:TIGR02168 171 KERRKETERK-LERTRENLD----RLEDILNELERQLKSLERQ-AEKAERYKEL--KAELRELELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1136 ELQEDLESERASRNKAEKQKRDLGEELEALKTEL-EDTLDSTAAQQELrskreQEVNILKKTLEEEAKTHEAQIQEMRQK 1214
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKEL-----YALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1215 hsqaVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVkvllqgkgdsehkrkkveaqlQELQVKFNEGERVRTELAD 1294
Cdd:TIGR02168 318 ----LEELEAQLEELESKLDELAEELAELEEKLEELKEEL---------------------ESLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1295 KVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLkqVEDEKNSFREQLEEEEEAKH 1374
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1375 NLEKQIATLHAQvadmkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQR 1454
Cdd:TIGR02168 451 ELQEELERLEEA--------------LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1455 QSACNLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKA---ELERLNKQF--RTEMED 1529
Cdd:TIGR02168 517 GLSGILGVLS---ELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTEiqGNDREI 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1530 LMSSKDDVGkSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAK-LRLEVNLQAMK--------------AQFERDL 1594
Cdd:TIGR02168 594 LKNIEGFLG-VAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKkLRPGYRIVTLDgdlvrpggvitggsAKTNSSI 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1595 QGRD---EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDC 1671
Cdd:TIGR02168 673 LERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1672 MRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR 1751
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1752 IAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKAsIT 1831
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK-RS 911
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1832 ALEAKIAQLEEQLdNETKERQAACKQVRRT--EKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1900
Cdd:TIGR02168 912 ELRRELEELREKL-AQLELRLEGLEVRIDNlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1012-1872 |
2.52e-30 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 131.34 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1012 AKEKKLLEDRIA---EFttnlteEEEKSKSLAKLK------NKHEAMITDLEERLRREEKQRQELEK----TRRKLEGDS 1078
Cdd:TIGR02169 152 PVERRKIIDEIAgvaEF------DRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1079 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQED-----------LESERAS 1147
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekigeLEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1148 RNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKhsqaVEELAEQLE 1227
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE----LEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1228 QTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELdnvt 1307
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL---- 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1308 gllsqsdsksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQV 1387
Cdd:TIGR02169 458 ----------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1388 ADMKKKMEDSVGCLETAeeVKRKLQK---DLEGLSQR-----HEEKVAAYDKLEKTKTRlQQELDDLLVDLDHQRQSACN 1459
Cdd:TIGR02169 528 AQLGSVGERYATAIEVA--AGNRLNNvvvEDDAVAKEaiellKRRKAGRATFLPLNKMR-DERRDLSILSEDGVIGFAVD 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1460 LEKKQKKF---------DQLLAE----------------------------------EKTISAKYAEERDRAEAEAREKE 1496
Cdd:TIGR02169 605 LVEFDPKYepafkyvfgDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1497 tkalSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAK 1576
Cdd:TIGR02169 685 ----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1577 LRLEVNLQAMKAQFErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDE 1656
Cdd:TIGR02169 761 KELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1657 AIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIanssg 1736
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI----- 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1737 kgalaleekRRLEARIAQLEEELEEEQGNTELInDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKElkvKLQ 1816
Cdd:TIGR02169 913 ---------EKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNML---AIQ 979
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1817 EMEGTVKskykasitaleaKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQV 1872
Cdd:TIGR02169 980 EYEEVLK------------RLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
991-1575 |
2.81e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 127.75 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 991 EAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1070
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1071 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNK 1150
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1151 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvnilkktlEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK 1230
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1231 RVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKfnEGERVRTELADKVTKLQVELDNVTGLL 1310
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR--GLAGAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1311 SQ----SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQ 1386
Cdd:COG1196 548 LQnivvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1387 VADmkkKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAcnlekkQKK 1466
Cdd:COG1196 628 VAA---RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL------EEA 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1467 FDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskDDVGKSVHELEK 1546
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL----EELERELERLER 774
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2550219468 1547 SKRAL--------------EQQVEEMKTQLEELEDELQATEDA 1575
Cdd:COG1196 775 EIEALgpvnllaieeyeelEERYDFLSEQREDLEEARETLEEA 817
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
980-1731 |
7.93e-28 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 123.25 E-value: 7.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 980 RQKLQLEKVTTEaKLKKLEEEQIILEDQncKLAKEKKLLEDRIAEFTTNLTEEEEkskSLAKLknkhEAMITDLEERL-R 1058
Cdd:TIGR02169 200 LERLRREREKAE-RYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEE---ELEKL----TEEISELEKRLeE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1059 REEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQknmalkkIRELESQISELQ 1138
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1139 EDLESERasrnkaeKQKRDLGEELEALKTELEDtldstaaqqelrskreqevniLKKTLEEEAKTHeaqiQEMRQKHSQA 1218
Cdd:TIGR02169 343 REIEEER-------KRRDKLTEEYAELKEELED---------------------LRAELEEVDKEF----AETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1219 VEELAEqleqtkrvkanlekakqtLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1298
Cdd:TIGR02169 391 REKLEK------------------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1299 LQVELdnvtgllsqsdsksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEK 1378
Cdd:TIGR02169 453 QEWKL--------------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1379 QIATLHAQVADMKKKMEDSVGCLETAeeVKRKLQK---DLEGLSQR-----HEEKVAAYDKLEKTKTRlQQELDDLLVDL 1450
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERYATAIEVA--AGNRLNNvvvEDDAVAKEaiellKRRKAGRATFLPLNKMR-DERRDLSILSE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1451 DHQRQSACNLEKKQKKF---------DQLLAE----------------------------------EKTISAKYAEERDR 1487
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYepafkyvfgDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1488 AEAEAREKEtkalSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELED 1567
Cdd:TIGR02169 676 LQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1568 ELQATEDAKLRLEVNLQAMKAQFErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHI 1647
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1648 DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL 1727
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
....
gi 2550219468 1728 ADEI 1731
Cdd:TIGR02169 909 EAQI 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
877-1720 |
1.86e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 115.55 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 877 KVREKQLAAENRLTEMETLqsqlMAEKLQLQEQLQAETElcaEAEELRArLTAKKQELE--EICHDLEARVEEEEERCQH 954
Cdd:TIGR02169 174 KALEELEEVEENIERLDLI----IDEKRQQLERLRRERE---KAERYQA-LLKEKREYEgyELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 955 LQAEKKKMQQNIQELEEQLEEEESARQKLQlekvTTEAKLKKL-EEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1033
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLE----ELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1034 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARV 1113
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1114 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNIL 1193
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1194 KKTLEE-----EAKTHEAQIQEMRQKHSQAVEELAE--------QLEQTKRVKANLEKAkqtLENERGELANEVKVllqg 1260
Cdd:TIGR02169 482 EKELSKlqrelAEAEAQARASEERVRGGRAVEEVLKasiqgvhgTVAQLGSVGERYATA---IEVAAGNRLNNVVV---- 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1261 KGDSEHKR-----KKVEA------QLQELQVKFNEGERVRTELADKVTKLQVELDNV-----------TGLLSQSDSKSS 1318
Cdd:TIGR02169 555 EDDAVAKEaiellKRRKAgratflPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARR 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1319 KLTK-DFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEeeeakhnLEKQIATLHAQVADMKKKMEDS 1397
Cdd:TIGR02169 635 LMGKyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1398 VGCLETAEEVKRKLQKDLEGLSQRHEekvAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTI 1477
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEE---KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1478 SAKYAEER--------DRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKR 1549
Cdd:TIGR02169 785 EARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1550 ALEQQVEEMKTQLEELEDELQatedaklrlevnlqamkaqferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMA 1629
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1630 VAARKKLEMDLKDLEAHIdSANKNRDEAIKQLRKLQAQMKDCMRELDD-----TRASR--EEILAQAKENEKKLKSMEAE 1702
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnMLAIQeyEEVLKRLDELKEKRAKLEEE 1001
|
890
....*....|....*...
gi 2550219468 1703 MIQLQEELAAAERAKRQA 1720
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1223-1944 |
6.37e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.00 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1223 AEQLEQTKRVKANLEKAKQTLE-NERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQV 1301
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1302 ELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEeeeeakhNLEKQIA 1381
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------SLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1382 TLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSACNLE 1461
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1462 KKqkKFDQLLAEEKTISAKYAEERDRAEAEareKETKALSLARALEEAMEQKAELERLNKQFRTeMEDLMSSKDDVGKSV 1541
Cdd:TIGR02168 435 LK--ELQAELEELEEELEELQEELERLEEA---LEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1542 HELEKSKRALEQQVEEMKTQLE-----ELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRD------EQSEEKKKQLVR 1610
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISvdegyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1611 QVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANkNRDEAIKQLRKLQAQMKdcMRELDDTRASREEILAQA- 1689
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1690 --------------KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQL 1755
Cdd:TIGR02168 666 aktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1756 EEELeeeqgntELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKyKASITALEA 1835
Cdd:TIGR02168 746 EERI-------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1836 KIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRR 1915
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
730 740
....*....|....*....|....*....
gi 2550219468 1916 KLQRELedatetadamnREVSSLKNKLRR 1944
Cdd:TIGR02168 898 ELSEEL-----------RELESKRSELRR 915
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1103-1931 |
1.91e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.08 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1103 EEELQAALARVEEeaaqknmALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeleALKTELEDTlDSTAAQQEL 1182
Cdd:TIGR02169 169 DRKKEKALEELEE-------VEENIERLDLIIDEKRQQLERLRREREKAERYQ--------ALLKEKREY-EGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1183 RSKREQEVNILKK--TLEEEAKTHEAQIQEMRQKHSQAVEELAEQleqTKRVKANLEKAKQTLENERGELANEVKVLLQG 1260
Cdd:TIGR02169 233 EALERQKEAIERQlaSLEEELEKLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRVKEKIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1261 KGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdSKSSKLTKDFSALESQLQDTQELLQE 1340
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT-------EEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1341 ENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK-------MEDSVGCLETAEEVKRKLQK 1413
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeeKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1414 DLEGLSQRHEEKVAAYDKLEKTKTRLQQElddllvdldhqrqsacnlekkqkkfdqLLAEEKTISAKYAEERDRAEAEar 1493
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRE---------------------------LAEAEAQARASEERVRGGRAVE-- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1494 eketkaLSLARALEEAMEQKAELERLNKQFRTEMEDLMSSK--------DDVGKSVHELEKSK---RALEQQVEEMKTQL 1562
Cdd:TIGR02169 514 ------EVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRlnnvvvedDAVAKEAIELLKRRkagRATFLPLNKMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1563 EELEdelQATEDAKLRLEVNLQAMKAQFERDLQG--RDE---QSEEKKKQLVRQVR--EMEAELED-----------ERK 1624
Cdd:TIGR02169 588 RDLS---ILSEDGVIGFAVDLVEFDPKYEPAFKYvfGDTlvvEDIEAARRLMGKYRmvTLEGELFEksgamtggsraPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1625 QRSMAVAARKKLEM---DLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1701
Cdd:TIGR02169 665 GILFSRSEPAELQRlreRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1702 EMIQLQEELAAAErakrqaqQERDELADEIANSSGKGALALEEKRRLEARIAQleEELEEEQGNTELINDRLKKANLQID 1781
Cdd:TIGR02169 745 DLSSLEQEIENVK-------SELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLR 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1782 QINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTV------KSKYKASITALEAKIAQLEEQLDNETKERQAAC 1855
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1856 KQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQrANASRRKLQRELEDATETADAM 1931
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEEIRAL 970
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
101-726 |
2.83e-24 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 111.37 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 101 LKERYYSGLIYTYSGLFCV-VINPYKNL------PIYSEEIVEMYKGKKRHE--MPPHIYAI------------------ 153
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 154 --TDTAYRSMMQDReDQSILCTGESGAGKTENTKKVIQYLAYVA---------------------------SSHKS---- 200
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftSSTKStiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 201 ---------------------------------------------------------KKDQGELERQL------------ 211
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeKLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 212 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVNGY---IVGANIETYLLEKSRAIRQA------KEERTFHI 276
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 277 FYYLLSGAGEH-----LKTDLLLEPYN--KYRFLSNGHVTIPG--------QQDKDMFQETMEAMRIMGIPEEEQMGLLR 341
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 342 VISGVLQLGNIVFKKERNTDQASMPDN---TAAQKVSHLLGI-NVTDFTRGILTPRIKV--GRDYVQKAQTKEQADFAIE 415
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 416 ALAKATYERMFRWLVLRINKAL-------DKTKRQ---------GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLqql 479
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 480 fnhtmfileqeeYQREGiewNFIDFGLDLQPCI-------DLIEKPAGPPGILALLDEECWFPKAT----------DKSF 542
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRPHLtardsekDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLF 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 543 VEKVMQEQGThpKFQKPKQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL 611
Cdd:cd14894 628 VRNIYDRNSS--RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRM 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 612 WKDEMQ-----STQRAYFyhrfpilhlepvdriigldqvaGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMatlrntn 686
Cdd:cd14894 706 LNESSQlgwspNTNRSML----------------------GSAESRLSGT-KSFVGQFRSHVNVLTSQDDKNM------- 755
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 2550219468 687 PNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICR 726
Cdd:cd14894 756 PFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1323-1946 |
2.25e-23 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 108.72 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1323 DFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLE 1402
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1403 TAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELddllvdldhqrqsaCNLEKKQKKFDQLLAeektisaKYA 1482
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEK--------------VTTEAKIKKLEEDIL-------LLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1483 EERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1562
Cdd:pfam01576 145 DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1563 EELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLK- 1641
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEa 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1642 ---DLEAHIDSANKNRDEAIKQLRKLqAQMKDCMREldDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKR 1718
Cdd:pfam01576 304 lktELEDTLDTTAAQQELRSKREQEV-TELKKALEE--ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1719 QAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNE 1798
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1799 NARQQLERQNKELKVKLQEmEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRN 1878
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1879 AEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGD 1946
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFD 607
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1058-1633 |
8.34e-22 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 103.20 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1058 RREEKQRQELEKTRRKLEG-DSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEA---AQKNMALKKIRELESQ 1133
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1134 ISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTaaqqELRSKREQEVNILKKTLEEEakthEAQIQEMRQ 1213
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDR----DEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1214 KHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA 1293
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1294 DKVTKLQVELDNVTGllsqsdsKSSKLTKDFSALESQLQDTQELLQE----ENRQKLSLSTKLKQVEDEknsfREQLEEe 1369
Cdd:PRK02224 412 DFLEELREERDELRE-------REAELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVETIEED----RERVEE- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1370 eeakhnLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKdLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVD 1449
Cdd:PRK02224 480 ------LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER-REDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1450 LDHQRQSAcnlEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKAL--SLARALEEAMEQKAELERLNKQFRTEM 1527
Cdd:PRK02224 553 AEEKREAA---AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiaDAEDEIERLREKREALAELNDERRERL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1528 EDLMSSKDDVGKSVHEleKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER--DLQGRDEQSEEKK 1605
Cdd:PRK02224 630 AEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEleELRERREALENRV 707
|
570 580 590
....*....|....*....|....*....|....
gi 2550219468 1606 KQL------VRQVREMEAELEDERKQRSMAVAAR 1633
Cdd:PRK02224 708 EALealydeAEELESMYGDLRAELRQRNVETLER 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1401-1944 |
8.57e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 8.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1401 LETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAK 1480
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1481 YAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1560
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1561 QLEELEDELQATEDAKLRLEVNLQAmkaqferdLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDL 1640
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEE--------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1641 KDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKK--LKSMEAEMIQLQEELAAAERAKR 1718
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvlIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1719 QAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGN-TELINDRLKKANLQIDQINTDLNLERSHAQKN 1797
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAaVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1798 ENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQldnetKERQAACKQVRRTEKKLKDVLLQVDDERR 1877
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE-----AELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1878 NAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET----ADAMNREVSSLKNKLRR 1944
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
880-1738 |
1.23e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 103.30 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 880 EKQLAAENRLTEMETlqsqlmAEKLQLQEQLQAETELCAEAEELRARLTAKKQEleeichdlEARVEEEEERCQHLQAEK 959
Cdd:PTZ00121 1096 AFGKAEEAKKTETGK------AEEARKAEEAKKKAEDARKAEEARKAEDARKAE--------EARKAEDAKRVEIARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 960 KKMQQNIQELEEQLEEEESARQKLQLEKVTteaKLKKLEEEQIILEDQncKLAKEKKLLEDRIAEfttnlteEEEKSKSL 1039
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAE---ELRKAEDARKAEAAR--KAEEERKAEEARKAE-------DAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1040 AKLKnkheamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIaelKMQLAKKEEELQAALARVEEEAAQ 1119
Cdd:PTZ00121 1230 KKAE----------EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKAEEKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1120 KNMALKKIRELESQISELQEDLESER----------ASRNKAEKQKRD---LGEELEALKTELEDTLDSTAAQQELRSKR 1186
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKkaeeakkkadAAKKKAEEAKKAaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1187 EQEVNILKKTLEEEAKTHEAqiqemrQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGelANEVKVLLQGKGDSEH 1266
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEA------KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1267 KRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDfsalESQLQDTQELLQEENRQKl 1346
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA----AEAKKKADEAKKAEEAKK- 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1347 slSTKLKQVEDEKNSFR----EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRH 1422
Cdd:PTZ00121 1524 --ADEAKKAEEAKKADEakkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1423 EE----KVAAYDKLEKTKTRlQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKE-- 1496
Cdd:PTZ00121 1602 EEekkmKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEea 1680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1497 TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKS-------VHELEKSKRALEQQVEEMKTQLEELEDEL 1569
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1570 QATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKklEMDLKDLEAHIDS 1649
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADS 1838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1650 ANKNRDEAikqlrklqaqmkdcmrelDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELAD 1729
Cdd:PTZ00121 1839 KNMQLEEA------------------DAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER 1900
|
....*....
gi 2550219468 1730 EIANSSGKG 1738
Cdd:PTZ00121 1901 EIPNNNMAG 1909
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1219-1819 |
1.44e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1219 VEELAEQLEQTKRVKAnLEKAKQTLENErgELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1298
Cdd:COG1196 202 LEPLERQAEKAERYRE-LKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1299 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEK 1378
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1379 QIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAC 1458
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1459 NLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELErlnkqfrtEMEDLMSSKDDVG 1538
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL--------EAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1539 KSVHELEKSKRaLEQQVEEMKTQLEELEDELQATEDAKLRLEVNlqamkaqfERDLQGRDEQSEEKKKQLVRQVREMEAE 1618
Cdd:COG1196 511 KAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1619 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKS 1698
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1699 MEAEmiQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANL 1778
Cdd:COG1196 662 LTGG--SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2550219468 1779 QIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEME 1819
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
877-1441 |
3.60e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 877 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQ 956
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 957 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKS 1036
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1037 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1116
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1117 AAQKNMALKKIRELESQISELQEDLESERASRN---------KAEKQKRDLGEELEALKTEL--EDTLDSTAAQQELRSK 1185
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligVEAAYEAALEAALAAALQNIvvEDDEVAAAAIEYLKAA 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1186 REQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSE 1265
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1266 HKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDfsALESQLQDTQELLQEENRQK 1345
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER--ELAEAEEERLEEELEEEALE 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1346 LSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDsvgcLET----AEEvkrklqkDLEGLSQR 1421
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA----LGPvnllAIE-------EYEELEER 796
|
570 580
....*....|....*....|
gi 2550219468 1422 HEEKVAAYDKLEKTKTRLQQ 1441
Cdd:COG1196 797 YDFLSEQREDLEEARETLEE 816
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
877-1612 |
7.06e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.45 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 877 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQ 956
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 957 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKS 1036
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1037 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA---ELKMQLAKKEEELQAALarv 1113
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGSVGERYATAI--- 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1114 eeEAAQKNMALKKIRELESQISELQEDLESERASR------NKAEKQKRDLGEELE-------------------ALKTE 1168
Cdd:TIGR02169 542 --EVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRatflplNKMRDERRDLSILSEdgvigfavdlvefdpkyepAFKYV 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1169 LEDTLdstaAQQELRSKREQEVNILKKTLEEEAKTHEAQI----QEMRQKHSQAVEELAEQLEQTKRVKAnLEKAKQTLE 1244
Cdd:TIGR02169 620 FGDTL----VVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggsRAPRGGILFSRSEPAELQRLRERLEG-LKRELSSLQ 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1245 NERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDF 1324
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1325 SALESQLQDTQELLQEEnrqklslstKLKQVEDEKNSfreqleeeeeakhnLEKQIATLHAQVADMKKKMEDSVGCLETA 1404
Cdd:TIGR02169 775 HKLEEALNDLEARLSHS---------RIPEIQAELSK--------------LEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1405 EEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKtisakyaEE 1484
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE-------RK 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1485 RDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkDDVGKSVHELEKSKRALE-------QQVEE 1557
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEpvnmlaiQEYEE 983
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1558 MKTQLEELEDELqatedAKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLVRQV 1612
Cdd:TIGR02169 984 VLKRLDELKEKR-----AKLEEE----------RKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
995-1887 |
1.41e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 96.19 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 995 KKLEEEQIILEDQNCKLAKEKKLLE--DRIAEFTTNLTEEEEKSKSLAKLKNKheamitdleERLRREEKQRQELEKTRR 1072
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEetENLAELIIDLEELKLQELKLKEQAKK---------ALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1073 KLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAE 1152
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1153 KQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvnilKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRV 1232
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE----LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1233 KANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQ 1312
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1313 SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKK 1392
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1393 KMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLA 1472
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1473 EEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDvgKSVHELEKSKRALE 1552
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAE--SELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1553 QQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAA 1632
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1633 RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQ-----MKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQ 1707
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAElleeeQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1708 EELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDL 1787
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1788 NLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKD 1867
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
890 900
....*....|....*....|
gi 2550219468 1868 VLLQVDDERRNAEQYKDQAD 1887
Cdd:pfam02463 1021 EFLELFVSINKGWNKVFFYL 1040
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1101-1731 |
3.68e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 94.75 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1101 KKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtLDSTAAQQ 1180
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1181 ELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKAnLEKAKQTLENERGELANEVKVLLQG 1260
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKE----IEELEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1261 KGDSEHKRKKVEAQLQELQVKFNEGErvrtELADKVTKLQVELDNVtgllsqsdSKSSKLTKDFSALESQLQDTQELLQE 1340
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEEL--------EERHELYEEAKAKKEELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1341 ENRQKLSlsTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGC-----LETAEEVKRKLQKDL 1415
Cdd:PRK03918 384 LTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCgreltEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1416 EGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVdldhqrqsacnLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREK 1495
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESE-----------LIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1496 ETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDA 1575
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1576 KLRLEVNLQAMKaqferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARK-----KLEMDLKDLEAHIDSA 1650
Cdd:PRK03918 611 EKELEREEKELK-----KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEEL 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1651 NKNRDEAIKQLRKLQaqmkdcmRELDDTRASREEIlaqakeneKKLKSMEAEMIQLQEELAAAE-RAKRQAQQERDELAD 1729
Cdd:PRK03918 686 EKRREEIKKTLEKLK-------EELEEREKAKKEL--------EKLEKALERVEELREKVKKYKaLLKERALSKVGEIAS 750
|
..
gi 2550219468 1730 EI 1731
Cdd:PRK03918 751 EI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1018-1597 |
4.78e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.34 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1018 LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST---DLSDQIAELQAQIAE 1094
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1095 LkmqlakkEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQ--------------KRDLGE 1160
Cdd:PRK02224 291 L-------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeslredaddleerAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1161 ELEALKTELEDtldstaAQQELRSKREQevnilkktleeeaktheaqiqemrqkhsqaVEELAEQLEQtkrvkanLEKAK 1240
Cdd:PRK02224 364 EAAELESELEE------AREAVEDRREE------------------------------IEELEEEIEE-------LRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1241 QTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKL 1320
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1321 TKDFSALESQlqdtqellQEENRQKLSLSTKLKQVEDEKNSFREQleeeeeaKHNLEKQIATLHAQVADMKKKME---DS 1397
Cdd:PRK02224 481 EAELEDLEEE--------VEEVEERLERAEDLVEAEDRIERLEER-------REDLEELIAERRETIEEKRERAEelrER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1398 VGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYD-KLEKTKTRLQQELDDllvdldhqRQSACNLEKKQKKFDQLLAEEKT 1476
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNsKLAELKERIESLERI--------RTLLAAIADAEDEIERLREKREA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1477 ISAKYAEERDR-AEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDvgksvheLEKSKRALEQQV 1555
Cdd:PRK02224 618 LAELNDERRERlAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQAEIGAVENEL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2550219468 1556 EEmktqLEELEDELQATEDAKLRLEV------NLQAMKAQFERDLQGR 1597
Cdd:PRK02224 691 EE----LEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQR 734
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
877-1738 |
1.03e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.50 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 877 KVREKQLAAENRLTEMETLQSQLMAEKLQ-LQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 955
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQaKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 956 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1035
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1036 SKSLAKLKNKHEAmitDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1115
Cdd:pfam02463 337 IEELEKELKELEI---KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1116 EAAQKNMALKKIRELESQISELQEDLESERA-----------------SRNKAEKQKRDLGEELEALKTELEDTLDSTAA 1178
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQGklteekeelekqelkllKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1179 QQELRSKREQEVNILKKTLEEEAKTHEA-QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1257
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGgRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1258 LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQEL 1337
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1338 LQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDsvgcletaEEVKRKLQKDLEG 1417
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL--------KKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1418 LSQRHEEKVAAYDKLEKTKTRLQQELDDllvdldhqrqsacNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKET 1497
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEE-------------KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1498 KALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKL 1577
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1578 RLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVaaRKKLEMDLKDLEAHIDSANKNRDEA 1657
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE--EAEILLKYEEEPEELLLEEADEKEK 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1658 IKQLRKLQAQMKDCM-RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSG 1736
Cdd:pfam02463 951 EENNKEEEEERNKRLlLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
..
gi 2550219468 1737 KG 1738
Cdd:pfam02463 1031 KG 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1610-1910 |
3.82e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.54 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1610 RQVREMEAELEdeRKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAqmkdcmrELDDTRASREEILAQA 1689
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1690 KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELI 1769
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1770 NDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTvKSKYKASITALEAKIAQLEEQLDNETK 1849
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1850 ERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRA 1910
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1127-1942 |
1.12e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 90.18 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1127 IRELESQISELQEDLESeraSRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA 1206
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1207 QiqemRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN--ERGELANEVKVLLQGKGDSEHKRK---KVEAQLQEL--Q 1279
Cdd:pfam15921 157 A----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilVDFEEASGKKIYEHDSMSTMHFRSlgsAISKILRELdtE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1280 VKFNEG---------ERVRTELADKVTKL-QVELDNVTGLLSQSDSKSSKLTKDFSALESQ---LQDTQELLQEENRQKL 1346
Cdd:pfam15921 233 ISYLKGrifpvedqlEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1347 SLStkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVAdmkkkmedsvgcLETAEEVKRKLQKDleglsQRHEEKV 1426
Cdd:pfam15921 313 SMY--MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV------------LANSELTEARTERD-----QFSQESG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1427 AAYDKLEKTKTRLqqelddllvdldHQRQSACNLEKKQKK--FDQLLAEEKTISAKYAEERDRaEAEAREKETKALSLAR 1504
Cdd:pfam15921 374 NLDDQLQKLLADL------------HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDR-NMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1505 ALEEAMEQK-AELERLNKQFR---TEMEDLMSSKDDVGKSVHELEKSKRALE---QQVEEMKTQLEELEDELQAT--EDA 1575
Cdd:pfam15921 441 ECQGQMERQmAAIQGKNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1576 KLRLEVNLQAmkaqfeRDLQGRDEQSEekkkqlvrQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRD 1655
Cdd:pfam15921 521 KLRSRVDLKL------QELQHLKNEGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1656 EAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSS 1735
Cdd:pfam15921 587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1736 GKGALALEEKRRLEARIaqleeeleeeQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENArqqlerQNKELKVKL 1815
Cdd:pfam15921 667 NELNSLSEDYEVLKRNF----------RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS------DGHAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1816 QeMEGTVKSKyKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVD-----------DERRNAEQYKD 1884
Cdd:pfam15921 731 G-MQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNkmagelevlrsQERRLKEKVAN 808
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1885 QA---DKASTRLKQLKRQLeeaeeEAQRANASRRKLQRELeDATETADAMNREVSSLKNKL 1942
Cdd:pfam15921 809 MEvalDKASLQFAECQDII-----QRQEQESVRLKLQHTL-DVKELQGPGYTSNSSMKPRL 863
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
985-1590 |
2.62e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 88.54 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 985 LEKVTTEAKLKKleEEQIILEDQNCKLAKEKKLLEDRIAEFttnLTEEEEKSKSLAKLKNKHeamitdleerlrreekqr 1064
Cdd:TIGR04523 105 LSKINSEIKNDK--EQKNKLEVELNKLEKQKKENKKNIDKF---LTEIKKKEKELEKLNNKY------------------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1065 QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEeeaaqknmalkKIRELESQISELQEDLESE 1144
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ-----------KNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1145 RASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV---NILKKTLEEEAKTHEAQIQEMRQKHSQavee 1221
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQ---- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1222 laeqlEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKkveaqlqELQVKFNEGERVRTELADKVTKLQV 1301
Cdd:TIGR04523 307 -----DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-------ELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1302 eldnvtgLLSQSDSKSS---KLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEK 1378
Cdd:TIGR04523 375 -------LKKENQSYKQeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1379 QIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELD--DLLVDLDHQRQS 1456
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKdlTKKISSLKEKIE 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1457 ACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSKDD 1536
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKE-------IEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1537 VGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQF 1590
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1555-1930 |
4.21e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1555 VEEMKTQLEELEDELQATEDAKlrlevNLQAMKAQFERDLQG-RDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAAR 1633
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYR-----ELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1634 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1713
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1714 ERAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQLEEELEEEQgntELINDRLKKANLQIDQINTDLNLERSH 1793
Cdd:COG1196 350 EEELEEAEAELAEAE--------------EALLEAEAELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1794 AQKNENARQQLERQNKELKVKLQEMEGTvkskyKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVD 1873
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1874 DERRNAEQYKDQADKASTRLKQ-LKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1930
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
878-1569 |
5.69e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.43 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 878 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHD---LEARVEEEEERCQH 954
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 955 LQAEKKKMQQniqeleeqleeEESARQKLQLEKVTTEAKLKKLEEEqiiledqncklakeKKLLEDRIAEFTTNLTEEEE 1034
Cdd:PRK03918 226 LEKEVKELEE-----------LKEEIEELEKELESLEGSKRKLEEK--------------IRELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1035 KSKSLAKLKNKHEAMITdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVE 1114
Cdd:PRK03918 281 KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1115 EEAAQKNMALKKIRELEsqiselqedleserasrnkaEKQKRDLGEELEALKTELEdtldstaaqqelrskreqEVNILK 1194
Cdd:PRK03918 359 ERHELYEEAKAKKEELE--------------------RLKKRLTGLTPEKLEKELE------------------ELEKAK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1195 KTLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKANLEKAKQTL-ENERGELANEVKVLLqgkgdsehkrKKVEA 1273
Cdd:PRK03918 401 EEIEEEISKITARIGELKKE----IKELKKAIEELKKAKGKCPVCGRELtEEHRKELLEEYTAEL----------KRIEK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1274 QLQELQVKFNEGERVRTELaDKVTKLQVELDNVTGLLSQSDSKSSKLTK-DFSALESQLQDTQELLQEENRQKLSLSTKL 1352
Cdd:PRK03918 467 ELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1353 KQVEdEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKkkmedsvgcLETAEEVKRKLqKDLEGLSQRHEEKVAAYDKL 1432
Cdd:PRK03918 546 KELE-KLEELKKKLAELEKKLDELEEELAELLKELEELG---------FESVEELEERL-KELEPFYNEYLELKDAEKEL 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1433 EKTKTRLQQELDDLLVDLDhqrqsacNLEKKQKKFDQLLAEEKTISAKYAEErdraeaEAREKETKALSLARALEEAMEQ 1512
Cdd:PRK03918 615 EREEKELKKLEEELDKAFE-------ELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELAGLRAE 681
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1513 KAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEqQVEEMKTQLEELEDEL 1569
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1036-1727 |
1.04e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.89 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1036 SKSLAKLKNKHEAMITDLE--ERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE-----EELQA 1108
Cdd:COG4913 231 VEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLA----ELEYLRAALRLWFAQRRLELLEAEleelrAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1109 ALARVEEEAAQKNMALKKIRELESQIS--------ELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQ 1180
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1181 ELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKV---L 1257
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFvgeL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1258 LQGKGDSEHKRKKVEAQL----------QELQVKFNE-------GERVRTEladKVTKLQVELDNVTgllSQSDSKSSKL 1320
Cdd:COG4913 467 IEVRPEEERWRGAIERVLggfaltllvpPEHYAAALRwvnrlhlRGRLVYE---RVRTGLPDPERPR---LDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1321 TKDFSALESQLQdtQELLQEENRQKlslstklkqVEDEknsfrEQLeeeeeakHNLEKQIaTLHAQVadmkkKMEDSVGC 1400
Cdd:COG4913 541 DFKPHPFRAWLE--AELGRRFDYVC---------VDSP-----EEL-------RRHPRAI-TRAGQV-----KGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1401 LETAEEVKRKLQkdlegLSQRHEEKVAAydkLEKTKTRLQQElddllvdldhqrqsacnLEKKQKKFDQLLAEEKTISAK 1480
Cdd:COG4913 592 KDDRRRIRSRYV-----LGFDNRAKLAA---LEAELAELEEE-----------------LAEAEERLEALEAELDALQER 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1481 YAEERDRAEAEAREKETKalSLARALEEAMEQKAELERLNKQFRT---EMEDLMSSKDDVGKSVHELEKSKRALEQQVEE 1557
Cdd:COG4913 647 REALQRLAEYSWDEIDVA--SAEREIAELEAELERLDASSDDLAAleeQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1558 MKTQLEELEDELQ-ATEDAKLRLEVNLQAMKAQferdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQ-RSMAVAARKK 1635
Cdd:COG4913 725 AEEELDELQDRLEaAEDLARLELRALLEERFAA-----ALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNRE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1636 LEMDLKDLEAHIDSAnknrDEAIKQLRKLqaqmkdcmrelddtrasREEILAQAKENEKKL--KSMEAEMIQLQEELaaa 1713
Cdd:COG4913 800 WPAETADLDADLESL----PEYLALLDRL-----------------EEDGLPEYEERFKELlnENSIEFVADLLSKL--- 855
|
730
....*....|....
gi 2550219468 1714 ERAKRQAQQERDEL 1727
Cdd:COG4913 856 RRAIREIKERIDPL 869
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
902-1644 |
2.27e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.79 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 902 EKLQLQEQLQAET-----ELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNiQELEEQLEEE 976
Cdd:TIGR00618 173 FPLDQYTQLALMEfakkkSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS-HAYLTQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 977 ESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLedRIAEfttnlteeeeKSKSLAKLKNKHEAMITDLEER 1056
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAA----------HIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1057 LRREEKQRQElektRRKLEGDSTDLSDQIAELQaqiaelkmQLAKKEEELqaalARVEEEAAQKNMALKKIRELESQISE 1136
Cdd:TIGR00618 320 MRSRAKLLMK----RAAHVKQQSSIEEQRRLLQ--------TLHSQEIHI----RDAHEVATSIREISCQQHTLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1137 LQEDLESERASRNKAEKQKRDLGEEleALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKH- 1215
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQRE--QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHl 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1216 ---SQAVEELaEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGErvrtel 1292
Cdd:TIGR00618 462 qesAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE------ 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1293 aDKVTKLQVELDNVTGllsQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEA 1372
Cdd:TIGR00618 535 -QTYAQLETSEEDVYH---QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1373 KHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDH 1452
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1453 QRQSAC-NLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAEL--ERLNKQFRTEMED 1529
Cdd:TIGR00618 691 QLTYWKeMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1530 LMS--SKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdeqseEKKKQ 1607
Cdd:TIGR00618 771 TAAlqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKSA 842
|
730 740 750
....*....|....*....|....*....|....*..
gi 2550219468 1608 LVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLE 1644
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
908-1463 |
3.31e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.58 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 908 EQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERcqhlQAEKKKMQQNIQELEEQLEEEESARQKLQLEK 987
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK----KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 988 VTTEAKlKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNL-----TEEEEKSKSLAKLKNKHEAMITDLEERLRREEK 1062
Cdd:PTZ00121 1484 KADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdeakkAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1063 QRQELEKTRrklEGDSTDLSDQIAELQAQIAELK----MQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQ 1138
Cdd:PTZ00121 1563 KKKAEEAKK---AEEDKNMALRKAEEAKKAEEARieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1139 EDLESErasRNKAEKQKRDlgEELEALKTELEdtldstaAQQELRSKREQEVniLKKTLEEEAKTHEAQIQEMRQKhsQA 1218
Cdd:PTZ00121 1640 KKEAEE---KKKAEELKKA--EEENKIKAAEE-------AKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEA--KK 1703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1219 VEELAEQLEQTKRVKANLEKAkqtlENERGELANEVKvllqgKGDSEHKRKKVEAQLQE------LQVKFNEGERVRTEL 1292
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKA----EEENKIKAEEAK-----KEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIR 1774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1293 ADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQeeNRQKLSLSTKLKQVEDEKNSFREQ---LEEE 1369
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI--NDSKEMEDSAIKEVADSKNMQLEEadaFEKH 1852
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1370 EEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDkleKTKTRLQQELDDLLVD 1449
Cdd:PTZ00121 1853 KFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNND---IIDDKLDKDEYIKRDA 1929
|
570
....*....|....
gi 2550219468 1450 LDhQRQSACNLEKK 1463
Cdd:PTZ00121 1930 EE-TREEIIKISKK 1942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1050-1816 |
4.73e-16 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 84.78 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1050 ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQ----IAELQA--------------QIAELKMQLAKKE---EELQA 1108
Cdd:pfam15921 112 VIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQlqntVHELEAakclkedmledsntQIEQLRKMMLSHEgvlQEIRS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1109 ALARVEEEAAQK-----NMALKKIRELESQISELQEDLESERASrnkAEKQKRDLGEELEALKTELEDTLDSTAAQQELR 1183
Cdd:pfam15921 192 ILVDFEEASGKKiyehdSMSTMHFRSLGSAISKILRELDTEISY---LKGRIFPVEDQLEALKSESQNKIELLLQQHQDR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1184 SKR---EQEVNIlkKTLEEEAKTHEAQ----------IQEM-RQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGE 1249
Cdd:pfam15921 269 IEQlisEHEVEI--TGLTEKASSARSQansiqsqleiIQEQaRNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1250 LANEVKVllqgkgdsehkrkkVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALES 1329
Cdd:pfam15921 347 LEKQLVL--------------ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1330 QLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKR 1409
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1410 KLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQkkfdqllaeektisakyaeerdrae 1489
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ------------------------- 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1490 aeareKETKALSLaraleeameQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEdEL 1569
Cdd:pfam15921 548 -----TECEALKL---------QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK-IL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1570 QATEDAKLrlevnlqamkaqfeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDS 1649
Cdd:pfam15921 613 KDKKDAKI--------------RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1650 ANKN----RDEAIKQLRKLQAQMKDCMRELDDTRASreeilaqakenekkLKSMEAE-------MIQLQEELaAAERAKR 1718
Cdd:pfam15921 679 LKRNfrnkSEEMETTTNKLKMQLKSAQSELEQTRNT--------------LKSMEGSdghamkvAMGMQKQI-TAKRGQI 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1719 QAQQERDELADE-IANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIndRLKKANLQIDQINTDLNLERSHAQKN 1797
Cdd:pfam15921 744 DALQSKIQFLEEaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL--RSQERRLKEKVANMEVALDKASLQFA 821
|
810 820
....*....|....*....|
gi 2550219468 1798 EnARQQLERQNKE-LKVKLQ 1816
Cdd:pfam15921 822 E-CQDIIQRQEQEsVRLKLQ 840
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1011-1689 |
1.39e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 83.24 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1011 LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelektrRKLegdsTDLSDQIAELQA 1090
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM------RQL----SDLESTVSQLRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1091 QIAELKMQLAKKEEELQAAL----ARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQK-----RDLGEE 1161
Cdd:pfam15921 332 ELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1162 --LEALKTELEDtldstaaqqelRSKREQEVNILKKTLEEEAKTH-EAQIQEMRQKHS--QAVEELAEQLEQTKRV---- 1232
Cdd:pfam15921 412 itIDHLRRELDD-----------RNMEVQRLEALLKAMKSECQGQmERQMAAIQGKNEslEKVSSLTAQLESTKEMlrkv 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1233 -------KANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRteladkvtKLQVELDN 1305
Cdd:pfam15921 481 veeltakKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR--------NVQTECEA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1306 VTGLLSQSDsksskltKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1385
Cdd:pfam15921 553 LKLQMAEKD-------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1386 QVADMKKKMEDSVGC----LETAEEVKRKLQK----------DLEGLSQRHEEKVAAY----DKLEKTKTRLQQELDDLL 1447
Cdd:pfam15921 626 RVSDLELEKVKLVNAgserLRAVKDIKQERDQllnevktsrnELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQ 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1448 VDLDHQRQSACNLEKKQKKFDQL-LAEEKTISAKyaeerdRAEAEARekETKALSLARALEEAMEQKAELERLNKQFRTE 1526
Cdd:pfam15921 706 SELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK------RGQIDAL--QSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1527 MEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERD---LQGRDEQSEE 1603
Cdd:pfam15921 778 LSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDvkeLQGPGYTSNS 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1604 KKKQLVRQVREMEAELEDERKQRSMAvaarkklemdlKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRE 1683
Cdd:pfam15921 858 SMKPRLLQPASFTRTHSNVPSSQSTA-----------SFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKA 926
|
....*.
gi 2550219468 1684 EILAQA 1689
Cdd:pfam15921 927 EDKGRA 932
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
992-1872 |
2.01e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 82.79 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 992 AKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEeeksksLAKLKNKHEAMITDLEERLRREEKQRQELEKTR 1071
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1072 RKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAalarveeeaaqknmalkkiRELESQISELQEDLESERASRNKA 1151
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS-------------------LATRLELDGFERGPFSERQIKNFH 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1152 EKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ------AVEELAEQ 1225
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSSDRILEL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1226 LEQTKRVKANLEKAKQTLENErgELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDN 1305
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTE--TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1306 VtgllSQSDSKSSKLTKDFSAlESQLQDTQEllqeenrqklSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1385
Cdd:TIGR00606 555 K----SRHSDELTSLLGYFPN-KKQLEDWLH----------SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1386 QVADMKKKMEDSVGC------LETAEEVKRKLQKDL--------------EGLSQRHEEKVAAYDKLEKTKTRLQQELDD 1445
Cdd:TIGR00606 620 QLSSYEDKLFDVCGSqdeesdLERLKEEIEKSSKQRamlagatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1446 LLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARaleEAMEQKAELERLNKQFRT 1525
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR---DIQRLKNDIEEQETLLGT 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1526 EMEDLMSSKD---DVGksvhelekSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERD-----LQGR 1597
Cdd:TIGR00606 777 IMPEEESAKVcltDVT--------IMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskIELN 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1598 DEQSEEKKKQlVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMreldd 1677
Cdd:TIGR00606 849 RKLIQDQQEQ-IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ----- 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1678 traSREEILAQAKENEKKLKSMEAEMI--QLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIaQL 1755
Cdd:TIGR00606 923 ---QEKEELISSKETSNKKAQDKVNDIkeKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI-NE 998
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1756 EEELEEEQGNTELINDRLKKANLQIDQINTDLN-LERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITale 1834
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKeVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALG--- 1075
|
890 900 910
....*....|....*....|....*....|....*...
gi 2550219468 1835 aKIAQLEEQLDNETKERQAacKQVRRTEKKLKDVLLQV 1872
Cdd:TIGR00606 1076 -RQKGYEKEIKHFKKELRE--PQFRDAEEKYREMMIVM 1110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1219-1943 |
2.49e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.42 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1219 VEELAEQLEQTKRVKANLEKAkQTLENERGELanEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1298
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERY-QALLKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1299 LQVELDNVTGLLSQ-SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLE 1377
Cdd:TIGR02169 270 IEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1378 KQIATLHAQVADMKKKMEDSVgclETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKT---RLQQELDDLLVDLDHQR 1454
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLR---AELEEVDKEFAETRDELKDYREKLEKLKREINELKReldRLQEELQRLSEELADLN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1455 QSACNLEKKQKKFDqllaeektisakyaEERDRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSK 1534
Cdd:TIGR02169 427 AAIAGIEAKINELE--------------EEKEDKALEIKKQEWK-------LEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1535 DDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGR-------DEQSEEKKKQ 1607
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRlnnvvveDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1608 LVRQVREMEAELEDERKQRSMAVAARKKLE-------MDLKDLEAHIDSANKN--RD----EAIKQLRKL--QAQMKDCM 1672
Cdd:TIGR02169 566 LLKRRKAGRATFLPLNKMRDERRDLSILSEdgvigfaVDLVEFDPKYEPAFKYvfGDtlvvEDIEAARRLmgKYRMVTLE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1673 RELDD--------TRASREEILAQAKENEKkLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEE 1744
Cdd:TIGR02169 646 GELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS-------RK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1745 KRRLEARIaqleeeleeeqgntELINDRLKKANLQIDQINTDLnleRSHAQKNENARQQLERQNKELkvklQEMEgTVKS 1824
Cdd:TIGR02169 718 IGEIEKEI--------------EQLEQEEEKLKERLEELEEDL---SSLEQEIENVKSELKELEARI----EELE-EDLH 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1825 KYKASITALEAKIA-----QLEEQLDNETKERQAACKQVRRTEKKLKDVLL---QVDDERRNAEQY----KDQADKASTR 1892
Cdd:TIGR02169 776 KLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQELQEQridlKEQIKSIEKE 855
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1893 LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLR 1943
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1328-1944 |
3.17e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.03 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1328 ESQLQDTQE-------LLQEENRQKLSLSTKLKQVEDEKNsFREQLEEEEEA-----KHNLEKQIATLHAQVADMKKKME 1395
Cdd:TIGR02168 178 ERKLERTREnldrledILNELERQLKSLERQAEKAERYKE-LKAELRELELAllvlrLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1396 DsvgcletAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 1475
Cdd:TIGR02168 257 E-------LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1476 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkddvgksVHELEKSKRALEQQV 1555
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-------VAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1556 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKK 1635
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELK---ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1636 LEMDLKDLEAHIDSAnKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQ--LQEELAAA 1713
Cdd:TIGR02168 480 AERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQavVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1714 ERAkrqaqqerdelADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQI------------- 1780
Cdd:TIGR02168 559 KKA-----------IAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlv 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1781 -DQINTDLNLERSHAQKNENARQQLERQNKE-LKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQV 1858
Cdd:TIGR02168 628 vDDLDNALELAKKLRPGYRIVTLDGDLVRPGgVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1859 RRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSL 1938
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
....*.
gi 2550219468 1939 KNKLRR 1944
Cdd:TIGR02168 788 EAQIEQ 793
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
878-1703 |
9.19e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 80.48 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 878 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELrarLTAKKQELEEICHDLEARVEEEEERCQHLQA 957
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKV---FQGTDEQLNDLYHNHQRTVREKERELVDCQR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 958 EKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEE--EEK 1035
Cdd:TIGR00606 327 ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIErqEDE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1036 SKSLAKLKNkheamitDLEERLRREEKQRQELEKTR----RKLEGDSTDLSDQIAELQAQIAELKM------QLAKKEEE 1105
Cdd:TIGR00606 407 AKTAAQLCA-------DLQSKERLKQEQADEIRDEKkglgRTIELKKEILEKKQEELKFVIKELQQlegssdRILELDQE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1106 LQAALARVEEEAAQKNMALKKIRELESQiselQEDLESERASRNKAEKQKrDLGEELEALKTELEDTLDSTAAQQELRSK 1185
Cdd:TIGR00606 480 LRKAERELSKAEKNSLTETLKKEVKSLQ----NEKADLDRKLRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1186 REQEVNIL---------KKTLEEEAKTHEAQIQEMRQKHSQAVEELAeQLEQTKRVKANLEKAKQTLENERGELANEVKV 1256
Cdd:TIGR00606 555 KSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA-SLEQNKNHINNELESKEEQLSSYEDKLFDVCG 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1257 LLQGKGDSEHKRKKVE---AQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQD 1333
Cdd:TIGR00606 634 SQDEESDLERLKEEIEkssKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKS 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1334 TQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEE------V 1407
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtI 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1408 KRKLQKDLEGLSQRHEEKVAAYD--KLEKTKTRLQQELDDLLVDLDHQRQSACNLEK----KQKKFDQL------LAEEK 1475
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKliqdQQEQIQHLksktneLKSEK 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1476 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVH-ELEKSKRALEQQ 1554
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1555 VEEMKTQLEELEDelqATEDAKLRLEVNLQAMKAQFerdlqgrdEQSEEKKKQLVRQVREMEAELEDERKQRSMAV--AA 1632
Cdd:TIGR00606 954 HGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL--------EECEKHQEKINEDMRLMRQDIDTQKIQERWLQdnLT 1022
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1633 RKKLEMDLKDLEAHIDSANKNRDEaiKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1703
Cdd:TIGR00606 1023 LRKRENELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
860-1165 |
1.12e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.10 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 860 QVSRQEEEMMAKEEELVKVREKQLAAEN-------RLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQ 932
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 933 ELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLA 1012
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1013 KEKK-------LLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQI 1085
Cdd:TIGR02168 845 EQIEelsedieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1086 AELQAQIAELKMQLAKKEEELqAALARVEEEAAQKNMALK---------KIRELESQISEL-------QEDLESERASRN 1149
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERL-SEEYSLTLEEAEALENKIeddeeearrRLKRLENKIKELgpvnlaaIEEYEELKERYD 1003
|
330
....*....|....*.
gi 2550219468 1150 KAEKQKRDLGEELEAL 1165
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETL 1019
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1027-1751 |
1.12e-14 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 80.27 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1027 TNLTEEEEKSKSL-AKLKNKHEAmITDLEERLRREEKQRQELEKTRR-KLEGDSTDLSDQIAELQAQIAELKMQLAKKEE 1104
Cdd:pfam12128 244 TKLQQEFNTLESAeLRLSHLHFG-YKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1105 ELQAA--------LARVEEEAAQKNMALKKIRELESQ-------------ISELQEDLESERASRNKAE----KQKRD-L 1158
Cdd:pfam12128 323 ELEALedqhgaflDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdVTAKYNRRRSKIKEQNNRDiagiKDKLAkI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1159 GEELEALKTELEDTLDstAAQQELRSKREQEVNILKktleEEAKTHEAQIQEM--RQKHSQAVEELAEQLEQTKrvkANL 1236
Cdd:pfam12128 403 REARDRQLAVAEDDLQ--ALESELREQLEAGKLEFN----EEEYRLKSRLGELklRLNQATATPELLLQLENFD---ERI 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1237 EKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSK 1316
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGK 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1317 --SSKLTK----DFSALESQLQDTQEL----LQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQ 1386
Cdd:pfam12128 554 viSPELLHrtdlDPEVWDGSVGGELNLygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1387 VADMKKKMEDSVGCLETAEEVKRKLqkdleglsqrHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSacnLEKKQKK 1466
Cdd:pfam12128 634 LEKASREETFARTALKNARLDLRRL----------FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1467 FDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMedlmsskddvgksvheleK 1546
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS-GAKAELKALETWYKRDL------------------A 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1547 SKRALEQQVEEMKTQLEELEDELQatedaklRLEVNLQAMkAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDerkqr 1626
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIE-------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISE----- 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1627 smavaarkkLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDtRASREEILAQAKENEKKLKSMEAEMIQL 1706
Cdd:pfam12128 826 ---------LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC-EMSKLATLKEDANSEQAQGSIGERLAQL 895
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 2550219468 1707 QEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR 1751
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDH 940
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
842-1414 |
1.12e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 842 KLRNWQWWRLFTKVKPLLQVSRQEEEMMAKE---EELVKVREKQLAAENRLTEMETLQSQLmaeKLQLQEQLQAEtELCA 918
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEArkaDELKKAEEKKKADEAKKAEEKKKADEA---KKKAEEAKKAD-EAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 919 EAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLE 998
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 999 EEQIILEDQNCKLAKEKKLLEdriaefttnLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelEKTRRKLEgds 1078
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADE---------AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA--EEAKKKAE--- 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1079 tdlsdqiAELQAQIAELKMQLAKKEEELQaalaRVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRdl 1158
Cdd:PTZ00121 1468 -------EAKKADEAKKKAEEAKKADEAK----KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK-- 1534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1159 gEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKA---- 1234
Cdd:PTZ00121 1535 -KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeak 1613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1235 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADK-----VTKLQVELDNVTGL 1309
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeAKKAEEDEKKAAEA 1693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1310 LSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSfREQLEEEEEAKHNLEKQIATLHAQVAD 1389
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK-AEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
570 580
....*....|....*....|....*
gi 2550219468 1390 MKKKMEDSVGCLETAEEVKRKLQKD 1414
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
881-1614 |
1.74e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 881 KQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAE----AEELRARLTAKKQELEEICHDLEARVEeeeercqhlq 956
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkkAEEKKKADEAKKAEEKKKADEAKKKAE---------- 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 957 aEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILE--DQNCKLAKEKKLLEDRIAEFTTNLTEEEE 1034
Cdd:PTZ00121 1313 -EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1035 KSKslaKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlAKKEEELQAALARVE 1114
Cdd:PTZ00121 1392 KAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK---KKAEEAKKAEEAKKK 1465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1115 EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILK 1194
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1195 KTLEEEAKTHEAQIQEMRQKHSQAVEElAEQLEQTKRVKANLEKAKQTLENERGELANEVKvllqgKGDSEHKRKKVEAQ 1274
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK-----KMKAEEAKKAEEAK 1619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1275 LQELQVKFNEGERVRTELADKVTKLQVEldnvtgllsqsdsKSSKLTKDFSalESQLQDTQELLQEENRQKlsLSTKLKQ 1354
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKK-------------KAEELKKAEE--ENKIKAAEEAKKAEEDKK--KAEEAKK 1682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1355 VEDEKNSFREQLEEEEEAKHNLEKqiatLHAQVADMKKKMEDsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEK 1434
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEE----LKKKEAEEKKKAEE----LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1435 TKTRLQQElddllvdldhQRQSACNLEKKQKKFDQLLAEEktisAKYAEERDRAEAEAREKETKAlSLARALEEAMEQKA 1514
Cdd:PTZ00121 1755 EKKKIAHL----------KKEEEKKAEEIRKEKEAVIEEE----LDEEDEKRRMEVDKKIKDIFD-NFANIIEGGKEGNL 1819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1515 ELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEE-------MKTQLEELEDELQATEDAKLRLEVNLQAMK 1587
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEdgnkeadFNKEKDLKEDDEEEIEEADEIEKIDKDDIE 1899
|
730 740 750
....*....|....*....|....*....|....*
gi 2550219468 1588 AQF-ERDLQGRDEQS-------EEKKKQLVRQVRE 1614
Cdd:PTZ00121 1900 REIpNNNMAGKNNDIiddkldkDEYIKRDAEETRE 1934
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
875-1434 |
2.43e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 875 LVKVREKQLAA-ENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQ 953
Cdd:PRK03918 194 LIKEKEKELEEvLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK----LEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 954 HLQAEKKKMQQNIQELEEQLEEEESARqKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1033
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1034 EKSKSLAKLKNKHEA--MITDLEERLRREEKQR-----QELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEEL 1106
Cdd:PRK03918 349 ELEKRLEELEERHELyeEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELK----KEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1107 QAALARVE-------------EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKteLEDTL 1173
Cdd:PRK03918 425 KKAIEELKkakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1174 DstaaqqELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ--AVEELAEQLEQTKRVKANLEKAKQTLENERGELA 1251
Cdd:PRK03918 503 E------QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1252 NEVKVLlqGKGDSEHKRKKVEaQLQELQVKFNEGERVRTELADKVTKLQVELDNvtglLSQSDSKSSKLTKDFSALESQL 1331
Cdd:PRK03918 577 KELEEL--GFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEELRKEL 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1332 QDTQELLQEENRQKlsLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKmedsvgcletAEEVKrKL 1411
Cdd:PRK03918 650 EELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA----------KKELE-KL 716
|
570 580
....*....|....*....|...
gi 2550219468 1412 QKDLEGLsQRHEEKVAAYDKLEK 1434
Cdd:PRK03918 717 EKALERV-EELREKVKKYKALLK 738
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1055-1883 |
5.04e-14 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 78.07 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1055 ERLRREEKQRQELEKTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKnmalKKIRELE 1131
Cdd:COG3096 282 ELSERALELRRELFGARRQL----AEEQYRLVEMARELEELSARESDLEQDYQAAsdhLNLVQTALRQQ----EKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1132 SQISELQEDLESERASRNKAEKQKRDLGEELEA-------LKTELED---TLDS--TAA---QQELRSKRE-QEVNILKK 1195
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVqqTRAiqyQQAVQALEKaRALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1196 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN-----ERGELANEVKVLLQGKGDSEH---K 1267
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYRSQQAlaqR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1268 RKKVEAQLQELQVKFNEGERVRTELADkvtklqveldnvtglLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1347
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEE---------------FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1348 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVadmkkkmedsvGC-LETAEEVKRKLQKDLEGLSQRHEEKv 1426
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS-----------GEaLADSQEVTAAMQQLLEREREATVER- 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1427 aayDKLEKTKTRLQQELDDLlvdldHQRQSACNLEKKQKKfDQ----LLAE---EKTISakyaeerDRAEAEAREKETKA 1499
Cdd:COG3096 647 ---DELAARKQALESQIERL-----SQPGGAEDPRLLALA-ERlggvLLSEiydDVTLE-------DAPYFSALYGPARH 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1500 LSLARALEEAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEK------SKRAL---------------- 1551
Cdd:COG3096 711 AIVVPDLSAVKEQLAGLEDC-------PEDLYliegdpDSFDDSVFDAEELEDavvvklSDRQWrysrfpevplfgraar 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1552 EQQVEEMKTQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED---- 1621
Cdd:COG3096 784 EKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEAELAALRQRRSELERELAQhraq 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1622 ERKQRSMAVAARKKLEMdlkdLEAHIDSANKNRDEAikqlrkLQAQMKDCMRELDDTRASREEI------LAQAKENEKK 1695
Cdd:COG3096 859 EQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELDAAQEAQAFIqqhgkaLAQLEPLVAV 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1696 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN----SSGKGALALEEKR----RLEARIAQLEEELEEEqgnte 1767
Cdd:COG3096 929 LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRrphfSYEDAVGLLGENSdlneKLRARLEQAEEARREA----- 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1768 liNDRLKKANLQIDQINTDL-NLERSHAQKNENArQQLERQNKELKVKL-QEMEGTV---KSKYKASITALEAKIAQLEE 1842
Cdd:COG3096 1004 --REQLRQAQAQYSQYNQVLaSLKSSRDAKQQTL-QELEQELEELGVQAdAEAEERArirRDELHEELSQNRSRRSQLEK 1080
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 2550219468 1843 QLDNETKERQAACKQVRRTEKKLKdvllqvdDERRNAEQYK 1883
Cdd:COG3096 1081 QLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAK 1114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1129-1941 |
9.53e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.49 E-value: 9.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1129 ELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA-- 1206
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDar 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1207 QIQEMRQKHSQAVEELAEQLEQTKRVKANlEKAKQTLENERGELANEVKVLLQGKgDSEHKRKKVEAQLQELQVKFNEGE 1286
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARKAEDARKAEEA-RKAEDAKKAEAARKAEEVRKAEELR-KAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1287 RVRTEL-ADKVTKLQ-VELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKlslSTKLKQVEdEKNSFRE 1364
Cdd:PTZ00121 1219 KAEDAKkAEAVKKAEeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAE-EKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1365 QLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVgclETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELD 1444
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK---KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1445 DLLVDLDHQRQSACNLEKKQKkfdqllAEEktisAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFR 1524
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKK------ADE----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1525 TEME-DLMSSKDDVGKSVHELEKsKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEE 1603
Cdd:PTZ00121 1442 EAKKaDEAKKKAEEAKKAEEAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1604 KKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQmkdcmrELDDTRASRE 1683
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE------EAKKAEEARI 1594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1684 EILAQAKENEKKLKSmeaemiqlqEELAAAERAKRQAQQERDELADEIANSSGKGALAlEEKRRLEariaqleeeleeeq 1763
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKA---------EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA-EEKKKAE-------------- 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1764 gntelindRLKKANlqidqintdlnlERSHAQKNENARQQLERQNKELKVKLQEMEgtvkSKYKASITALEAKIAQLEEQ 1843
Cdd:PTZ00121 1651 --------ELKKAE------------EENKIKAAEEAKKAEEDKKKAEEAKKAEED----EKKAAEALKKEAEEAKKAEE 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1844 LDNETKERQAACKQVRRTEKKLKdvlLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELED 1923
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
810
....*....|....*...
gi 2550219468 1924 ATETADAMNREVSSLKNK 1941
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1182-1751 |
2.22e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.85 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1182 LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnEVKVLlqgk 1261
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETL---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1262 gdsehkrkkvEAQLQELQVKFNEGERVRTELADKVTKLQVEL----DNVTGLLSQSDsksskltkdfsaLESQLQDTQEL 1337
Cdd:PRK02224 257 ----------EAEIEDLRETIAETEREREELAEEVRDLRERLeeleEERDDLLAEAG------------LDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1338 LQEE-NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLE 1416
Cdd:PRK02224 315 RREElEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1417 GLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAkyaeerdraeaearEKE 1496
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEC--------------GQP 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1497 TKALSLARALEEAMEQKAELERLNKQFRTEMEDLmSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDak 1576
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE-- 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1577 lRLEvNLQAMKAQFERDLQGRDEQSEEKKKQlVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDE 1656
Cdd:PRK02224 538 -RAE-ELRERAAELEAEAEEKREAAAEAEEE-AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1657 aikqlRKLQAQMKDCMRELDDTRASREEILAqAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSG 1736
Cdd:PRK02224 615 -----REALAELNDERRERLAEKRERKRELE-AEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
570
....*....|....*
gi 2550219468 1737 KgalaLEEKRRLEAR 1751
Cdd:PRK02224 689 E----LEELEELRER 699
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
981-1730 |
2.81e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 75.53 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 981 QKLQLEKVTTEAKLK----KLEEEQIILEDQNcKLAKEKKLLEDRIaefTTNLTEEEEKSKSLAKLKNKHEAMITDLEER 1056
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1057 LRREEKQRQELEKTRRKLEGDSTDLSDQIAelqaqiaelKMQLAKKEEELQAALARVEEEAaqknmalkKIRELESQISE 1136
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIE---------KMILAFEELRVQAENARLEMHF--------KLKEDHEKIQH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1137 LQEDLESERasrNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQevnilkktLEEEAKTHEAQIQEMRQKHS 1216
Cdd:pfam05483 227 LEEEYKKEI---NDKEKQVSLLLIQITEKENKMKDL---TFLLEESRDKANQ--------LEEKTKLQDENLKELIEKKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1217 QAVEELAEqleqtkrVKANLEKAKQTLENERGELANEVKVLLQgkgdsehKRKKVEAQLQELQVKFNEGERVRTELADKV 1296
Cdd:pfam05483 293 HLTKELED-------IKMSLQRSMSTQKALEEDLQIATKTICQ-------LTEEKEAQMEELNKAKAAHSFVVTEFEATT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1297 TKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVE---DEKNSFREQLEEEEEAK 1373
Cdd:pfam05483 359 CSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEkllDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1374 HNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQ 1453
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1454 RQSACNLEKKQKKfdqLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS 1533
Cdd:pfam05483 519 QEDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1534 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1613
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLE 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1614 EMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENE 1693
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
730 740 750
....*....|....*....|....*....|....*..
gi 2550219468 1694 KKLKSmeaemiQLQEELAAAERAKRQAQQERDELADE 1730
Cdd:pfam05483 756 LSLKK------QLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1020-1261 |
4.02e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 73.26 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1020 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1099
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1100 AKKEEELQAALArveeeAAQKNMALKKIRELESQiselQEDLESERASR--NKAEKQKRDLGEELEALKTELEDTLDSTA 1177
Cdd:COG4942 100 EAQKEELAELLR-----ALYRLGRQPPLALLLSP----EDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1178 AQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1257
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....
gi 2550219468 1258 LQGK 1261
Cdd:COG4942 251 LKGK 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1401-1944 |
6.01e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1401 LETAEEvKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACN---------LEKKQKKFDQLL 1471
Cdd:COG4913 244 LEDARE-QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRaelarleaeLERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1472 AEEKTISAKYAE-----------ERDRAEAEAREKETKALSLARALEeAMEQKAELERlnKQFRTEMEDLMSSKDDVGKS 1540
Cdd:COG4913 323 EELDELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLA-ALGLPLPASA--EEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1541 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ-----------SEEKKKQ-- 1607
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelievrPEEERWRga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1608 ------------LV-----RQVRE------MEAELEDERKQRSMAVAARKKLE-------MDLKD------LEAHIdsaN 1651
Cdd:COG4913 480 iervlggfaltlLVppehyAAALRwvnrlhLRGRLVYERVRTGLPDPERPRLDpdslagkLDFKPhpfrawLEAEL---G 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1652 KNRD----EAIKQLRK------LQAQMKD--CMRELDDTRASREE-ILAQakENEKKLKSMEAEMIQLQEELAAAERAKR 1718
Cdd:COG4913 557 RRFDyvcvDSPEELRRhpraitRAGQVKGngTRHEKDDRRRIRSRyVLGF--DNRAKLAALEAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1719 QAQQERDeladeianssgkgalALEEKRRLEARIAQleeeleeeqgntelindrlkkanLQIDQINTDLnLERSHAQKnE 1798
Cdd:COG4913 635 ALEAELD---------------ALQERREALQRLAE-----------------------YSWDEIDVAS-AEREIAEL-E 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1799 NARQQLERQNKELkvklqemegtvkskykasitaleakiAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRN 1878
Cdd:COG4913 675 AELERLDASSDDL--------------------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1879 AEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETAdamNREVSSLKNKLRR 1944
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL---RARLNRAEEELER 791
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1404-1981 |
9.09e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1404 AEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAE 1483
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1484 ERDRAEAEAREKETKALSLARALEEAmeQKAELERLNKQFR-TEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1562
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAA--RKAEEERKAEEARkAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKF 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1563 EELEDELQATEDAKLRLEvnlQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERK----------QRSMAVAA 1632
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAE---EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadeakkkaeeAKKKADAA 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1633 RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMK---------DCMRELDDTRASREEILAQAKENEKK---LKSME 1700
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeeakkkaDAAKKKAEEKKKADEAKKKAEEDKKKadeLKKAA 1414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1701 A------EMIQLQEELAAAERAKRQAQQERDelADEIANSSGKGALALEEKRRLE-ARIAQLEEELEEEQGNTELINDRL 1773
Cdd:PTZ00121 1415 AakkkadEAKKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEeAKKADEAKKKAEEAKKADEAKKKA 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1774 KKANLQIDQINTDLNLERS--HAQKNENARQQLERQNKELKVKLQEMEGTVKSKykasiTALEAKIAQLEEQLDNETKER 1851
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-----KADELKKAEELKKAEEKKKAE 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1852 QAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQleeaeeEAQRANASRRKLQRELEDATETADAM 1931
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA------EEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1932 NREVSSLKNKLRRGDLPFVVPR-RMARKGAGDGSDEEVDGKADGAEAKPAE 1981
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAaEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
880-1340 |
1.15e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 880 EKQLAAENRLTEMETLQSQlmAEKLQLQEQLQAE----TELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 955
Cdd:PRK02224 228 QREQARETRDEADEVLEEH--EERREELETLEAEiedlRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 956 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1035
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1036 SKSLaklknkhEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1115
Cdd:PRK02224 386 IEEL-------EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECG 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1116 EAAQKNMALKKIRELESQISELQEDLESERASRNKAEKqKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKK 1195
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1196 TLEEEAKTHEAQIQEMRQKHSQAvEELAEQLEQTKRVKANLEKAKQTLENERGELAN--EVKVLLQGKGDSEHKRKKVEA 1273
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAA-AEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKRE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1274 QLQELQVKFNE-----GERVRtELADKVTKLQVE------------LDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQE 1336
Cdd:PRK02224 617 ALAELNDERRErlaekRERKR-ELEAEFDEARIEearedkeraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
....
gi 2550219468 1337 LLQE 1340
Cdd:PRK02224 696 LRER 699
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1062-1889 |
1.83e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.08 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1062 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDL 1141
Cdd:TIGR00618 124 KKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1142 ESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQevnilkktleeeaKTHEAQIQEMRQKHSQAVEE 1221
Cdd:TIGR00618 204 QLLTLCTPCMPDTYHERKQVLEKELKHLRE------ALQQTQQSHAY-------------LTQKREAQEEQLKKQQLLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1222 LAEQLEQTKRVKANLEKAkqtleNERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRteladkvtklqv 1301
Cdd:TIGR00618 265 LRARIEELRAQEAVLEET-----QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL------------ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1302 eldnvtgllsqsdSKSSKLTKDFSALESQLQDTQELLQEENRqklslstkLKQVEDEKNSFREQLEEeeeaKHNLEKQIA 1381
Cdd:TIGR00618 328 -------------MKRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQ----QHTLTQHIH 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1382 TLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLE 1461
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1462 KKQKKFDQLLAEEKtisakyaeerDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMEDLMSSKDDVGK-- 1539
Cdd:TIGR00618 463 ESAQSLKEREQQLQ----------TKEQIHLQETRKKAVVLARLLELQ-EEPCPLCGSCIHPNPARQDIDNPGPLTRRmq 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1540 ----SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQgrdeqseekkkQLVRQVREM 1615
Cdd:TIGR00618 532 rgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN-----------ITVRLQDLT 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1616 EAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCM-RELDDTRASREEILAQAKENEK 1694
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQeRVREHALSIRVLPKELLASRQL 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1695 KLKSMEAEMIQL---QEELAAAERAKRQAQQ---ERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNtEL 1768
Cdd:TIGR00618 681 ALQKMQSEKEQLtywKEMLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK-AR 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1769 INDRLKKANLQIDQINTDLNLERShAQKNENARQQLERQNKELKVKLQEMEGTVKSkYKASITALEAKIAQLEEQLDNET 1848
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHL-AAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFLSRL 837
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 2550219468 1849 KERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKA 1889
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1087-1817 |
2.61e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 72.36 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1087 ELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERasrNKAEKQKRDLGEELEALK 1166
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK---DKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1167 TEledtldstaaqQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQTLENE 1246
Cdd:TIGR04523 114 ND-----------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1247 RGELANEVKvllqgkgDSEHKRKKVEAQLQELQVKFNEgervRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSA 1326
Cdd:TIGR04523 182 KLNIQKNID-------KIKNKLLKLELLLSNLKKKIQK----NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1327 LESQLQDTQELLQEENRQklsLSTKLKQVEDEKNSFReqleeeeeakhNLEKQIATLHAQVADMKKKMEDSV-----GCL 1401
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQ---LSEKQKELEQNNKKIK-----------ELEKQLNQLKSEISDLNNQKEQDWnkelkSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1402 ETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEK-KQKKFDQLLAEEKTISAk 1480
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQIND- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1481 yaeerdrAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1560
Cdd:TIGR04523 396 -------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1561 QLEELEDELQATEdaklrlevnlqamkaqferdlqgrdEQSEEKKKQLVRQVREMEaELEDERKQrsmavaarkkLEMDL 1640
Cdd:TIGR04523 469 QLKVLSRSINKIK-------------------------QNLEQKQKELKSKEKELK-KLNEEKKE----------LEEKV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1641 KDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMREL--DDTRASREEILAQAKENEKKLKsmeaemiQLQEELAAAERAKR 1718
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIE-------ELKQTQKSLKKKQE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1719 QAQQERDELADEIANSSGKgalaLEEKrrlEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNE 1798
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKE----IEEK---EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
730
....*....|....*....
gi 2550219468 1799 NARQQLERQNKELKVKLQE 1817
Cdd:TIGR04523 659 NKWPEIIKKIKESKTKIDD 677
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1033-1519 |
2.71e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1033 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR 1112
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1113 VEEEAAQKNMAL--KKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV 1190
Cdd:COG4717 132 QELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1191 NILKKTLEEEAKTHEAQIQEMRQKhsQAVEELAEQLEQTKR----------VKANLEKAKQTLENERGELANEVKVLLQG 1260
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENE--LEAAALEERLKEARLllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1261 KGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQlqdTQELLQE 1340
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL---EEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1341 ENRQKLSLSTKLKQVEDEKnSFREQLeEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGcletaeevkrklQKDLEGLSQ 1420
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEE-ELRAAL-EQAEEYQELKEELEELEEQLEELLGELEELLE------------ALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1421 RHEEKVAAYDKLEKTKTRLQQElddllvdldhqrQSACNLEKKQKKFDQLLAEektisAKYAEERDRAEAEAREKETKAL 1500
Cdd:COG4717 433 ELEELEEELEELEEELEELREE------------LAELEAELEQLEEDGELAE-----LLQELEELKAELRELAEEWAAL 495
|
490
....*....|....*....
gi 2550219468 1501 SLARALEEAMEQKAELERL 1519
Cdd:COG4717 496 KLALELLEEAREEYREERL 514
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1052-1226 |
3.65e-12 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 68.03 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1052 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMAlKKIRELE 1131
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1132 SqiseLQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldstaaqQELRSKREQEVNILKKTLEEEAKTHEAQIQEM 1211
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 2550219468 1212 RQKHSQAVEELAEQL 1226
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1498-1733 |
4.20e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1498 KALSL-ARALeeAMEQkaeLERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAlEQQVEEMKTQ---LEELEDELQATE 1573
Cdd:COG4913 192 KALRLlHKTQ--SFKP---IGDLDDFVREYMLEEPDTFEAADALVEHFDDLERA-HEALEDAREQielLEPIRELAERYA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1574 DAKLRLEVN------LQAMKAQFERDL-QGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMD-LKDLEA 1645
Cdd:COG4913 266 AARERLAELeylraaLRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1646 HIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEmiqLQEELAAAERAKRQAQQERD 1725
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELR 422
|
....*...
gi 2550219468 1726 ELADEIAN 1733
Cdd:COG4913 423 ELEAEIAS 430
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
875-1636 |
5.65e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 71.62 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 875 LVKVREKQLAAE-----NRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEE 949
Cdd:TIGR00606 346 LVEQGRLQLQADrhqehIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 950 ERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKL--EEEQIILEDQNCKLAKEKKLLEDRIAEFTT 1027
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIleLDQELRKAERELSKAEKNSLTETLKKEVKS 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1028 NLTEEEEKSKSLAKL------KNKHEAMITDLE----------ERLRREEKQ--------------RQELEKTRRKLEGD 1077
Cdd:TIGR00606 506 LQNEKADLDRKLRKLdqemeqLNHHTTTRTQMEmltkdkmdkdEQIRKIKSRhsdeltsllgyfpnKKQLEDWLHSKSKE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1078 STDLSDQIAELQAQIAEL---KMQLAKKEEELQAALARVEEeaaqKNMALKKIRELESQISELQEDLESERASRN----- 1149
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLeqnKNHINNELESKEEQLSSYED----KLFDVCGSQDEESDLERLKEEIEKSSKQRAmlaga 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1150 --------------------------KAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1203
Cdd:TIGR00606 662 tavysqfitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1204 HEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERgELANEVKVLLQGKGDSEHKRKKVEAQLQELQVkfN 1283
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERFQMELKDVERKIAQQAAKLQG--S 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1284 EGERVRTELADKVTKLQVELDNVTgllsqsdsksskltkdfsaleSQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1363
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVV---------------------SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIG 877
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1364 EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKtrlqqel 1443
Cdd:TIGR00606 878 TNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD---SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK------- 947
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1444 ddllvdldhqrqsacnlekkqKKFDQLLAEEKTISAKYAEERDRaeaEAREKETKALSLARALEEAMEQKaelERLNKQF 1523
Cdd:TIGR00606 948 ---------------------EKVKNIHGYMKDIENKIQDGKDD---YLKQKETELNTVNAQLEECEKHQ---EKINEDM 1000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1524 RTEMEDLMSSK--DDVGKSVHELEKSKRALEQQVEEMKTQLEEL-EDELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQ 1600
Cdd:TIGR00606 1001 RLMRQDIDTQKiqERWLQDNLTLRKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRN-HVLALGRQKG 1079
|
810 820 830
....*....|....*....|....*....|....*.
gi 2550219468 1601 SEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKL 1636
Cdd:TIGR00606 1080 YEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTEL 1115
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1347-1942 |
6.12e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.82 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1347 SLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKV 1426
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1427 AAYDKLEKTK--------------TRLQQELDDLLVDLDHQRQSACNLEKKQKKF-DQLLAEEKTIsakyaeerDRAEAE 1491
Cdd:TIGR04523 124 VELNKLEKQKkenkknidkflteiKKKEKELEKLNNKYNDLKKQKEELENELNLLeKEKLNIQKNI--------DKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1492 AREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQ---QVEEMKTQLEELEDE 1568
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQlkdEQNKIKKQLSEKQKE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1569 LQATEDAKLRLEVNLQAMKAQFErDLqgRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHID 1648
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEIS-DL--NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1649 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELaaaerakRQAQQERDELA 1728
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI-------KKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1729 DEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1808
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1809 KELKVKLQEMEGTVKSkYKASITALEAKIAQLEEQLDNetKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADK 1888
Cdd:TIGR04523 506 KELEEKVKDLTKKISS-LKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1889 ASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1942
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1063-1319 |
6.71e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1063 QRQELEKTRRKLEgdstDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEEAAQKNmalKKIRELESQISELQEDLe 1142
Cdd:COG4942 18 QADAAAEAEAELE----QLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALA---RRIRALEQELAALEAEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1143 serasrNKAEKQKRDLGEELEALKTELEDTLDstAAQQelRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEEL 1222
Cdd:COG4942 86 ------AELEKEIAELRAELEAQKEELAELLR--ALYR--LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1223 AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVE 1302
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*..
gi 2550219468 1303 LDNVTGLLSQSDSKSSK 1319
Cdd:COG4942 236 AAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1499-1742 |
9.33e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1499 ALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLR 1578
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1579 LEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAvAARKKLEMDLKDLEAHIDSANKNRDEAI 1658
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1659 KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1738
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
....
gi 2550219468 1739 ALAL 1742
Cdd:COG4942 254 KLPW 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1556-1944 |
1.02e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1556 EEMKTQLEELEDELQATEDAKLRLEVN-LQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELEDERKQRsmavAARK 1634
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNgLESELAELDEEI----ERYEEQREQARETRDEADEVLEEHEERR----EELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1635 KLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE 1714
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1715 RAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHA 1794
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1795 QKNENARQQLERQNKELKVKLQEMEGTVK---------------------------SKYKASITALEAKIAQLEEQLDnE 1847
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVE-E 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1848 TKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET 1927
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
410
....*....|....*..
gi 2550219468 1928 ADAMNREVSSLKNKLRR 1944
Cdd:PRK02224 574 VAELNSKLAELKERIES 590
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
891-1489 |
1.22e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.33 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 891 EMETLQSQLMA-EKL-QLQEQLQAETELCAEAEELRARLTA-----KKQELEEICHDLEARVEEEEERCQHLQAEKKKMQ 963
Cdd:COG4913 243 ALEDAREQIELlEPIrELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 964 QNIQELEEQLEEEESAR-QKLQLEKVTTEAKLKKLEEEQIILEDQ----NCKLAKEKKLLEDRIAEFTTNLTEEEEKSKS 1038
Cdd:COG4913 323 EELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1039 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAE-LQAQIAELK-----MQLAKKEEELQAALAR 1112
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPfvgelIEVRPEEERWRGAIER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1113 ----------VEEEAAQKnmALKKIRELesqisELQEDLESERASRNKAEKQKRDLGEelEALKTELEdtLDSTAAQQEL 1182
Cdd:COG4913 483 vlggfaltllVPPEHYAA--ALRWVNRL-----HLRGRLVYERVRTGLPDPERPRLDP--DSLAGKLD--FKPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1183 RSKREQEVNILKKTLEEEAKTHEAQIQEMRQ-KHSQAVEELAEQleqtKRVKANL------EKAKQTLENERGELANEVK 1255
Cdd:COG4913 552 EAELGRRFDYVCVDSPEELRRHPRAITRAGQvKGNGTRHEKDDR----RRIRSRYvlgfdnRAKLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1256 VLLQGKGDSEHKRKKVEAQLQELQ--VKFNEGERVRTELADKVTKLQVELDNvtglLSQSDSksskltkDFSALESQLQD 1333
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELER----LDASSD-------DLAALEEQLEE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1334 TQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADmkkKMEDSVGCLETAEEVKRKLQK 1413
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVERELRENLEE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1414 DLEGLSQRHEEkvaAYDKLEKTKTRLQQELDDLLV------------DLDHQRQSACNLEKKQKKFDQLLAEEKT----- 1476
Cdd:COG4913 774 RIDALRARLNR---AEEELERAMRAFNREWPAETAdldadleslpeyLALLDRLEEDGLPEYEERFKELLNENSIefvad 850
|
650
....*....|...
gi 2550219468 1477 ISAKYAEERDRAE 1489
Cdd:COG4913 851 LLSKLRRAIREIK 863
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1460-1945 |
3.18e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1460 LEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskdDVGK 1539
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1540 SVHELEKSKRALEQQVEEMKTQLEELED---ELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREME 1616
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1617 AELEDERKQRSMAVAARKKLEMDLKDLEA-HIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN--- 1692
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENeLEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1693 ----EKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQgNTEL 1768
Cdd:COG4717 286 lallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1769 INDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKA-SITALEAKIAQLEEQLDNE 1847
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1848 TKERQAACKQVRRTEKKLKDVLLQvdderrnaeqykDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET 1927
Cdd:COG4717 445 EEELEELREELAELEAELEQLEED------------GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
490
....*....|....*....
gi 2550219468 1928 -ADAMNREVSSLKNKLRRG 1945
Cdd:COG4717 513 rLPPVLERASEYFSRLTDG 531
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1128-1936 |
3.88e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1128 RELESQISELQEDLESERASRNKAEK--QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAkthE 1205
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE---L 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1206 AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER-GELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNE 1284
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1285 GERVRTELADkvtklqveldNVTGLLSQSDSKSSKLTKDFSALESQLQDTQEllqeenrqklslstKLKQVEDEKNSfre 1364
Cdd:COG4913 378 SAEEFAALRA----------EAAALLEALEEELEALEEALAEAEAALRDLRR--------------ELRELEAEIAS--- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1365 qleeeeeakhnLEKQIATLHAQVADMKKKMEDSVGCLET-----AE--EVK---RKLQKDLEGL----------SQRHEE 1424
Cdd:COG4913 431 -----------LERRKSNIPARLLALRDALAEALGLDEAelpfvGEliEVRpeeERWRGAIERVlggfaltllvPPEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1425 KVA-AYDKLeKTKTRLQqelddllvdldhqrqsacnlekkqkkfdqllaeektisakYAEERDRAEAEAREKETKAlSLA 1503
Cdd:COG4913 500 AALrWVNRL-HLRGRLV----------------------------------------YERVRTGLPDPERPRLDPD-SLA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1504 RaleeameqkaELERLNKQFRTEMEDLMSSKDDVGK--SVHELEKSKRALeqqveemktqleeledelqaTEDAKLRLEv 1581
Cdd:COG4913 538 G----------KLDFKPHPFRAWLEAELGRRFDYVCvdSPEELRRHPRAI--------------------TRAGQVKGN- 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1582 nlqamKAQFERDLQGRDEQ-------SEEKKKQLVRQVREMEAELEDerkqrsmAVAARKKLEMDLKDLEAhidsanknR 1654
Cdd:COG4913 587 -----GTRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAE-------AEERLEALEAELDALQE--------R 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1655 DEAIKQLRKLQAQMKDcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANs 1734
Cdd:COG4913 647 REALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ- 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1735 sgkgalALEEKRRLEARIAQLEEELEEEQgnTELINDRLKKANLQidqintdlNLERSHAQKNENARQQLERQNKELKVK 1814
Cdd:COG4913 725 ------AEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGD--------AVERELRENLEERIDALRARLNRAEEE 788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1815 LQEMEGTVKSKYKASITALEAKIAQLEE------QLDNE---TKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQykdq 1885
Cdd:COG4913 789 LERAMRAFNREWPAETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREIKE---- 864
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1886 adkastRLKQLKRQLEEAE---------EEAQRANASRRKLQRELEDATETADAMNREVS 1936
Cdd:COG4913 865 ------RIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1234-1720 |
4.67e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1234 ANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQS 1313
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1314 DsksskLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEdeknsfreqleeeeeakhNLEKQIATLHAQVADMKKK 1393
Cdd:COG4717 129 P-----LYQELEALEAELAELPERLEELEERLEELRELEEELE------------------ELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1394 MEdsvgcLETAEEVKRkLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQrqsacNLEKKQKKFDQLLAE 1473
Cdd:COG4717 186 LS-----LATEEELQD-LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-----ALEERLKEARLLLLI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1474 EKTISAKYAEERDRAEAEAREKETKALSLA----------RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE 1543
Cdd:COG4717 255 AAALLALLGLGGSLLSLILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1544 LEKSKRALEQQVEEMKTQLEELEDELQ--ATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKkQLVRQVREMEAELED 1621
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1622 ERK--QRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCM--RELDDTRASREEILAQAKENEKKLK 1697
Cdd:COG4717 414 LLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWA 493
|
490 500
....*....|....*....|...
gi 2550219468 1698 SMEAEMIQLQEELAAAERAKRQA 1720
Cdd:COG4717 494 ALKLALELLEEAREEYREERLPP 516
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1291-1934 |
5.69e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.94 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1291 ELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNsfreqlEEEE 1370
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN------GELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1371 EAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQ---ELDDLL 1447
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSkikEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1448 VDLDHQRQSAcnleKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEA--------------MEQK 1513
Cdd:pfam12128 392 IAGIKDKLAK----IREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1514 AELERLNK------QFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQA---TEDAKLRLEVNL- 1583
Cdd:pfam12128 468 NFDERIERareeqeAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagTLLHFLRKEAPDw 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1584 -QAMKAQFERDLQGR-DEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQL 1661
Cdd:pfam12128 548 eQSIGKVISPELLHRtDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1662 RKLQAQMKDCMRELDDTRASreeiLAQAKENEKKLKS-MEAEMIQLQEelaAAERAKRQAQQERDELADEIANSSGKGAL 1740
Cdd:pfam12128 628 VQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1741 ALEEKRR--LEARIAQLEEELeeeqgntELINDRlkkaNLQIDQINTDLNLERSHAQKNENArqqLERQNK-ELKVKlqE 1817
Cdd:pfam12128 701 WLEEQKEqkREARTEKQAYWQ-------VVEGAL----DAQLALLKAAIAARRSGAKAELKA---LETWYKrDLASL--G 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1818 MEGTVKSKYKASITALEAKIAQLE---------EQLDNET--KERQAACKQVRRTEKKLKDvlLQVDDERRNAEqykdqa 1886
Cdd:pfam12128 765 VDPDVIAKLKREIRTLERKIERIAvrrqevlryFDWYQETwlQRRPRLATQLSNIERAISE--LQQQLARLIAD------ 836
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2550219468 1887 dkASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNRE 1934
Cdd:pfam12128 837 --TKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSE 882
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
980-1532 |
6.09e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.74 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 980 RQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKL------------LEDRIAEF---TTNLTEE-EEKSKSLAKLK 1043
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknksLESQISELkkqNNQLKDNiEKKQQEINEKT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1044 ---NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlaKKEEELQAALARVEEEAAQK 1120
Cdd:TIGR04523 246 teiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1121 NMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTL--- 1197
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqnq 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1198 EEEAKTHEAQIQEMRQKH---SQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1274
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1275 LQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKlslstKLKQ 1354
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL-----KKEN 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1355 VEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEK 1434
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1435 TKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKA 1514
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEK 718
|
570
....*....|....*...
gi 2550219468 1515 ELERLnKQFRTEMEDLMS 1532
Cdd:TIGR04523 719 ELKKL-DEFSKELENIIK 735
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1471-1944 |
6.25e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1471 LAEEKTISAKYAEERDRAEA----------EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKS 1540
Cdd:PRK02224 215 LAELDEEIERYEEQREQAREtrdeadevleEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1541 VHEL-------EKSKRALEQQVEEMKTQLEELEDELqatEDAKLRLevnlQAMKAQFERdLQGRDEQSEEKKKQLVRQVR 1613
Cdd:PRK02224 295 RDDLlaeagldDADAEAVEARREELEDRDEELRDRL---EECRVAA----QAHNEEAES-LREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1614 EMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENE 1693
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1694 KKLKSMEA-EMIQLQEELAAAERAKrQAQQERDELADEIANssgkgalALEEKRRLEARIAQLEEELEEEQGnTELINDR 1772
Cdd:PRK02224 447 ALLEAGKCpECGQPVEGSPHVETIE-EDRERVEELEAELED-------LEEEVEEVEERLERAEDLVEAEDR-IERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1773 LKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKAsITALEAKIAQLEEQLDNETK--- 1849
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE-VAELNSKLAELKERIESLERirt 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1850 ---ERQAACKQVRRTEKKLKDvLLQVDDERRnaeqykDQADKASTRLKQLKRQ-----LEEAEEEAQRANASRRKLQREL 1921
Cdd:PRK02224 597 llaAIADAEDEIERLREKREA-LAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKL 669
|
490 500
....*....|....*....|...
gi 2550219468 1922 EDATETADAMNREVSSLKNKLRR 1944
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEE 692
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1464-1867 |
8.44e-11 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 66.84 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1464 QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE 1543
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1544 LEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKaqferdlqgrdeqseEKKKQLVRQVREMEAELEDER 1623
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1624 KQRSMAVAARKKLEMDLKDLEAHIDsankNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1703
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1704 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGA---LALEEKRrleariAQLEEELEEEQGNTELINDRLKKANLQI 1780
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAdasLALREGR------ARWAQERETLQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1781 DQINTDLNLERSHAQK-----------NENARQQLERQNKELKVKLQEMEGTvKSKYKASITALEAKIAQLEEQLDNET- 1848
Cdd:pfam07888 328 QRLEERLQEERMEREKlevelgrekdcNRVQLSESRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVAd 406
|
410 420
....*....|....*....|
gi 2550219468 1849 -KERQAACKQVRRTEKKLKD 1867
Cdd:pfam07888 407 aKWSEAALTSTERPDSPLSD 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1351-1947 |
1.38e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1351 KLKQVEDEKNSFREQLEEEEEAKHNLEKQIATlhaqvadMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEkvaayd 1430
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKE-------KEKELEEVLREINEISSELPELREELEKLEKEVKE------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1431 kLEKTKTRLqqelddllvdldhqrqsacnlEKKQKKFDQLLAEEKTISAKYAEERDRAEaEAREKETKALSLARALEEAM 1510
Cdd:PRK03918 233 -LEELKEEI---------------------EELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1511 EQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQV---EEMKTQLEELEDELQATEDAKLRLEVNLQAmk 1587
Cdd:PRK03918 290 EKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL-- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1588 aqFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsmavaARKKLEMDLKDLEAHI---DSANKNRDEAIKQLRKL 1664
Cdd:PRK03918 364 --YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-------AKEEIEEEISKITARIgelKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1665 QAQMKDCMRELDDTRasREEILAqakENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERD---------ELADEIANSS 1735
Cdd:PRK03918 435 KGKCPVCGRELTEEH--RKELLE---EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliklkELAEQLKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1736 GK-GALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN----KE 1810
Cdd:PRK03918 510 EKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEE 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1811 LKVKLQEMEGTVK-----SKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDE---------- 1875
Cdd:PRK03918 590 LEERLKELEPFYNeylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeyeelreeyl 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1876 ---------RRNAEQYKDQADKASTRLKQLKRQLeeaeeeaqranASRRKLQRELED---ATETADAMNREVSSLKNKLR 1943
Cdd:PRK03918 670 elsrelaglRAELEELEKRREEIKKTLEKLKEEL-----------EEREKAKKELEKlekALERVEELREKVKKYKALLK 738
|
....
gi 2550219468 1944 RGDL 1947
Cdd:PRK03918 739 ERAL 742
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1037-1872 |
1.39e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1037 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDL--SDQIAELQAQIAELKMQLAKKEEELQAALARVE 1114
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqQEKIERYQADLEELEERLEEQNEVVEEADEQQE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1115 EEAAQKNMALKKIRELESQISELQE--DLESERASRNKAEKQkrdLGEELEALKTELEDTLDSTAA-QQELRSKREQEVN 1191
Cdd:PRK04863 380 ENEARAEAAEEEVDELKSQLADYQQalDVQQTRAIQYQQAVQ---ALERAKQLCGLPDLTADNAEDwLEEFQAKEQEATE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1192 ILkktLEEEAKTHEAqiQEMRQKHSQAVEELAEQLEQTKRVKANlEKAKQTLenerGELANEVKVLLQGKGdsehkrkkV 1271
Cdd:PRK04863 457 EL---LSLEQKLSVA--QAAHSQFEQAYQLVRKIAGEVSRSEAW-DVARELL----RRLREQRHLAEQLQQ--------L 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1272 EAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdsksskltkDFSALESQLQDTQELLQEENRQKLSLSTK 1351
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDED---------------ELEQLQEELEARLESLSESVSEARERRMA 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1352 LKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKvaayDK 1431
Cdd:PRK04863 584 LRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEE----------FEDSQDVTEYMQQLLERERELTVER----DE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1432 LEKTKTRLQQElddllVDLDHQRQSAcNLEKKQKKFDQ----LLAEektISAKYAEErDRAEAEAREKETKALSLARALE 1507
Cdd:PRK04863 650 LAARKQALDEE-----IERLSQPGGS-EDPRLNALAERfggvLLSE---IYDDVSLE-DAPYFSALYGPARHAIVVPDLS 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1508 EAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEKS----------------------KRALEQQVEEMK 1559
Cdd:PRK04863 720 DAAEQLAGLEDC-------PEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLR 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1560 TQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED----ERKQRSMA 1629
Cdd:PRK04863 793 AEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqEQQQRSQL 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1630 VAARKKLEMdlkdLEAHIDSANKNRDEA-IKQLRKLQAQMKDCmreLDDTR--ASREEILAQAKENEKKLKSMEAEMIQL 1706
Cdd:PRK04863 868 EQAKEGLSA----LNRLLPRLNLLADETlADRVEEIREQLDEA---EEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQL 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1707 QEELAAAERAKRQAQQERDELADEIANssgKGALALEEKRRLEAriaqleeeleEEQGNTELINDRLKKANLQIDQINTD 1786
Cdd:PRK04863 941 KQDYQQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMLA----------KNSDLNEKLRQRLEQAEQERTRAREQ 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1787 LNLERS-HAQKNE------NARQQLERQNKELKVKLQEM-----EG------TVKSKYKASITALEAKIAQLEEQLDNET 1848
Cdd:PRK04863 1008 LRQAQAqLAQYNQvlaslkSSYDAKRQMLQELKQELQDLgvpadSGaeerarARRDELHARLSANRSRRNQLEKQLTFCE 1087
|
890 900
....*....|....*....|....
gi 2550219468 1849 KERQAACKQVRRTEKKLKDVLLQV 1872
Cdd:PRK04863 1088 AEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1057-1926 |
2.23e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.13 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1057 LRREEKQRQELEKTRRKLEGDSTDLSdqiaELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKN---MALKKIREL 1130
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLV----EMARELAELNEAESDLEQDYQAAsdhLNLVQTALRQQEkieRYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1131 ESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE---------EEA 1201
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglpdltaDNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1202 KTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL-----ENERGELANEVKVLLQgkgdsEHKRKKVEA-QL 1275
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVrkiagEVSRSEAWDVARELLR-----RLREQRHLAeQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1276 QELQVKFNEGERvRTELADKVTKLQVELDNVTGLLSQSDSksskltkDFSALESQLQDTQELLQEENRQKLSLSTKLKQV 1355
Cdd:PRK04863 516 QQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1356 EDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKvaayDKLEKT 1435
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLAAQDALARLREQSGEE----------FEDSQDVTEYMQQLLERERELTVER----DELAAR 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1436 KTRLQQELDDLlvdldHQRQSAcNLEKKQKKFDQ----LLAEektISAKYAEErDRAEAEAREKETKALSLARALEEAME 1511
Cdd:PRK04863 654 KQALDEEIERL-----SQPGGS-EDPRLNALAERfggvLLSE---IYDDVSLE-DAPYFSALYGPARHAIVVPDLSDAAE 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1512 QKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEKS----------------------KRALEQQVEEMKTQLE 1563
Cdd:PRK04863 724 QLAGLEDC-------PEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAERE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1564 ELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED----ERKQRSMAVAAR 1633
Cdd:PRK04863 797 ELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqEQQQRSQLEQAK 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1634 KKLEMdlkdLEAHIDSANKNRDEA-IKQLRKLQAQMKDCmreLDDTR--ASREEILAQAKENEKKLKSMEAEMIQLQEEL 1710
Cdd:PRK04863 872 EGLSA----LNRLLPRLNLLADETlADRVEEIREQLDEA---EEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDY 944
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1711 AAAERAKRQAQQERDELADEIANssgKGALALEEKRRLEAriaqleeeleEEQGNTELINDRLKKANLQIDQintdlnle 1790
Cdd:PRK04863 945 QQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMLA----------KNSDLNEKLRQRLEQAEQERTR-------- 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1791 rshaqknenARQQLERQNKELKVKLQemegtVKSKYKASITALEAKIAQLEEQLDNET-KERQAACKQVRRTEKKLKDVL 1869
Cdd:PRK04863 1004 ---------AREQLRQAQAQLAQYNQ-----VLASLKSSYDAKRQMLQELKQELQDLGvPADSGAEERARARRDELHARL 1069
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1870 LQvDDERRNaeqykdqadkastrlkQLKRQLEEAEEEAQRANASRRKLQRELEDATE 1926
Cdd:PRK04863 1070 SA-NRSRRN----------------QLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1269-1941 |
2.50e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1269 KKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDtqellqeENRQKLSL 1348
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN-------DKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1349 STKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAA 1428
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1429 YDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLaralEE 1508
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL----EQ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1509 AMEQKAELERLNKQFRTEMEDLMSSKD-DVGKSVHElekskraleqQVEEMKTQLEELEDELQATEDAKLRLEVNLqamk 1587
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEqDWNKELKS----------ELKNQEKKLEEIQNQISQNNKIISQLNEQI---- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1588 AQFERDLQGRDEQSEEKKKQLvrqvREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSA---NKNRDEAIKQL--- 1661
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQREL----EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklNQQKDEQIKKLqqe 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1662 -RKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGAL 1740
Cdd:TIGR04523 421 kELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1741 ALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNlERSHAQKNENARQQLERQNKELkvklqemeg 1820
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN-KDDFELKKENLEKEIDEKNKEI--------- 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1821 tvkSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKdvllqvdderrnaeqykdqadkastrlkQLKRQL 1900
Cdd:TIGR04523 571 ---EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS----------------------------SLEKEL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2550219468 1901 EEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1941
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1707-1952 |
3.59e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1707 QEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTD 1786
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1787 LNLERSHAQKNENARQQLERQNK-ELKVKLQEMEGTVKSK--YKASITALEAKIAQLEEQLDNETKERQaackQVRRTEK 1863
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRA----ELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1864 KLKDVLLQVDDERRNAEQYKDQADKAstrLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLR 1943
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
....*....
gi 2550219468 1944 RGDLPFVVP 1952
Cdd:COG4942 252 KGKLPWPVS 260
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
875-1391 |
4.34e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.13 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 875 LVKVREKqlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTakkQELEEICHDLEARVEEEEERCQH 954
Cdd:pfam05483 246 LIQITEK----ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEED 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 955 LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeqiILEDQNCKLAKEkkllEDRIAEFTTNLTEEEE 1034
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKN----EDQLKIITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1035 KSKSLAKLKNKHEAMITDLEERLRREEK---QRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL----------AK 1101
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseehyLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1102 KEEELQAALARVE----EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALK---TELEDTLD 1174
Cdd:pfam05483 472 EVEDLKTELEKEKlkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekeMNLRDELE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1175 STaaQQELRSKREQ--------EVNILKKTLEEEAKTHEAQIQEMR--------QKHSQAVEELAEQLEQTKRVKANLEK 1238
Cdd:pfam05483 552 SV--REEFIQKGDEvkckldksEENARSIEYEVLKKEKQMKILENKcnnlkkqiENKNKNIEELHQENKALKKKGSAENK 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1239 AKQTLENERGELANEVKVLLQGKGD-SEHKRKKVEAQLQELQVKFNEGERVRTeLADKVTKLQVELD-----NVTGLLSQ 1312
Cdd:pfam05483 630 QLNAYEIKVNKLELELASAKQKFEEiIDNYQKEIEDKKISEEKLLEEVEKAKA-IADEAVKLQKEIDkrcqhKIAEMVAL 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550219468 1313 SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMK 1391
Cdd:pfam05483 709 MEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
27-72 |
5.95e-10 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 56.28 E-value: 5.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2550219468 27 AAKKLVWVPSDKSGFEPASLKEEVGEEAIVELvENGKKVKVNKDDI 72
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1235-1889 |
6.10e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.27 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1235 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSD 1314
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1315 SKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK- 1393
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1394 --MEDSVGCLETAEEVKRKLQKDLEGL----SQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKF 1467
Cdd:TIGR04523 197 lkLELLLSNLKKKIQKNKSLESQISELkkqnNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1468 DQllAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVG---KSVHEL 1544
Cdd:TIGR04523 277 EQ--NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkKELTNS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1545 EKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFE------RDLQGRDEQSEEKKKQLVRQVREMEAE 1618
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQnqeklnQQKDEQIKKLQQEKELLEKEIERLKET 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1619 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKS 1698
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1699 MEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalaleekrrleariaqleeeleeeqgntelINDRLKKANL 1778
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNK-----------------------------------DDFELKKENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1779 QIDQINTDLNLERSHAQKNEnarqqLERQNKELKVKLQEmegtvkskYKASITALEAKIAQLEEQLDNETKERQAACKQV 1858
Cdd:TIGR04523 560 EKEIDEKNKEIEELKQTQKS-----LKKKQEEKQELIDQ--------KEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
650 660 670
....*....|....*....|....*....|.
gi 2550219468 1859 RRTEKKLKDVLLQVDDERRNAEQYKDQADKA 1889
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
880-1475 |
9.09e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.97 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 880 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEK 959
Cdd:pfam05483 201 ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 960 KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKlledriaeftTNLTEEEEKSKSL 1039
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE----------AQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1040 AKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSDQIAELQaQIAELKMQLAKKEEELQAALARVEEEAAQ 1119
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSELE-EMTKFKNNKEVELEELKKILAEDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1120 KNMALKKIRELESQISELQEDLESErasrnkaEKQKRDLGEELEALKTELEDTLDS-----TAAQQELRSKREQEVNILK 1194
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELIFLLQAR-------EKEIHDLEIQLTAIKTSEEHYLKEvedlkTELEKEKLKNIELTAHCDK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1195 KTLEEEAKTHEAQIQEMRQKHSQavEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1274
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQ--EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1275 LQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQ------DTQELLQEENRQKLS- 1347
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayeikvNKLELELASAKQKFEe 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1348 -LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKL----QKDLEGLSQRH 1422
Cdd:pfam05483 655 iIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIieerDSELGLYKNKE 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 1423 EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 1475
Cdd:pfam05483 735 QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
953-1281 |
1.54e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.22 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 953 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKleEEQIILEDQNCKLAKEKKLleDRIaefttnltEE 1032
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMEREREL--ERI--------RQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1033 EEKSKSLAKLKNKHEAM----ITDLE----ERLRREEKQRQELEKTRRKlegdSTDLSDQIAELQAQIAELKMQLAKKEE 1104
Cdd:pfam17380 356 EERKRELERIRQEEIAMeisrMRELErlqmERQQKNERVRQELEAARKV----KILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1105 ELQAALARVEEEAAQKnmaLKKIRELE----SQISELQEDLESERASRNKAEKQKRD--LGEEL--EALKTELEDTLDST 1176
Cdd:pfam17380 432 ARQREVRRLEEERARE---MERVRLEEqerqQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQrrKILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1177 AAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEkakqTLENERgELANEVKv 1256
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE----AMERER-EMMRQIV- 582
|
330 340
....*....|....*....|....*
gi 2550219468 1257 llqgkgDSEHKRKKVEAQLQELQVK 1281
Cdd:pfam17380 583 ------ESEKARAEYEATTPITTIK 601
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1039-1652 |
2.42e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 62.45 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1039 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAA 1118
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1119 QKNMALKKIRELESQISELQEDLES--ERASRNKAEKQKRDLgeELEALKTELEDTLDstaaQQELRSKREQEVNILKKT 1196
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISClkNELSELRRQIQRAEL--ELQSTNSELEELQE----RLDLLKAKASEAEQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1197 LE---EEAKTHEAQIQEMRQKHSQAVEELAEqleqTKRVKANLEKAKqTLENERGELANEVKVLLQGKGDSEhkrkKVEA 1273
Cdd:pfam05557 158 LEkqqSSLAEAEQRIKELEFEIQSQEQDSEI----VKNSKSELARIP-ELEKELERLREHNKHLNENIENKL----LLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1274 QLQELQVKFNEGERVRTELADkvtkLQVELdnvtgllsqsdsksSKLTKDFSALESQLQDTQELLqeenRQKLSLSTKLK 1353
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAAT----LELEK--------------EKLEQELQSWVKLAQDTGLNL----RSPEDLSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1354 QVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHE---EKVAAYD 1430
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyrAILESYD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1431 K-LEKTKTRLQqelddllvdldhqrqsacnLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALeEA 1509
Cdd:pfam05557 367 KeLTMSNYSPQ-------------------LLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL-QA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1510 MEQKAELErlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELedELQATEDAK----LRLEVNLQA 1585
Cdd:pfam05557 427 LRQQESLA--------DPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR--CLQGDYDPKktkvLHLSMNPAA 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1586 MKAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDerkQRSMAVAARKKLEMDLKDLEAHIDSANK 1652
Cdd:pfam05557 497 EAYQQRKNQL---EKLQAEIERLKRLLKKLEDDLEQ---VLRLPETTSTMNFKEVLDLRKELESAEL 557
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1081-1719 |
2.43e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.53 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1081 LSDQIAELQAQIAELKMQLAKKEEELQAALARVE---EEAAQKNMALKKirELESQISELQEdleserasrnkaekQKRD 1157
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKtfwSPELKKERALRK--EEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1158 LGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAvEELAEQLEQTKRVKANLE 1237
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEH-ERQAKELFLLRKTLEEME 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1238 ----KAKQTLeNERGELANEVKVLLQGKG--------DSEHKRKKVEAQLQ------ELQVKFNEGERVRTELADKvTKL 1299
Cdd:pfam10174 144 lrieTQKQTL-GARDESIKKLLEMLQSKGlpkksgeeDWERTRRIAEAEMQlghlevLLDQKEKENIHLREELHRR-NQL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1300 QVELDNVTGL---LSQSDSKSSKLTKDFSALESQLQ--DTQELLQEENRQKlslstKLKQVEDEKNSFR------EQLEE 1368
Cdd:pfam10174 222 QPDPAKTKALqtvIEMKDTKISSLERNIRDLEDEVQmlKTNGLLHTEDREE-----EIKQMEVYKSHSKfmknkiDQLKQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1369 EEEAKHN----LEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELD 1444
Cdd:pfam10174 297 ELSKKESellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1445 DLLVDLDHQRQSACNLEKK----QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLArALEEAMEQKAE-LERL 1519
Cdd:pfam10174 377 TLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1520 NKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ------ATEDAKLR-LEVNLQAMKAQFER 1592
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1593 dLQGRD------EQSEEKKKQLVRQVREMEAELEDERKQRSMAVA-------ARKKLEMDLKDLEAHIDSANKNRDEAIK 1659
Cdd:pfam10174 536 -LENQLkkahnaEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAeverllgILREVENEKNDKDKKIAELESLTLRQMK 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1660 QLRKLQAQMKDCMRELddtRASREEILAQAKENEKKLKSMEAEmIQLQEELAAAERAKRQ 1719
Cdd:pfam10174 615 EQNKKVANIKHGQQEM---KKKGAQLLEEARRREDNLADNSQQ-LQLEELMGALEKTRQE 670
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1084-1244 |
2.52e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 59.94 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1084 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeELE 1163
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1164 ALKTELEdtldSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL 1243
Cdd:COG1579 93 ALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
.
gi 2550219468 1244 E 1244
Cdd:COG1579 169 A 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
880-1247 |
2.81e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 880 EKQLAAENRLTEMETLQSQLMAEKLQ---LQEQLQAETELCAEAEELRARLTAKKQELEEICHDL----EARVEEEEERC 952
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 953 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTtEAKLKKLEEEQIILEDQN--CKLAKEKKLLEDRIAEFTTNLT 1030
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLLLLIAAalLALLGLGGSLLSLILTIAGVLF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1031 EEEE----KSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST-------DLSDQIAELQAQIAEL---- 1095
Cdd:COG4717 281 LVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlspeellELLDRIEELQELLREAeele 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1096 -KMQLAKKEEELQAALARV----EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDlgEELEALKTELE 1170
Cdd:COG4717 361 eELQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1171 DTLDSTAAQQELRSKREQEVNILKKTLEEEAktheaQIQEMRQKHSQAVEELAEQLEQTKRVK---ANLEKAKQTLENER 1247
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDG-----ELAELLQELEELKAELRELAEEWAALKlalELLEEAREEYREER 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1552-1754 |
4.09e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1552 EQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVA 1631
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1632 ARKKLEMDLKDLEAHIDSanKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1711
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2550219468 1712 AAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1754
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
916-1146 |
4.52e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 916 LCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLK 995
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 996 KLEEEQIILEDQnckLAKEKKLLEDRIAEFTTNLTEEE-------EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELE 1068
Cdd:COG4942 87 ELEKEIAELRAE---LEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1069 KTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERA 1146
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1150-1867 |
5.40e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.28 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1150 KAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQE---MRQKHSQAVEELAEQL 1226
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnaTRHLCNLLKETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1227 EQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGER-VRTELADKVTKlqveldn 1305
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEeYKKEINDKEKQ------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1306 VTGLLSQSDSKSSKLtKDFSalesqlqdtqeLLQEENRQKLSlstklkQVEDEKNSFREQLEEEEEAKHNLEKQIAtlha 1385
Cdd:pfam05483 242 VSLLLIQITEKENKM-KDLT-----------FLLEESRDKAN------QLEEKTKLQDENLKELIEKKDHLTKELE---- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1386 qvaDMKKKMEDSVGCLETAEEvkrKLQKDLEGLSQRHEEKVAAYDKLEKTKTrlqqeldDLLVDLDHQRQSACNLEK--- 1462
Cdd:pfam05483 300 ---DIKMSLQRSMSTQKALEE---DLQIATKTICQLTEEKEAQMEELNKAKA-------AHSFVVTEFEATTCSLEEllr 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1463 -KQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARaLEEAMEQKAELERLNKQFRTEMEDLMSSKDDV---- 1537
Cdd:pfam05483 367 tEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE-LKKILAEDEKLLDEKKQFEKIAEELKGKEQELifll 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1538 ---GKSVHELE-------KSKRALEQQVEEMKTQLEELE---DELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEK 1604
Cdd:pfam05483 446 qarEKEIHDLEiqltaikTSEEHYLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1605 KKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREE 1684
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1685 ILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEEleeeqg 1764
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEK------ 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1765 nTELINDRLKKANLQID-----QINTDLNLERSHAQKNENARQQLERQNKELKVKLQEmEGTVKSKYKASITALEAKIAQ 1839
Cdd:pfam05483 680 -AKAIADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE-QSSAKAALEIELSNIKAELLS 757
|
730 740
....*....|....*....|....*...
gi 2550219468 1840 LEEQLDNETKERQAACKQVRRTEKKLKD 1867
Cdd:pfam05483 758 LKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1074-1302 |
6.30e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.19 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1074 LEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR--VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKA 1151
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1152 EKQkrdLGEELEALKTELEDTLDSTAAQQelRSKREQEVNILKKTLEEE---AKTHEAQIQEMRQKHSQAVEELAEQLEQ 1228
Cdd:COG3206 246 RAQ---LGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1229 TKRVkanLEKAKQTLENERGELANEVKVLlqgkgdsehkrKKVEAQLQELQVKFNEGERVRTELADKVTKLQVE 1302
Cdd:COG3206 321 ELEA---LQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1649-1892 |
7.80e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1649 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1728
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1729 DEIANSSGKGALALeekRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1808
Cdd:COG4942 97 AELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1809 KELKVKLQEMEgtvksKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADK 1888
Cdd:COG4942 174 AELEALLAELE-----EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 2550219468 1889 ASTR 1892
Cdd:COG4942 249 AALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1480-1954 |
8.10e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1480 KYAEERDRAEAEAREKET--KALSLARALEEAMEQKAELERLNKQfrtemedlmsskddvgksVHELEKSKRALEQQVEE 1557
Cdd:COG4913 259 ELAERYAAARERLAELEYlrAALRLWFAQRRLELLEAELEELRAE------------------LARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1558 MKTQLEELEDELQateDAKLRLEVNLQAMKAQFERDLQGRdeqsEEKKKQLVRQVREMEAELEDERKQrsmAVAARKKLE 1637
Cdd:COG4913 321 LREELDELEAQIR---GNGGDRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASAEE---FAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1638 MDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRAS-----------REEILAQAKENEKKLKSMeAEMIQL 1706
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRksniparllalRDALAEALGLDEAELPFV-GELIEV 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1707 QEELA----AAERAKRQAQQ-----ERDELAdeianssgkgALALEEKRRLEARIaqleeeleeeqgNTELINDRLKKAN 1777
Cdd:COG4913 470 RPEEErwrgAIERVLGGFALtllvpPEHYAA----------ALRWVNRLHLRGRL------------VYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1778 ---LQIDQINTDLNLERSHAQknENARQQLERQNKELKVK-LQEM---------EGTVKSKY------------------ 1826
Cdd:COG4913 528 rprLDPDSLAGKLDFKPHPFR--AWLEAELGRRFDYVCVDsPEELrrhpraitrAGQVKGNGtrhekddrrrirsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1827 ---KASITALEAKIAQLEEQLdNETKERQAACKQVRRTEKKLKDVLLQVDD-------------ERRNAEQYKDQADKAS 1890
Cdd:COG4913 606 fdnRAKLAALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASS 684
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1891 TRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGDLPFVVPRR 1954
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1083-1274 |
8.63e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1083 DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLEserASRNKAEKQKRDLGEEL 1162
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1163 EALK---------------TELEDTLDSTAAQQELRSKREQEVNILKKtLEEEAKTHEAQIQEMRQKHSQAVEELAEQLE 1227
Cdd:COG3883 93 RALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2550219468 1228 QTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1274
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1491-1938 |
8.67e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1491 EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ 1570
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1571 ATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKdLEAHID 1648
Cdd:PRK03918 225 KLEKEVKELEelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1649 SANKNRDEAIKQLRKLQAQMKDCMRELDDtrasREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK----------- 1717
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKakkeelerlkk 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1718 RQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTElindRLKKANLQIDQINTDLNLERSHAQKN 1797
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKCPVCGRELTEEHRKELLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1798 EnARQQLERQNKELKvKLQEMEgtvkSKYKASITALEAKIAQLEEQLdnetKERQAAcKQVRRTEKKLKDVLLQ-VDDER 1876
Cdd:PRK03918 456 E-YTAELKRIEKELK-EIEEKE----RKLRKELRELEKVLKKESELI----KLKELA-EQLKELEEKLKKYNLEeLEKKA 524
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 1877 RNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRanasRRKLQRELEDATETADAMNREVSSL 1938
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEEL 582
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1039-1200 |
9.08e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 58.01 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1039 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL--AKKEEELQAALARVEEE 1116
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1117 AAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtldstAAQQELRSKREQevniLKKT 1196
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE------AELEELEAEREE----LAAK 171
|
....
gi 2550219468 1197 LEEE 1200
Cdd:COG1579 172 IPPE 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1104-1571 |
1.16e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1104 EELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKR--DLGEELEALKTELEDT---LDSTAA 1178
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1179 QQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLl 1258
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1259 qgkgDSEHKRKKVEAQLQELQVKFNeGERVRTELADKVTKLQVELDNVTGLLSQSDS----KSSKLTKDFSALESQLQDT 1334
Cdd:COG4717 233 ----ENELEAAALEERLKEARLLLL-IAAALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1335 QELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAkhnlEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKD 1414
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDR----IEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1415 LEGLSQRHEEKvAAYDKLEKTKTRLQQelddllvdldhqrqsacnlekkqkkfdQLLAEEKTISAKYA-EERDRAEAEAR 1493
Cdd:COG4717 384 EEELRAALEQA-EEYQELKEELEELEE---------------------------QLEELLGELEELLEaLDEEELEEELE 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1494 EKETKALSLARALEEAMEQKAELErlnkqfrTEMEDLMSSkddvgksvHELEKskraLEQQVEEMKTQLEELEDELQA 1571
Cdd:COG4717 436 ELEEELEELEEELEELREELAELE-------AELEQLEED--------GELAE----LLQELEELKAELRELAEEWAA 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1413-1810 |
1.91e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1413 KDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDqLLAEEKTISAKYAEERDRAEA-E 1491
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1492 AREKETKAL--SLARALEEAMEQKAELERLNKQF----RTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 1565
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1566 EDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQ-------------LVRQVREMEAELEDERKQRSMAVAA 1632
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1633 RKKLE-MDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASReEILAQAKENEKKLKSMEAEMIQLQEELA 1711
Cdd:COG4717 313 LEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1712 AAERAKRQAQQERDELADEIANSSG--KGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNL 1789
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|.
gi 2550219468 1790 ERSHAQKnENARQQLERQNKE 1810
Cdd:COG4717 472 AELLQEL-EELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1344-1578 |
2.00e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1344 QKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHE 1423
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1424 EKVAAYDKLEKTktrLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLA 1503
Cdd:COG4942 101 AQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1504 RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLR 1578
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1047-1251 |
2.04e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1047 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1126
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1127 IRELESQISELQEDLESE-------RASR-NKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE 1198
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldRLSAlSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 1199 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA 1251
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
978-1244 |
2.13e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 58.54 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 978 SARQKLQLEKVTTEAKLK-------KLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMI 1050
Cdd:pfam19220 41 RELPQAKSRLLELEALLAqeraaygKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1051 TDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIREL 1130
Cdd:pfam19220 121 EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1131 ESQ-------ISELQEDLESERASRNKAEKQkrdLGEELEALKTELE------DTLDSTAA--QQELRSKREQEVNILKK 1195
Cdd:pfam19220 201 ETQldatrarLRALEGQLAAEQAERERAEAQ---LEEAVEAHRAERAslrmklEALTARAAatEQLLAEARNQLRDRDEA 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2550219468 1196 TLEEEAKTHEAQIqEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQTLE 1244
Cdd:pfam19220 278 IRAAERRLKEASI-ERDTLERR-LAGLEADLERRTQQFQEMQRARAELE 324
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1464-1926 |
2.71e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1464 QKKFDQLLAEEKTISAkyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERlnKQFRTEMEDLMSSKDDVGKSVHE 1543
Cdd:TIGR00606 172 KQKFDEIFSATRYIKA---LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR--DQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1544 LEKSKRALeQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDER 1623
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1624 KQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLK--SMEA 1701
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVieRQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1702 EMIQLQEELAAAERAKRQAQQERDELADEIansSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKanlqiD 1781
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEK---KGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL-----D 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1782 QINTDLNLERSHAQKNENARQQLERqnkELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRT 1861
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKE---VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1862 EKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATE 1926
Cdd:TIGR00606 555 KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
905-1121 |
2.77e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 905 QLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEES--ARQK 982
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAelEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 983 LQLEKVTTEA-KLKKLEEEQIILEDQNCK--------LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDL 1053
Cdd:COG4942 104 EELAELLRALyRLGRQPPLALLLSPEDFLdavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1054 EERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKN 1121
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
879-1546 |
3.38e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 58.68 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 879 REKQLAAENRlTEMETLQSQLMA---EKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 955
Cdd:pfam10174 43 KERALRKEEA-ARISVLKEQYRVtqeENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 956 QAEKKK--------------MQQNIQELEEQLEEEESARQKLqLEKVTTEAKLKKLEEE------------------QII 1003
Cdd:pfam10174 122 QSEHERqakelfllrktleeMELRIETQKQTLGARDESIKKL-LEMLQSKGLPKKSGEEdwertrriaeaemqlghlEVL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1004 LEDQNCKLAKEKKLLEDRiaeftTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSD 1083
Cdd:pfam10174 201 LDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1084 QIAELQA----------QIAELKMQLAKKEEELQAALARVEE------------EAAQKNMALKKIRE--LESQISELQE 1139
Cdd:pfam10174 273 EIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETltnqnsdckqhiEVLKESLTAKEQRAaiLQTEVDALRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1140 DLESERASRNKAEKQKRDLGEELEALKTELEDTLDstaaqqeLRSKREQEVNILKKTLE---EEAKTHEAQIQEMRqkhs 1216
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKD-------MLDVKERKINVLQKKIEnlqEQLRDKDKQLAGLK---- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1217 QAVEELAEQLEQTKRVKANLEKA----KQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTEL 1292
Cdd:pfam10174 422 ERVKSLQTDSSNTDTALTTLEEAlsekERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1293 ADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQElLQEENRQKLSLSTKLKQVEDEKNSFREQ------- 1365
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQEVARYKEEsgkaqae 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1366 -------LEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKlqKDLEGLSQRHEEKVAAYDKlektktR 1438
Cdd:pfam10174 581 verllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK--KGAQLLEEARRREDNLADN------S 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1439 LQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALsLArALEEAMEQKAELER 1518
Cdd:pfam10174 653 QQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL-LA-AISEKDANIALLEL 730
|
730 740
....*....|....*....|....*...
gi 2550219468 1519 LNKQFRTEMEDLMSSKDDVGKSVHELEK 1546
Cdd:pfam10174 731 SSSKKKKTQEEVMALKREKDRLVHQLKQ 758
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
877-1143 |
3.74e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 877 KVREKQLAAE-NRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEarvEEEEERCQHL 955
Cdd:pfam17380 364 RIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRL 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 956 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNcklakeKKLLEDRIAEFTTNLTEEEEK 1035
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR------RKILEKELEERKQAMIEEERK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1036 SKSLAKLKNKHEAMITDLEERLRREEKQRQELE-KTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQaalaRVE 1114
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKA----RAE 590
|
250 260 270
....*....|....*....|....*....|
gi 2550219468 1115 EEAAQKNMALKKIreLESQISELQ-EDLES 1143
Cdd:pfam17380 591 YEATTPITTIKPI--YRPRISEYQpPDVES 618
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1543-1944 |
4.16e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALE----QQVEEMKTQLEELEDELQATEDAKLRLevnlqamkaqfeRDLQGRDEQSEEKKKQLVRQVREMEAE 1618
Cdd:COG4717 50 RLEKEADELFkpqgRKPELNLKELKELEEELKEAEEKEEEY------------AELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1619 LE--DERKQRSMAVAARKKLEMDLKDLEAHIDSAnknrDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAK-ENEKK 1695
Cdd:COG4717 118 LEklEKLLQLLPLYQELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1696 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR-----IAQLEEELEEEQGNTELIN 1770
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1771 DRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKY------KASITALEAKIAQLEEQL 1844
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlppdlsPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1845 DNETKERQAACKQVRRTEKK--LKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQR--ANASRRKLQRE 1920
Cdd:COG4717 354 REAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEE 433
|
410 420
....*....|....*....|....
gi 2550219468 1921 LEDATETADAMNREVSSLKNKLRR 1944
Cdd:COG4717 434 LEELEEELEELEEELEELREELAE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1206-1428 |
4.94e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1206 AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFneg 1285
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1286 ERVRTELADKVTKLQV--ELDNVTGLLSQSDSksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1363
Cdd:COG4942 100 EAQKEELAELLRALYRlgRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1364 EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAA 1428
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
883-1533 |
6.44e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.93 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 883 LAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICH------DLEARVEEEEERCQHLQ 956
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHlhfgykSDETLIASRQEERQETS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 957 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTT-EAKLKKLEEEQIILEDQNCKLAK-----------EKKLLEDRIAE 1024
Cdd:pfam12128 286 AELNQLLRTLDDQWKEKRDELNGELSAADAAVAKdRSELEALEDQHGAFLDADIETAAadqeqlpswqsELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1025 FTTN---LTEEEEKSKSLAKLKNKHEamITDLEERL--RREEKQRQELEKT----------RRKLEGDSTDLSDQ----- 1084
Cdd:pfam12128 366 LTGKhqdVTAKYNRRRSKIKEQNNRD--IAGIKDKLakIREARDRQLAVAEddlqaleselREQLEAGKLEFNEEeyrlk 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1085 --IAELQAQIA------ELKMQLAKKEEELQAA-----LARVEEEAAQKNMALKKIR----------------ELESQIS 1135
Cdd:pfam12128 444 srLGELKLRLNqatatpELLLQLENFDERIERAreeqeAANAEVERLQSELRQARKRrdqasealrqasrrleERQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1136 ELQEDLESERAS-----RNKAEKQKRDLGEELEA---LKTELEDTLDSTAAQQE-------LRSKREQ--EVNILKKTLE 1198
Cdd:pfam12128 524 ELELQLFPQAGTllhflRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGElnlygvkLDLKRIDvpEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1199 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER---GELANEV--------KVLLQGKGDSEHK 1267
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARldlRRLFDEKqsekdkknKALAERKDSANER 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1268 RKKVEAQLQELQVKFNEG-ERVRTELADKVTKLQVELDNVTGLLsqsDSKSSKLTKDFSALESQLQDTQELLQEENRQKL 1346
Cdd:pfam12128 684 LNSLEAQLKQLDKKHQAWlEEQKEQKREARTEKQAYWQVVEGAL---DAQLALLKAAIAARRSGAKAELKALETWYKRDL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1347 slstKLKQVEDEKNSfreqleeeeeakhNLEKQIATLHAQVADMKKKMEDS----VGCLETAEEVKRKLQKDLEGLSQRH 1422
Cdd:pfam12128 761 ----ASLGVDPDVIA-------------KLKREIRTLERKIERIAVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAI 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1423 EEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSacnLEKKQKKFDQLLAEEKTISAKYAEER-----DRAEAEAREKET 1497
Cdd:pfam12128 824 SE-------LQQQLARLIADTKLRRAKLEMERKA---SEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERLA 893
|
730 740 750
....*....|....*....|....*....|....*.
gi 2550219468 1498 KALSLARALEEAMEQkaeLERLNKQFRTEMEDLMSS 1533
Cdd:pfam12128 894 QLEDLKLKRDYLSES---VKKYVEHFKNVIADHSGS 926
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
894-1724 |
1.12e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 894 TLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLeARVEEEEErcqhlQAEK-KKMQQNIQELEEQ 972
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL-NLVQTALR-----QQEKiERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 973 LEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQnckLAKEKKLLE--DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMI 1050
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQ---LADYQQALDvqQTRAIQYQQAVQALERAKQLCGLPDLTADNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1051 TDLEERLRREEKQR-QELEKTRRKLegdstDLSDQIAELQAQIAELKMQLAKKEEELQA------ALARVEEE---AAQK 1120
Cdd:PRK04863 441 EDWLEEFQAKEQEAtEELLSLEQKL-----SVAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvareLLRRLREQrhlAEQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1121 NMALKKIRELEsQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDStaAQQELRSKREQevnilKKTLEEE 1200
Cdd:PRK04863 516 QQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES--LSESVSEARER-----RMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1201 AKTHEAQIQEMRQKHSQ------AVEELAEQLEQTKRVKANLEKA-KQTLENERGelanevkvLLQGKGDSEHKRKKVEA 1273
Cdd:PRK04863 588 LEQLQARIQRLAARAPAwlaaqdALARLREQSGEEFEDSQDVTEYmQQLLERERE--------LTVERDELAARKQALDE 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1274 QLQEL-QVKFNEGERVRTeLADKVTKLQVEL--DNVT--------GLLSQsdSKSSKLTKDFSALESQLQDTQELLQEen 1342
Cdd:PRK04863 660 EIERLsQPGGSEDPRLNA-LAERFGGVLLSEiyDDVSledapyfsALYGP--ARHAIVVPDLSDAAEQLAGLEDCPED-- 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1343 rqklslstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATlhaqvADMKKKMEDSVGCLETAEEVKRklqkdLEGLSQRH 1422
Cdd:PRK04863 735 ---------LYLIEGDPDSFDDSVFSVEELEKAVVVKIAD-----RQWRYSRFPEVPLFGRAAREKR-----IEQLRAER 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1423 EEKVAAYDKLEKTKTRLQQelddllvdlDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSL 1502
Cdd:PRK04863 796 EELAERYATLSFDVQKLQR---------LHQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQ 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1503 ARALEEAMEQKAEL---------ERLNKQFRTEMEDLMSSKDDV------GKSVHELEKSKRAL---EQQVEEMKTQLEE 1564
Cdd:PRK04863 867 LEQAKEGLSALNRLlprlnlladETLADRVEEIREQLDEAEEAKrfvqqhGNALAQLEPIVSVLqsdPEQFEQLKQDYQQ 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1565 LEDELQATeDAKLRLEVNLQAMKAQFE-RDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDL 1643
Cdd:PRK04863 947 AQQTQRDA-KQQAFALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASL 1025
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1644 EAHIDSANKNRDEAIKQLRKLQAQMKDCMRELddTRASREEILAQAKEN-------EKKLKSMEAEMIQLQEELAAAERA 1716
Cdd:PRK04863 1026 KSSYDAKRQMLQELKQELQDLGVPADSGAEER--ARARRDELHARLSANrsrrnqlEKQLTFCEAEMDNLTKKLRKLERD 1103
|
....*...
gi 2550219468 1717 KRQAQQER 1724
Cdd:PRK04863 1104 YHEMREQV 1111
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1687-1900 |
1.30e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1687 AQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDeladeIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNT 1766
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1767 ELINDRLKKANLQIDQINTDLNLershaqknenarQQLERQNKELKVKLQEMEGTVKSKYKAsITALEAKIAQLEEQLDN 1846
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVI------------QQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQ 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1847 ETKERQAAckqvrrTEKKLKDVLLQVDDERRNAEQYKDQAD---KASTRLKQLKRQL 1900
Cdd:COG3206 310 EAQRILAS------LEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREV 360
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1106-1331 |
1.53e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1106 LQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSK 1185
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1186 REQEVNILKKTLEEEAKTHE-----------------AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERG 1248
Cdd:COG4942 95 LRAELEAQKEELAELLRALYrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1249 ELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSklTKDFSALE 1328
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP--AAGFAALK 252
|
...
gi 2550219468 1329 SQL 1331
Cdd:COG4942 253 GKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1599-1825 |
1.60e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1599 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDT 1678
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1679 RASREEILAQAkenEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEE 1758
Cdd:COG4942 103 KEELAELLRAL---YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1759 LEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSK 1825
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
989-1240 |
1.62e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 989 TTEAKLKKLEEEQIILEDQncklAKEKKLLEDRIAEFTTNLTE-EEEKSKSLAKLKNKHEAMITDLEERLRREEK----- 1062
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEERLKELEPfyney 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1063 -----QRQELEKTRRKLEGDSTDLSDQIAELqaqiAELKMQLAKKEEELQAALARVEEEAAQKnmALKKIRELESQISEL 1137
Cdd:PRK03918 605 lelkdAEKELEREEKELKKLEEELDKAFEEL----AETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGL 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1138 QEDLESERASRNKAEKQKRDLGEELEAL---KTELEDTLDSTAAQQELRSKreqeVNILKKTLEEEAktheaqIQEMRQK 1214
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEERekaKKELEKLEKALERVEELREK----VKKYKALLKERA------LSKVGEI 748
|
250 260
....*....|....*....|....*.
gi 2550219468 1215 HSQAVEELAEQLEQTKRVKANLEKAK 1240
Cdd:PRK03918 749 ASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
908-1365 |
1.67e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 908 EQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEeeesaRQKLQLEK 987
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQLLPLYQE-----LEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 988 VTTEAKLKKLEEEQIILEDqnckLAKEKKLLEDRIAEFTTNLTEEEE-----KSKSLAKLKNKHEAMITDLEERLRREEK 1062
Cdd:COG4717 142 AELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEqlslaTEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1063 QRQELEKTRRKLEGDSTDLsdQIAELQAQIAELKMQL-----------------AKKEEELQAALARVEEEAAQKNMALK 1125
Cdd:COG4717 218 AQEELEELEEELEQLENEL--EAAALEERLKEARLLLliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1126 KIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQevnilkktLEEEAKTHE 1205
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--------LEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1206 AQIQE---MRQKHSQAVEELAEQLEQTKRVKaNLEKAKQTLENERGELANEVKVLLQGKGDSEhkrkkVEAQLQELQVKF 1282
Cdd:COG4717 368 LEQEIaalLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1283 NEGERVRTELADKVTKLQVELDNVTGllsqsdskssklTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF 1362
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEE------------DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
...
gi 2550219468 1363 REQ 1365
Cdd:COG4717 510 REE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1543-1741 |
1.86e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQ---FERDLQGRDEQSEEKKKQLVRQVREME--- 1616
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREELGERARALYrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1617 ---------------AELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRAS 1681
Cdd:COG3883 100 gsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1682 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1741
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
920-1308 |
2.02e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.06 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 920 AEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQqniqeleEQLEEEESARQKLQLEKVTTEAKLKKLEE 999
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE-------RQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1000 EQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST 1079
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1080 DLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKqkrdLG 1159
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG----LG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1160 EELEALKTELEDTldstaaQQELRSKREQ--EVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEqtkRVKANLE 1237
Cdd:pfam07888 258 EELSSMAAQRDRT------QAELHQARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIE---KLSAELQ 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1238 KAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQE----LQVKFNEGERVRT---ELADKVTKLQVELDNVTG 1308
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQElkasLRVAQKEKEQLQAekqELLEYIRQLEQRLETVAD 406
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1033-1155 |
2.44e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.99 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1033 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakkEEELQAALAR 1112
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2550219468 1113 VEEEAAQknmALKKIRELESQISELQ--EDLESERASRNKAEKQK 1155
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYASVkaHELIEARKRLNKANEKK 623
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
979-1191 |
2.66e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 979 ARQKLQlekvTTEAKLKKLEEEQIILEdqnckLAKEKKLLEDRIAEFTTNLT-------EEEEKSKSLAKLKNKHEAMIT 1051
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAearaelaEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1052 DLEE--RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAkkeEELQAALARVEEEAAQknmALKKIRE 1129
Cdd:COG3206 258 ELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 1130 LESQISELQEDLESErasrNKAEKQKRDLGEELEALKTELEDTLdstAAQQELRSKREQEVN 1191
Cdd:COG3206 332 LQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVG 386
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
984-1366 |
2.79e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 55.73 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 984 QLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQ 1063
Cdd:COG5185 225 AKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1064 RQELEKTRRKLEgdstdlsdqiaelQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkiRELESQISELQEDLES 1143
Cdd:COG5185 305 IDIKKATESLEE-------------QLAAAEAEQELEESKRETETGIQNLTAEIEQGQ------ESLTENLEAIKEEIEN 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1144 ERASRNKAEKQkrdlgEELEALKTELEDTLDSTaaQQELRSKREQEVNILkKTLEEEAKTHEAQIQEMRQKHSQAVEELA 1223
Cdd:COG5185 366 IVGEVELSKSS-----EELDSFKDTIESTKESL--DEIPQNQRGYAQEIL-ATLEDTLKAADRQIEELQRQIEQATSSNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1224 EQleqtkrvkanlEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKveaqlQELQVKFNEGERVRTELADKV----TKL 1299
Cdd:COG5185 438 EV-----------SKLLNELISELNKVMREADEESQSRLEEAYDEIN-----RSVRSKKEDLNEELTQIESRVstlkATL 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 1300 QVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLK-----QVEDEKNSFREQL 1366
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNaktdgQAANLRTAVIDEL 573
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1162-1623 |
2.85e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1162 LEALKTELEDTLDstAAQQELRSKREQEVNILKKTLEEEakthEAQIQEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQ 1241
Cdd:COG4717 40 LAFIRAMLLERLE--KEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEE-YAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1242 TLENERGELANEVKV--LLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA---DKVTKLQVELDNVTGLLSQSDSK 1316
Cdd:COG4717 113 ELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEeleAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1317 S-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKnsFREQLEEEEEAKHNLEKQIATLHAQVADMKKKME 1395
Cdd:COG4717 193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1396 DSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 1475
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1476 TISAKYAEERDRAEAEAREKETKAL-------------SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKsvH 1542
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALlaeagvedeeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--E 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEE-KKKQLVRQV-REMEAE 1618
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEwAALKLALELlEEAREE 508
|
....*
gi 2550219468 1619 LEDER 1623
Cdd:COG4717 509 YREER 513
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1673-1897 |
3.05e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1673 RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEE--LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA 1750
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1751 RIAQLEEELEEEQGNTELINDRLkkanlQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASI 1830
Cdd:COG3206 248 QLGSGPDALPELLQSPVIQQLRA-----QLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1831 TALEAKIAQLEEQLDNETKERQaackQVRRTEKKLKDvlLQvdderRNAEQYKDQADKASTRLKQLK 1897
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLA----ELPELEAELRR--LE-----REVEVARELYESLLQRLEEAR 378
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1344-1909 |
3.19e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1344 QKLSLSTKLKQVEDEKN----SFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAE-------EVKRKLQ 1412
Cdd:pfam05557 3 ELIESKARLSQLQNEKKqmelEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEealreqaELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1413 KDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERD------ 1486
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQnlekqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1487 --RAEAEAREKE--------TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQvE 1556
Cdd:pfam05557 163 ssLAEAEQRIKElefeiqsqEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-E 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1557 EMKTQLEELEDELQATEdAKLRLEVNLQAMKAQFER---DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRsmavaar 1633
Cdd:pfam05557 242 KYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1634 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSME--AEMIQLQE 1708
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1709 ELAAAERAkrqaqqeRDELADEIANSSGKGALALEekRRLEARIAQLEEELeeeQGNTELINDRLKKANlqidqinTDLN 1788
Cdd:pfam05557 394 AHNEEMEA-------QLSVAEEELGGYKQQAQTLE--RELQALRQQESLAD---PSYSKEEVDSLRRKL-------ETLE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1789 LERshaqknenarQQLERQNKELKVKL--QEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLK 1866
Cdd:pfam05557 455 LER----------QRLREQKNELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE 524
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2550219468 1867 DVLLQVDderRNAEQYKDQADKastRLKQLKRQLEEAEEEAQR 1909
Cdd:pfam05557 525 DDLEQVL---RLPETTSTMNFK---EVLDLRKELESAELKNQR 561
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1649-1866 |
3.97e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1649 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1728
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1729 DEIANSSGKGAL--ALEEKRRLEARIAQLEEELEEEQGNTELINDrLKKANLQIDQINTDLnlershaqknENARQQLER 1806
Cdd:COG3883 93 RALYRSGGSVSYldVLLGSESFSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAEL----------EAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1807 QNKELKVKLQEMEgTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLK 1866
Cdd:COG3883 162 LKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
953-1151 |
4.15e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 953 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEqiiLEDQNCKLAKEKKLLEDRIAEF------- 1025
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGERARALyrsggsv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1026 --------TTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKM 1097
Cdd:COG3883 103 syldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1098 QLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKA 1151
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1427-1939 |
4.17e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.29 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1427 AAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTIsakyAEERDRAEAEAREKETKALSLARAL 1506
Cdd:PRK01156 166 RNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSIT----LKEIERLSIEYNNAMDDYNNLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1507 EEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKR-----------------ALEQQVEEMKTQLEELEDEL 1569
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1570 QATEDAKLRLEVnLQAMKAQFERDLQGRDE---------QSEEKKKQLVRQVREMEAELEDERKQR-------------- 1626
Cdd:PRK01156 322 NKYHAIIKKLSV-LQKDYNDYIKKKSRYDDlnnqileleGYEMDYNSYLKSIESLKKKIEEYSKNIermsafiseilkiq 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1627 ----SMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKD---------CMRELDDTRASReeilaQAKENE 1693
Cdd:PRK01156 401 eidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcpvCGTTLGEEKSNH-----IINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1694 KKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRL 1773
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1774 KKANLQI-DQINTDLNleRSHAQKN----ENARQQLERQNKELK---VKLQEMEGT---VKSKYKASITALEAKIAQLEE 1842
Cdd:PRK01156 556 KSLKLEDlDSKRTSWL--NALAVISlidiETNRSRSNEIKKQLNdleSRLQEIEIGfpdDKSYIDKSIREIENEANNLNN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1843 QLdNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELE 1922
Cdd:PRK01156 634 KY-NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
570
....*....|....*..
gi 2550219468 1923 DATETADAMNREVSSLK 1939
Cdd:PRK01156 713 ELSDRINDINETLESMK 729
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1047-1181 |
5.15e-07 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 54.09 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1047 EAMITDLEERLRRE--EKQRQELEKTRRKLEGDSTDLSD------------QIAELQAQIAELKMQLAKKEEELQAALAR 1112
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 1113 VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQkrdlgEELEALKTEL---EDTLDSTAAQQE 1181
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1128-1939 |
5.85e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.96 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1128 RELESQISELQEDLESERASRNKAEKQKRDLGEELEALkteledtldsTAAQQELrskrEQEVNILKKTLeeeAKTHEA- 1206
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEEL----------SARESDL----EQDYQAASDHL---NLVQTAl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1207 QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGD-----SEHKRKKVEAQlQELQVK 1281
Cdd:COG3096 344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqalDVQQTRAIQYQ-QAVQAL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1282 fnEGERVRTELADkvtklqVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELlQEENRQKLSLSTKLK-QVEDEK- 1359
Cdd:COG3096 423 --EKARALCGLPD------LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAA-RRQFEKAYELVCKIAgEVERSQa 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1360 -NSFREQLEEEEEAKHNLEkQIATLHAQVADmkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTR 1438
Cdd:COG3096 494 wQTARELLRRYRSQQALAQ-RLQQLRAQLAE-----------LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1439 LQQELDDLLVDLDHQRQSACNLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLA--RALEEAMEQKAEL 1516
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQL---EQLRARIKELAARAPAWLAAQDALERLREQSGEALAdsQEVTAAMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1517 ERLNKQfrtemedlmsSKDdvgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQATEDAKLRLEVNLQ----- 1584
Cdd:COG3096 639 EREATV----------ERD-------ELAARKQALESQIERLSqpggaedPRLLALAERLGGVLLSEIYDDVTLEdapyf 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1585 ------AMKAQFERDLQGrdeqseekkkqlvrqVREMEAELED--------ERKQRSMAVAARKKLEMDLKDL------- 1643
Cdd:COG3096 702 salygpARHAIVVPDLSA---------------VKEQLAGLEDcpedlyliEGDPDSFDDSVFDAEELEDAVVvklsdrq 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1644 -----------------EAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKklksmEAEMiql 1706
Cdd:COG3096 767 wrysrfpevplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDP-----EAEL--- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1707 qeelaaaerakRQAQQERDELADEIANssgkgalaleekrrLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQintd 1786
Cdd:COG3096 839 -----------AALRQRRSELERELAQ--------------HRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE---- 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1787 lnlerSHAQKNENARQQLErqnkelkvKLQEMEGTVKSKYKAsITALEAKIAQL------EEQLDNETKERQAACKQVRR 1860
Cdd:COG3096 890 -----TLADRLEELREELD--------AAQEAQAFIQQHGKA-LAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRRLKQ 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1861 TEKKLKDVLlqvddERRNAEQYKD---QADKASTRLKQLKRQLEeaeeeaqRANASRRKLQRELEDATETADAMNREVSS 1937
Cdd:COG3096 956 QIFALSEVV-----QRRPHFSYEDavgLLGENSDLNEKLRARLE-------QAEEARREAREQLRQAQAQYSQYNQVLAS 1023
|
..
gi 2550219468 1938 LK 1939
Cdd:COG3096 1024 LK 1025
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
895-1631 |
5.90e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.96 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 895 LQSQLMAEKLQLQEQLQAETELCAE-AEELRARLTAKKQELEEICHDLEARVEEEEE-RCQHLQAekKKMQQNIQELEEQ 972
Cdd:COG3096 413 IQYQQAVQALEKARALCGLPDLTPEnAEDYLAAFRAKEQQATEEVLELEQKLSVADAaRRQFEKA--YELVCKIAGEVER 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 973 LEEEESAR--------QKLQLEKVTT-EAKLKKLEEEqiiLEDQNcklaKEKKLLEDRIAEFTTNLTEEEEksksLAKLK 1043
Cdd:COG3096 491 SQAWQTARellrryrsQQALAQRLQQlRAQLAELEQR---LRQQQ----NAERLLEEFCQRIGQQLDAAEE----LEELL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1044 NKHEAMITDLEERLRREEKQRQELektRRKLEgdstdlsdqiaELQAQIAELKmQLAKKEEELQAALARVEEEAAQknmA 1123
Cdd:COG3096 560 AELEAQLEELEEQAAEAVEQRSEL---RQQLE-----------QLRARIKELA-ARAPAWLAAQDALERLREQSGE---A 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1124 LKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALkteledTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1203
Cdd:COG3096 622 LADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL------SQPGGAEDPRLLALAERLGGVLLSEIYDDVTL 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1204 HEAQIQEMR---QKHSQAVEELAeqleqtkRVKANLEKAKQTLEN----ERGELANEVKVLlqgkgDSEHKRKKVEAQLQ 1276
Cdd:COG3096 696 EDAPYFSALygpARHAIVVPDLS-------AVKEQLAGLEDCPEDlyliEGDPDSFDDSVF-----DAEELEDAVVVKLS 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1277 ELQVKFNE-------GERVRTELADkvtKLQVELDNVTGLLSQSD---SKSSKLTKDFSALESQ------LQDTQELLQE 1340
Cdd:COG3096 764 DRQWRYSRfpevplfGRAAREKRLE---ELRAERDELAEQYAKASfdvQKLQRLHQAFSQFVGGhlavafAPDPEAELAA 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1341 ENRQklslstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGclETAEEVKRKLQKDLEGLS- 1419
Cdd:COG3096 841 LRQR-------RSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLA--DRLEELREELDAAQEAQAf 911
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1420 -QRHEEKVAaydKLEKTKTRLQQELDdllvdldhqrqsacNLEKKQKKFDQLLAEEKTISAK---YAEERDRAEAEAREK 1495
Cdd:COG3096 912 iQQHGKALA---QLEPLVAVLQSDPE--------------QFEQLQADYLQAKEQQRRLKQQifaLSEVVQRRPHFSYED 974
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1496 ETKALSLARALEEAMEQK---AELERLnkQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELedELQAT 1572
Cdd:COG3096 975 AVGLLGENSDLNEKLRARleqAEEARR--EAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL--GVQAD 1050
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1573 EDAKLRLEVNLQAMKAQFERDLQGRDE------QSEEKKKQLVRQVREMEAELEDERKQRSMAVA 1631
Cdd:COG3096 1051 AEAEERARIRRDELHEELSQNRSRRSQlekqltRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA 1115
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1047-1888 |
6.50e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.06 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1047 EAMITDLEERLRREEKQRQELEKTRRKL-----EGDSTDLSDQIAELQAQI-AELKMQLAK-------KEEELQAALARV 1113
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQNMETATVELhlsniENKKNELLDIIVEIKKHIhGEINKDLNKiledfknKEKELSNKINDY 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1114 EEEAAQKNMALKKIRELESQISElQEDLESerasrNKAEKQKRDLGEELEALKTeledtldsTAAQQELRSKREQEVnil 1193
Cdd:TIGR01612 775 AKEKDELNKYKSKISEIKNHYND-QINIDN-----IKDEDAKQNYDKSKEYIKT--------ISIKEDEIFKIINEM--- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1194 kKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQL-EQTKRVKANLEKAKQTLE----NERGELANEVKVLLQGKGDSEHKR 1268
Cdd:TIGR01612 838 -KFMKDDFLNKVDKFINFENNCKEKIDSEHEQFaELTNKIKAEISDDKLNDYekkfNDSKSLINEINKSIEEEYQNINTL 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1269 KKVEaqlQELQVKFNEGERVRtELADKVTKLQVELDNVTGLLSQSDS---------------KSSKLTKDFS--ALESQL 1331
Cdd:TIGR01612 917 KKVD---EYIKICENTKESIE-KFHNKQNILKEILNKNIDTIKESNLieksykdkfdntlidKINELDKAFKdaSLNDYE 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1332 QDTQELLQEENRQKLSLSTklkqveDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVgcLETAEEVKRKL 1411
Cdd:TIGR01612 993 AKNNELIKYFNDLKANLGK------NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI--YNIIDEIEKEI 1064
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1412 QKDLEGLSQRHEEKV-AAYDKLEKTKTRLqqelddllvdldhqrqsacnlekKQKKFDQLLAEEktiSAKYAEERDRAea 1490
Cdd:TIGR01612 1065 GKNIELLNKEILEEAeINITNFNEIKEKL-----------------------KHYNFDDFGKEE---NIKYADEINKI-- 1116
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1491 eareketkalslaraleeameqKAELERLNKQfrtemedlmsskddVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ 1570
Cdd:TIGR01612 1117 ----------------------KDDIKNLDQK--------------IDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1571 AT---EDAKlRLEVNLQAMKAQFERDLQGRDEQseekkKQLVRQVREMEAELEDERKQRSMAVAARKKLEmdlKDLEAHI 1647
Cdd:TIGR01612 1161 KAisnDDPE-EIEKKIENIVTKIDKKKNIYDEI-----KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLG---KLFLEKI 1231
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1648 DSANKNRDEAIKQLRKLqaqmkdcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEelaaaERAKRQAQQERDEL 1727
Cdd:TIGR01612 1232 DEEKKKSEHMIKAMEAY-------IEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD-----DKDHHIISKKHDEN 1299
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1728 ADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKK-AN----LQIDQINTDLNLERSHAQKnenarq 1802
Cdd:TIGR01612 1300 ISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEiANiyniLKLNKIKKIIDEVKEYTKE------ 1373
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1803 qLERQNKELKVKLQEMEGTVKsKYKASITALEAKiAQLEEQLDNetkerqaacKQVRRTEKKLKDVLLQVDDERRNAEQY 1882
Cdd:TIGR01612 1374 -IEENNKNIKDELDKSEKLIK-KIKDDINLEECK-SKIESTLDD---------KDIDECIKKIKELKNHILSEESNIDTY 1441
|
....*.
gi 2550219468 1883 KDQADK 1888
Cdd:TIGR01612 1442 FKNADE 1447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1378-1635 |
6.83e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1378 KQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQElddllvdldhqrqsa 1457
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1458 cnLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDV 1537
Cdd:COG4942 85 --LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1538 GKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAmkaqferdLQGRDEQSEEKKKQLVRQVREMEA 1617
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEALIARLEA 234
|
250
....*....|....*...
gi 2550219468 1618 ELEDERKQRSMAVAARKK 1635
Cdd:COG4942 235 EAAAAAERTPAAGFAALK 252
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1046-1298 |
8.24e-07 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 53.22 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1046 HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalk 1125
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1126 kirELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ--EVNILKKTLEEEAKT 1203
Cdd:pfam09787 115 ---ELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQltETLIQKQTMLEALST 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1204 heaqiqemrQKHSQAVEelaeqleqtkrvkanLEKAKQTLENERGELANEVKVLLQGKGDSEHKRkkveaqLQELQVKFN 1283
Cdd:pfam09787 192 ---------EKNSLVLQ---------------LERMEQQIKELQGEGSNGTSINMEGISDGEGTR------LRNVPGLFS 241
|
250
....*....|....*
gi 2550219468 1284 EGERVRTELADKVTK 1298
Cdd:pfam09787 242 ESDSDRAGMYGKVRK 256
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1039-1173 |
8.95e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.09 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1039 LAKLKNKHEAmiTDLEERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE---EELQAALARVEE 1115
Cdd:COG2433 382 LEELIEKELP--EEEPEAEREKEHEERELTEEEEEIR----RLEEQVERLEAEVEELEAELEEKDeriERLERELSEARS 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1116 EAAQKNMALKKIRELESQISELQEDLESErasRNKAEKQKRDLGEELEALKTELEDTL 1173
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
812-1270 |
9.54e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 812 RGYLARKAFAKRQQQLTAMKVLQRNCAAYLKLRNWQWWRLFT---KVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENR 888
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQ 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 889 LTEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEICHDLEARVEEEeercQHLQAEKKKMQQNIQ 967
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEdVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD----NRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 968 ELEEQLEEEESARQKLQLEKVTTEAKLK-KLEEEQIILEDQNCklAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKh 1046
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQpEQDLQDVRLHLQQC--SQELALKLTALHALQLTLTQERVREHALSIRVLP- 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1047 eamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1126
Cdd:TIGR00618 672 -------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQS 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1127 IRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA 1206
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1207 QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEnergELANEVKVLLQGKGDSEHKRKK 1270
Cdd:TIGR00618 825 TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----QLTQEQAKIIQLSDKLNGINQI 884
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
875-1723 |
1.00e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 875 LVKVREKQLAAENRLTEMetlqsqlmAEKLQLQEQLQA--ETELCAEAEELRARLTAKKQ---------ELEEICHDLEA 943
Cdd:COG3096 294 LFGARRQLAEEQYRLVEM--------ARELEELSARESdlEQDYQAASDHLNLVQTALRQqekieryqeDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 944 R---VEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILedQNCKLAKEKklLED 1020
Cdd:COG3096 366 QeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALC--GLPDLTPEN--AED 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1021 RIAEFTtnlteeeekskslAKLKNKHEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQiaelkmQLA 1100
Cdd:COG3096 442 YLAAFR-------------AKEQQATEEVL-ELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTAR------ELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1101 KKEEELQAALARVEEEAAQknmalkkIRELEsQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDStaAQQ 1180
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQ-------LAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE--LEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1181 ELRSKREQevnilKKTLEEEAKTHEAQIQEMRQKH------SQAVEELAEQLEQTKRVKANLEKAKQT-LENERGelane 1253
Cdd:COG3096 572 QAAEAVEQ-----RSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEALADSQEVTAAMQQlLERERE----- 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1254 vkvLLQGKGDSEHKRKKVEAQLQEL-QVKFNEGERVRTeLADKV--TKLQVELDNVT--------GLLsqSDSKSSKLTK 1322
Cdd:COG3096 642 ---ATVERDELAARKQALESQIERLsQPGGAEDPRLLA-LAERLggVLLSEIYDDVTledapyfsALY--GPARHAIVVP 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1323 DFSALESQLQDTQE-----LLQEENRQKLSLST-KLKQVEDE---KNSFReQLEEEEEAKHNL------EKQIATLHAQv 1387
Cdd:COG3096 716 DLSAVKEQLAGLEDcpedlYLIEGDPDSFDDSVfDAEELEDAvvvKLSDR-QWRYSRFPEVPLfgraarEKRLEELRAE- 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1388 ADmkkkmEDSVGCLETAEEVkRKLQKDLEGLSQ---RH------EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAC 1458
Cdd:COG3096 794 RD-----ELAEQYAKASFDV-QKLQRLHQAFSQfvgGHlavafaPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLD 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1459 NLEKKQKKFDQLLAEEKTISAKYAEERDRaeaEAREKetkalslaraLEEAMEQKAELERLNKQFRtEMEDLMSSKDDVG 1538
Cdd:COG3096 868 QLKEQLQLLNKLLPQANLLADETLADRLE---ELREE----------LDAAQEAQAFIQQHGKALA-QLEPLVAVLQSDP 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1539 KSVHELEKSKRALEQQVEEMKTQLEELEDELQ-----ATEDAKLRLEVN---LQAMKAQFERDLQGRdEQSEEKKKQLVR 1610
Cdd:COG3096 934 EQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLGENsdlNEKLRARLEQAEEAR-REAREQLRQAQA 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1611 QVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRdeAIKQLRKLQAQmkdcmreLDDTRASREEIlaqak 1690
Cdd:COG3096 1013 QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEER--ARIRRDELHEE-------LSQNRSRRSQL----- 1078
|
890 900 910
....*....|....*....|....*....|...
gi 2550219468 1691 enEKKLKSMEAEMIQLQEELAAAERAKRQAQQE 1723
Cdd:COG3096 1079 --EKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
918-1524 |
1.04e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.98 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 918 AEAEELRARLTAKKQELE--EICH-----DLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKlQLEkvtt 990
Cdd:pfam05557 2 AELIESKARLSQLQNEKKqmELEHkrariELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALRE-QAE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 991 EAKLKKLEEEQIiledqnCKLAKEKKLLEDRIAEFTTNLTEEeeksksLAKLknKHEAMITDLEERLRREEKQ--RQELE 1068
Cdd:pfam05557 77 LNRLKKKYLEAL------NKKLNEKESQLADAREVISCLKNE------LSEL--RRQIQRAELELQSTNSELEelQERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1069 KTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKEEelqaaLARVEEEAAQKNMALKKIRELESQISELQEDLESERASR 1148
Cdd:pfam05557 143 LLKAKA----SEAEQLRQNLEKQQSSLAEAEQRIKE-----LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1149 NKAEKQKRD---LGEELEALKTELEDTLDSTAAQQELRSKREQevniLKKTLEEEAKTHEAQIQEMRQKhsqavEELAEQ 1225
Cdd:pfam05557 214 KHLNENIENkllLKEEVEDLKRKLEREEKYREEAATLELEKEK----LEQELQSWVKLAQDTGLNLRSP-----EDLSRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1226 LEQTKRVKANLEKAKQTLENERGELANEVKVLlqgkgdsEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDN 1305
Cdd:pfam05557 285 IEQLQQREIVLKEENSSLTSSARQLEKARREL-------EQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1306 VTGLLSQSDSK------SSKLTKDFSALESQLQDTQELLQEenrqklsLSTKLKQVEDEKNSFREQLEEeeeakhnLEKQ 1379
Cdd:pfam05557 358 YRAILESYDKEltmsnySPQLLERIEEAEDMTQKMQAHNEE-------MEAQLSVAEEELGGYKQQAQT-------LERE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1380 IATLHAQVAdmkkkMEDSVGCLETAEEVKRKLQkDLEGLSQRHEEKVAAYDkLEKTKTRLQQELDDLLVDLDHQRQSACN 1459
Cdd:pfam05557 424 LQALRQQES-----LADPSYSKEEVDSLRRKLE-TLELERQRLREQKNELE-MELERRCLQGDYDPKKTKVLHLSMNPAA 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1460 LEKKQKK--FDQLLAEEKTISAKYAEERDRAEAEAREKETkalSLARALEEAMEQKAELERLNKQFR 1524
Cdd:pfam05557 497 EAYQQRKnqLEKLQAEIERLKRLLKKLEDDLEQVLRLPET---TSTMNFKEVLDLRKELESAELKNQ 560
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1086-1361 |
1.10e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1086 AELQAQIAELKMQlaKKEEELQAALARVEEEAAQknmALKKIRELESQISELQEDLEserasrnKAEKQKRDLGEELEAL 1165
Cdd:PRK11281 39 ADVQAQLDALNKQ--KLLEAEDKLVQQDLEQTLA---LLDKIDRQKEETEQLKQQLA-------QAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1166 KTELEDTLDSTAAQQELRskreqevnilkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN 1245
Cdd:PRK11281 107 KDDNDEETRETLSTLSLR------------QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1246 ERGELANevkVLLQGKGDSEHKRKKVEAQLQ--ELQVKFNegervRTELADKvTKLQvELDNvtgllSQSDSKSSKLTKd 1323
Cdd:PRK11281 175 IRNLLKG---GKVGGKALRPSQRVLLQAEQAllNAQNDLQ-----RKSLEGN-TQLQ-DLLQ-----KQRDYLTARIQR- 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 2550219468 1324 fsaLESQLQDTQELLqeeNRQKLSLSTklKQVEDEKNS 1361
Cdd:PRK11281 239 ---LEHQLQLLQEAI---NSKRLTLSE--KTVQEAQSQ 268
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1402-1931 |
1.18e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1402 ETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKY 1481
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1482 AEERDRAEAEAREKETKALSLARALE------EAMEQKAELERLNKQFR--TEMEDLMSSKDDVGKSVHELEKSKRALEQ 1553
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEkmilafEELRVQAENARLEMHFKlkEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1554 QVEEMKTQLEELEDELQATEDAKLRLEvnlqamkaqferdlqGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAAR 1633
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLE---------------EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1634 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE----NEKKLKSMEAEMIQLQEE 1709
Cdd:pfam05483 313 KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1710 LAAAERAKRQAQQERDEL--------------------ADEIANSSGKGALALEEKRR----LEARI-----AQLEEELE 1760
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELkkilaedeklldekkqfekiAEELKGKEQELIFLLQAREKeihdLEIQLtaiktSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1761 EEQGNTELINDRLKKANL------------QIDQINTDLNLE-RSHAQKNENARQQLERQNKELKvKLQEMEGTVKSKYK 1827
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELtahcdklllenkELTQEASDMTLElKKHQEDIINCKKQEERMLKQIE-NLEEKEMNLRDELE 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1828 ASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEA 1907
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
570 580
....*....|....*....|....
gi 2550219468 1908 QRANASRRKLQRELEDATETADAM 1931
Cdd:pfam05483 632 NAYEIKVNKLELELASAKQKFEEI 655
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
823-1496 |
1.19e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.90 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 823 RQQQLTAMKVLQRNCAAYLKLRNWqwwRLFTKVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEME---TLQSQL 899
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknsLTETLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 900 MAEKLQLQEQLQAETELCAEAEELRAR------------LTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQ 967
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 968 ELEEQLEEEESARQKLQLEkvtteakLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTT---------NLTEEEEKSKS 1038
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKE-------LASLEQNKNHINNELESKEEQLSSYEDKLFDVCGsqdeesdleRLKEEIEKSSK 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1039 ----LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVE 1114
Cdd:TIGR00606 654 qramLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1115 EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQEVNILK 1194
Cdd:TIGR00606 734 GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV---TIMERFQMELKDVERKIAQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1195 KTLEEEAKTHEAQIQEMRQKHSQAVEEL---AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLlqgkGDSEHKRKKV 1271
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQQVNQEKQEKQHELdtvVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI----GTNLQRRQQF 886
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1272 EAQLQELQVKFNEgervrteladkvtklqveldnvtgLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKlslstk 1351
Cdd:TIGR00606 887 EEQLVELSTEVQS------------------------LIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN------ 936
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1352 lKQVEDEKNSFREQLEEEEEAKHNLEKQIAT-LHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGL-----SQRHEEK 1425
Cdd:TIGR00606 937 -KKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMrqdidTQKIQER 1015
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1426 VAA--------YDKLEKTKTRLQQELDDLLVDLDHQRQSACNleKKQKKFDQLLAEEKTISAK---YAEERDRAEAEARE 1494
Cdd:TIGR00606 1016 WLQdnltlrkrENELKEVEEELKQHLKEMGQMQVLQMKQEHQ--KLEENIDLIKRNHVLALGRqkgYEKEIKHFKKELRE 1093
|
..
gi 2550219468 1495 KE 1496
Cdd:TIGR00606 1094 PQ 1095
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1021-1345 |
1.19e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.75 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1021 RIAEFTTNLTEEEEKSKSLAKLKNkheAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA 1100
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSD---FQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1101 KKEEELQAalarveeeAAQKNMalkKIRELESQISELQEDLESERASRNKAEKQkrdLGEELEALKTE---LEDtlDSTA 1177
Cdd:PLN02939 181 ETDARIKL--------AAQEKI---HVEILEEQLEKLRNELLIRGATEGLCVHS---LSKELDVLKEEnmlLKD--DIQF 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1178 AQQELRSKREQEVNILKktLEEEAKTHEAQIQEMRQKHSQAVEELAEQleQTKRVKANLEKAkQTLENERGELANEVK-- 1255
Cdd:PLN02939 245 LKAELIEVAETEERVFK--LEKERSLLDASLRELESKFIVAQEDVSKL--SPLQYDCWWEKV-ENLQDLLDRATNQVEka 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1256 -VLLQGKGDSEHKRKKVEAQLQELQV-KFNegervrtelADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQD 1333
Cdd:PLN02939 320 aLVLDQNQDLRDKVDKLEASLKEANVsKFS---------SYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
330
....*....|..
gi 2550219468 1334 TQELLQEENRQK 1345
Cdd:PLN02939 391 TLSKLKEESKKR 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1543-1764 |
1.24e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQSEEKKKQLVRQVREMEAELEDE 1622
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1623 RKQ-RSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1701
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLLSPEDFL----DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 1702 EMIQLQEELAAAERAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQLEEELEEEQG 1764
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLE--------------KELAELAAELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1289-1518 |
1.28e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1289 RTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEE 1368
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1369 EeeaKHNLEKQIATLHaqvadmKKKMEDSVGCLETAEEVKRkLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLV 1448
Cdd:COG4942 102 Q---KEELAELLRALY------RLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1449 DLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELER 1518
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1656-1950 |
1.39e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1656 EAIKQLRKLQAQMKDCMR---ELDDTRASREeILAQAKENEKKLKSMEAEMIQLQEELAAAERAkrQAQQERDELADEIA 1732
Cdd:COG4913 222 DTFEAADALVEHFDDLERaheALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1733 NssgkgalALEEKRRLEARIAQLEeeleeeqgntelinDRLKKANLQIDQintdlnLERSHAQKNENARQQLERQNKELK 1812
Cdd:COG4913 299 E-------LRAELARLEAELERLE--------------ARLDALREELDE------LEAQIRGNGGDRLEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1813 VKLQEMEGTVKskykasitALEAKIAQLEEQLDNETKERQAACKQVRRtekklkdvllQVDDERRNAEQYKDQADKASTR 1892
Cdd:COG4913 352 RELEERERRRA--------RLEALLAALGLPLPASAEEFAALRAEAAA----------LLEALEEELEALEEALAEAEAA 413
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1893 LKQLKRQLEEAEEEAQRANASRRKLQRELEDATetaDAMNREVsslknKLRRGDLPFV 1950
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRKSNIPARLLALR---DALAEAL-----GLDEAELPFV 463
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1014-1239 |
1.56e-06 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 53.40 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1014 EKKLLEDRiaeftTNLTEEEEKSKSLAklknkhEAMITDLEERLRREEKQRQELEKTRR-----------KLEGDSTDLs 1082
Cdd:PLN03188 1046 EKKLEQER-----LRWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRcaeelkeamqmAMEGHARML- 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1083 DQIAELQaqiaELKMQLAKKEEELQAALARVEEEAAQ---KNMALKKIRELESQISELQedleSERasrnkaEKQKRDLG 1159
Cdd:PLN03188 1114 EQYADLE----EKHIQLLARHRRIQEGIDDVKKAAARagvRGAESKFINALAAEISALK----VER------EKERRYLR 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1160 EELEALKTELEDTLDSTAAQQEL--RSKREQEVNIL--KKTLEEEAKTHEA--QIQEMRQKHSQAVEELAEQLEQTKRVK 1233
Cdd:PLN03188 1180 DENKSLQAQLRDTAEAVQAAGELlvRLKEAEEALTVaqKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPK 1259
|
....*.
gi 2550219468 1234 ANLEKA 1239
Cdd:PLN03188 1260 EAIRPA 1265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1030-1246 |
1.63e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1030 TEEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA 1109
Cdd:COG3883 16 PQIQAKQKELSELQAE----LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1110 LARVEE------------------EAAQKNMALKKIRELESQ-ISELQEDLESERASRNKAEKQKrdlgEELEALKTELE 1170
Cdd:COG3883 92 ARALYRsggsvsyldvllgsesfsDFLDRLSALSKIADADADlLEELKADKAELEAKKAELEAKL----AELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1171 DTLDSTAAQQElrskreqEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENE 1246
Cdd:COG3883 168 AAKAELEAQQA-------EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
881-1580 |
1.63e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.22 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 881 KQLAAENRLTEMETLQSQ--LMAEKLQLQEQLQAETELCAEAEELRARLTAKkqelEEICHDLEARVEEEEERCQHLQAE 958
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKmrLEAQAMELDALAVAEKAGQAEAEGLRAALAGA----EMVRKNLEEGSQRELEEIQRLHQE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 959 kkkmQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQncklaKEKKLLEDRIAEfttnLTEEEEKSKS 1038
Cdd:pfam07111 152 ----QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQ-----KEAELLRKQLSK----TQEELEAQVT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1039 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQ---AALARVEE 1115
Cdd:pfam07111 219 LVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTrkiQPSDSLEP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1116 EAAQKNMALkkIRELESQISELQEDLESERASRNKAEKQKRDLGEELealkteledtldstaaqQELRSKREQEVNILKK 1195
Cdd:pfam07111 299 EFPKKCRSL--LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL-----------------QEQVTSQSQEQAILQR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1196 TLEEeaKTHEAQIQEMRQKHSQAveELAEQLEQTKRVKANLEKAKQTLENERGELanevkvllqgkgdsehkrKKVEAQL 1275
Cdd:pfam07111 360 ALQD--KAAEVEVERMSAKGLQM--ELSRAQEARRRQQQQTASAEEQLKFVVNAM------------------SSTQIWL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1276 QELQVKFNEGERVRTELADKVTKLQVELDNVTGL------LSQSDSKSSKLTKDFSALESQLQ-DTQELLQEENRQKLSL 1348
Cdd:pfam07111 418 ETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLmarkvaLAQLRQESCPPPPPAPPVDADLSlELEQLREERNRLDAEL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1349 STKLKQVEDEKNSFREQ----LEEEEEAKHNLEKQIATLHAQVADMKKKMEDSV-GCLETAEE---VKRKLQKDLEGLSQ 1420
Cdd:pfam07111 498 QLSAHLIQQEVGRAREQgeaeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARqGQQESTEEaasLRQELTQQQEIYGQ 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1421 RHEEKVAaydkleKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISakyaEERDRAEAEAREKEtkAL 1500
Cdd:pfam07111 578 ALQEKVA------EVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERN----QELRRLQDEARKEE--GQ 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1501 SLARALEE----------AMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV---EEMKTQLEELED 1567
Cdd:pfam07111 646 RLARRVQElerdknlmlaTLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPIPAAVptrESIKGSLTVLLD 725
|
730
....*....|...
gi 2550219468 1568 ELQATEDAKLRLE 1580
Cdd:pfam07111 726 NLQGLSEAISREE 738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1679-1944 |
1.81e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1679 RASREEiLAQAKENEKKLKSMEAEMIQ----LQEELAAAERAKRQAQQERDELADEIANSSGKgalALEEKRRLEARIAQ 1754
Cdd:TIGR02169 173 EKALEE-LEEVEENIERLDLIIDEKRQqlerLRREREKAERYQALLKEKREYEGYELLKEKEA---LERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1755 LEEELEEEQGNTELINDRLKKANLQIDQINTDLNlershaQKNENARQQLERQNKELKvklqemegtvkskykASITALE 1834
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIK------DLGEEEQLRVKEKIGELE---------------AEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1835 AKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASR 1914
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270
....*....|....*....|....*....|
gi 2550219468 1915 RKLQRELEDATETADAMNREVSSLKNKLRR 1944
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1453-1821 |
1.85e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1453 QRQSACNLEKKQKKFDqllaeektisaKYAEERDRAEAEAREKEtkalslaraleeaMEQKAELERLNKQFRTEMEDlms 1532
Cdd:pfam17380 279 QHQKAVSERQQQEKFE-----------KMEQERLRQEKEEKARE-------------VERRRKLEEAEKARQAEMDR--- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1533 skddvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLrlevnlqAMKAQFERDLQgRDEQSEEKKKQLVRQv 1612
Cdd:pfam17380 332 ------QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEI-------AMEISRMRELE-RLQMERQQKNERVRQ- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1613 remeaELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN 1692
Cdd:pfam17380 397 -----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1693 EKKLKSmeaemiqlqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRR-LEARIAQLEEELEEEQGNTELIND 1771
Cdd:pfam17380 472 RKRKKL----------ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1772 RLKKANL----QIDQINTDLNLERSHAQKNENARQQLeRQNKELKVKLQEMEGT 1821
Cdd:pfam17380 542 RRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1220-1842 |
2.01e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1220 EELAEQLEQTKRVKANLEKAKQTLENERGELAN--EVKVLLQGKGDS-EHKRKKVEAQLQELQVKFNEGERVRTELADKV 1296
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNidYLEEKLKSSNLElENIKKQIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1297 TKLQVELDNVTGLLSQSDSKSsKLTKDFSALESQLQdtqeLLQEENRQKLSLSTKLKQVEDEKnsfreqleeeEEAKHNL 1376
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKN-RYESEIKTAESDLS----MELEKNNYYKELEERHMKIINDP----------VYKNRNY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1377 EKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQkDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDhqrqs 1456
Cdd:PRK01156 297 INDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLK----- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1457 acNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAreketkalslaralEEAMEQKAELERLNKQFRTEMEDLMSSKDD 1536
Cdd:PRK01156 371 --SIESLKKKIEEYSKNIERMSAFISEILKIQEIDP--------------DAIKKELNEINVKLQDISSKVSSLNQRIRA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1537 VGKSVHELEKSKRALEQQ----VEEMKTQLEELEDELQATEDAKLRLEVNLQamkaQFERDLQGRDEQSEEKKKQLVRQV 1612
Cdd:PRK01156 435 LRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIR----EIEIEVKDIDEKIVDLKKRKEYLE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1613 REMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRE-------------LDDTR 1679
Cdd:PRK01156 511 SEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYE----EIKNRYKSLKLEDLDSKRTswlnalavislidIETNR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1680 ASREEILAQAKENEKKLKSMEAEMiqlqeelaaaERAKRQAQQERDELADEIANSSGKGALALEEKRRLEaRIAQLEEEL 1759
Cdd:PRK01156 587 SRSNEIKKQLNDLESRLQEIEIGF----------PDDKSYIDKSIREIENEANNLNNKYNEIQENKILIE-KLRGKIDNY 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1760 EEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYK--ASITALEAKI 1837
Cdd:PRK01156 656 KKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINEtlESMKKIKKAI 735
|
....*
gi 2550219468 1838 AQLEE 1842
Cdd:PRK01156 736 GDLKR 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
879-1120 |
2.48e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 879 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcaeaEELRARLTAKKQELeeicHDLEARVEEEEERCQHLQAE 958
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQL----------AALERRIAALARRI----RALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 959 KKKMQQNIqeleeqleeeesARQKLQLEKVTTEA-KLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEE-EEKS 1036
Cdd:COG4942 92 IAELRAEL------------EAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEElRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1037 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEE 1116
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAE 235
|
....
gi 2550219468 1117 AAQK 1120
Cdd:COG4942 236 AAAA 239
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
939-1942 |
2.49e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.13 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 939 HDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlEKVTTEAK----LKKLEEEQIILEDQNCKLAKE 1014
Cdd:TIGR01612 561 HEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELK-EKIKNISDkneyIKKAIDLKKIIENNNAYIDEL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1015 KKLLEDRIAEFTTNL-----TEEEEKSK----SLAKLKN--------------KHEAMITDLEERLRREEKQRQELEKTR 1071
Cdd:TIGR01612 640 AKISPYQVPEHLKNKdkiysTIKSELSKiyedDIDALYNelssivkenaidntEDKAKLDDLKSKIDKEYDKIQNMETAT 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1072 RKL-----EGDSTDLSDQIAELQAQI-AELKMQLAK-------KEEELQAALARVEEEAAQKNMALKKIRELESQISElQ 1138
Cdd:TIGR01612 720 VELhlsniENKKNELLDIIVEIKKHIhGEINKDLNKiledfknKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND-Q 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1139 EDLESerasrNKAEKQKRDLGEELEALKTeledtldsTAAQQELRSKREQEVnilkKTLEEEAKTHEAQIQEMRQKHSQA 1218
Cdd:TIGR01612 799 INIDN-----IKDEDAKQNYDKSKEYIKT--------ISIKEDEIFKIINEM----KFMKDDFLNKVDKFINFENNCKEK 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1219 VEELAEQL-EQTKRVKANLEKAKQTLE----NERGELANEVKVLLQGKGDSEHKRKKVEaqlQELQVKFNEGERVRtELA 1293
Cdd:TIGR01612 862 IDSEHEQFaELTNKIKAEISDDKLNDYekkfNDSKSLINEINKSIEEEYQNINTLKKVD---EYIKICENTKESIE-KFH 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1294 DKVTKLQVELDNVTGLLSQSDS---------------KSSKLTKDFS--ALESQLQDTQELLQEENRQKLSLSTklkqve 1356
Cdd:TIGR01612 938 NKQNILKEILNKNIDTIKESNLieksykdkfdntlidKINELDKAFKdaSLNDYEAKNNELIKYFNDLKANLGK------ 1011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1357 DEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVgcLETAEEVKRKLQKDLEGLSQRHEEKV-AAYDKLEKT 1435
Cdd:TIGR01612 1012 NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI--YNIIDEIEKEIGKNIELLNKEILEEAeINITNFNEI 1089
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1436 KTRLqqelddllvdldhqrqsacnlekKQKKFDQLLAEEktiSAKYAEERDRAEAEAREKETKALSLARALEEAmeqKAE 1515
Cdd:TIGR01612 1090 KEKL-----------------------KHYNFDDFGKEE---NIKYADEINKIKDDIKNLDQKIDHHIKALEEI---KKK 1140
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1516 LERLNKQFRTEMEDLMSSKDDV--GKSVHELEKSKRALEQQVEEMKTQLEELE---DELQATEDAKLRLEvNLQAMKAQF 1590
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDVADKAisNDDPEEIEKKIENIVTKIDKKKNIYDEIKkllNEIAEIEKDKTSLE-EVKGINLSY 1219
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1591 ERDLQGRD-EQSEEKKKQLVRQVREMEAELE--DERKQRSMAVAARKKLEMDLK------------DLEAHIDSanKNRD 1655
Cdd:TIGR01612 1220 GKNLGKLFlEKIDEEKKKSEHMIKAMEAYIEdlDEIKEKSPEIENEMGIEMDIKaemetfnishddDKDHHIIS--KKHD 1297
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1656 EAIKQLRKLQAQM-KDCMRE--LDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAEraKRQAQQERDELADEIA 1732
Cdd:TIGR01612 1298 ENISDIREKSLKIiEDFSEEsdINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNK--IKKIIDEVKEYTKEIE 1375
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1733 NSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDrlKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELK 1812
Cdd:TIGR01612 1376 ENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDD--KDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVL 1453
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1813 VKLQEMEGT-------VKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKlKDVLLQVDDE---------- 1875
Cdd:TIGR01612 1454 LLFKNIEMAdnksqhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELFEQYKKDvtellnkysa 1532
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1876 ---RRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1942
Cdd:TIGR01612 1533 laiKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSL 1602
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
880-1341 |
2.84e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.50 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 880 EKQLAAENR--------LTEMETLQSQLMAEKLQLQEQLQAET---------ELCAEAEELR----------ARLTAKKQ 932
Cdd:PRK10246 232 EKQLLTAQQqqqqslnwLTRLDELQQEASRRQQALQQALAAEEkaqpqlaalSLAQPARQLRphweriqeqsAALAHTRQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 933 ELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlEKVTTEAKLKKLEEEQIILEDQNCKLA 1012
Cdd:PRK10246 312 QIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNN-ELAGWRAQFSQQTSDREQLRQWQQQLT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1013 KEKKLLeDRIAEFTTNLTeEEEKSKSLAKLKNKHEamitdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQI 1092
Cdd:PRK10246 391 HAEQKL-NALPAITLTLT-ADEVAAALAQHAEQRP-----LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1093 AELKMQLAKKEEELQAALARVEEEAaqknmalkKIRELESQISELQE---------------------DLESERASRNKA 1151
Cdd:PRK10246 464 NEMRQRYKEKTQQLADVKTICEQEA--------RIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLDAL 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1152 EKQKRDLGEE-------LEALKTEL---EDTLDSTAAQQELRSKREQEV----NILKKTLEE------EAKTHEAQIQEM 1211
Cdd:PRK10246 536 EKEVKKLGEEgaalrgqLDALTKQLqrdESEAQSLRQEEQALTQQWQAVcaslNITLQPQDDiqpwldAQEEHERQLRLL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1212 RQKHS-QAveELAEQLEQTKRVKANLEKAKQTLENERGELAnevkVLLQGKGDSE---HKRKKVEAQLQELQVKFNEGER 1287
Cdd:PRK10246 616 SQRHElQG--QIAAHNQQIIQYQQQIEQRQQQLLTALAGYA----LTLPQEDEEAswlATRQQEAQSWQQRQNELTALQN 689
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1288 VRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1341
Cdd:PRK10246 690 RIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLE 743
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1487-1900 |
3.54e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1487 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 1542
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDleqdyqaasdhlnlvqtalrqqekIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1608
Cdd:PRK04863 356 DLEELEERLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQQTRAIQYQQAvQALERAKQLcglpdl 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1609 -VRQVREMEAELEDERKQrsmAVAARKKLEMDLKDLEAhidsANKNRDEAIKQLRKLQAQMkdcmrelddtraSREEILA 1687
Cdd:PRK04863 436 tADNAEDWLEEFQAKEQE---ATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEV------------SRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1688 QAKENEKKLKSMEAEMIQLQE---ELAAAERAKRQaQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEeleeeqg 1764
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQlrmRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE------- 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1765 ntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKVKLQEMEgtvkSKYKASITALEAkIAQLEEQL 1844
Cdd:PRK04863 569 ---------------------SLSESVSEARER---RMALRQQLEQLQARIQRLA----ARAPAWLAAQDA-LARLREQS 619
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 1845 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKAS-------TRLKQLKRQL 1900
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSqpggsedPRLNALAERF 682
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
983-1202 |
3.93e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.21 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 983 LQLEKVTTEAKLKKLEEEQI---ILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEE--KSKSLAkLKNKHEAM------IT 1051
Cdd:PLN02939 175 LEMRLSETDARIKLAAQEKIhveILEEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1052 DLEERLRREEKQRQELEKTRRKLEgdSTDLSDQiaELQAQIAELKMQ-LAKKEEELQAALARVEEEAAQKNMALKKIREL 1130
Cdd:PLN02939 254 ETEERVFKLEKERSLLDASLRELE--SKFIVAQ--EDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDL 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 1131 ESQISELQEDLESERASRNKAEKQKRdLGEELEALKTELEDTLDSTAAQQELRSKREQEV-NILKKTLEEEAK 1202
Cdd:PLN02939 330 RDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFqDTLSKLKEESKK 401
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1065-1383 |
4.41e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1065 QELEKTRRKLegdstdlsDQIAELQAQIAELKMQLAKKEEELQ------AALARVEEEAAQKNMALKKIRELESQISELQ 1138
Cdd:PRK11281 63 QDLEQTLALL--------DKIDRQKEETEQLKQQLAQAPAKLRqaqaelEALKDDNDEETRETLSTLSLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1139 EDLESERASRNKAEKQkrdlgeeLEALKTELEDtldstaAQQEL--RSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHS 1216
Cdd:PRK11281 135 DQLQNAQNDLAEYNSQ-------LVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1217 QAVEELAEQLEQTKRVKANLekakQTLENERGELANEvkvllqgkgdsehKRKKVEAQLQELQVKFNEGERVRTElaDKV 1296
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNTQL----QDLLQKQRDYLTA-------------RIQRLEHQLQLLQEAINSKRLTLSE--KTV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1297 TKLQveldnvtgllsqsdsksskltkdfSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF-------REQLEEE 1369
Cdd:PRK11281 263 QEAQ------------------------SQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLtqqnlrvKNWLDRL 318
|
330
....*....|....
gi 2550219468 1370 EEAKHNLEKQIATL 1383
Cdd:PRK11281 319 TQSERNIKEQISVL 332
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1169-1944 |
4.52e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1169 LEDTLDSTAAQQELRSKREQEVNILKKTLEEEAkTHEAQIQEMRQKHSQAVEELA------EQLEQTKRVKANLEKAkqt 1242
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELA-ELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEEL--- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1243 leNERGELANEVKVLLQGKGDsEHKRKKVEAQLqelqvkfnEGERVRTELADKVTKLQVE-------------LDNVTGL 1309
Cdd:PRK04863 361 --EERLEEQNEVVEEADEQQE-ENEARAEAAEE--------EVDELKSQLADYQQALDVQqtraiqyqqavqaLERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1310 LSQSDSKSSKLTKDFSALESQLQD-TQELLQEEnrQKLSLSTKLKQV-----------------EDEKNSFREQLEEEEE 1371
Cdd:PRK04863 430 CGLPDLTADNAEDWLEEFQAKEQEaTEELLSLE--QKLSVAQAAHSQfeqayqlvrkiagevsrSEAWDVARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1372 AKHnLEKQIATLHAQVADMKKKMEDsvgcletaeevKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLD 1451
Cdd:PRK04863 508 QRH-LAEQLQQLRMRLSELEQRLRQ-----------QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1452 HQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAeAREKETKALSLARALEEAMEQKAELERlnkQFRTEMEdlm 1531
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR-LREQSGEEFEDSQDVTEYMQQLLERER---ELTVERD--- 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1532 sskddvgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQATEDAKLRLEVNLQ-----------AMKAQFERD 1593
Cdd:PRK04863 649 -----------ELAARKQALDEEIERLSqpggsedPRLNALAERFGGVLLSEIYDDVSLEdapyfsalygpARHAIVVPD 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1594 LQGrdeqseekkkqlvrqVREMEAELEDerkqrsmavaarkkLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDcmR 1673
Cdd:PRK04863 718 LSD---------------AAEQLAGLED--------------CPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--R 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1674 ELddtRASR--EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgALALE-----EKR 1746
Cdd:PRK04863 767 QW---RYSRfpEVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHL---AVAFEadpeaELR 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1747 RLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQIN-----TDLNLERSHAQKNENARQQLERqnkelkvkLQEMEGT 1821
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprLNLLADETLADRVEEIREQLDE--------AEEAKRF 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1822 VKsKYKASITALEAKIAQL---EEQLDNETKERQAAcKQVRRTEKKLKDVLLQVDdERRNAEQYKDQAD---KASTRLKQ 1895
Cdd:PRK04863 913 VQ-QHGNALAQLEPIVSVLqsdPEQFEQLKQDYQQA-QQTQRDAKQQAFALTEVV-QRRAHFSYEDAAEmlaKNSDLNEK 989
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 2550219468 1896 LKRQLEeaeeeaqRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1944
Cdd:PRK04863 990 LRQRLE-------QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1483-1725 |
4.55e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1483 EERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1562
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1563 EELEDELQATEDAKLRLEvNLQAMKAQFERDLQGRDeQSEEKKKQLVRQVREMEAELEDERKQRsmavaarkKLEMDLKD 1642
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKAL--------EKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1643 LEAHIDSANKNRDEAIKQLRKLQ-------AQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL----- 1710
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELrelrk 244
|
250 260
....*....|....*....|....
gi 2550219468 1711 ---------AAAERAKRQAQQERD 1725
Cdd:COG1340 245 elkklrkkqRALKREKEKEELEEK 268
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1014-1309 |
4.56e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.76 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1014 EKKL--LEDRIAEFTTnLTEE---EEKSKSLAKLKNKheamITDLEERLRREEKQRQELEktrrklegdsTDLSDQIAEL 1088
Cdd:PRK04778 171 EKQLenLEEEFSQFVE-LTESgdyVEAREILDQLEEE----LAALEQIMEEIPELLKELQ----------TELPDQLQEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1089 QAQIAELKMQ--------LAKKEEELQAALARVEEEAAQKNM--ALKKIRELESQISELQEDLESERASRNKAEKQKRDL 1158
Cdd:PRK04778 236 KAGYRELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDLdeAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1159 GEELEALKTELEDTldstaaQQELRskREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEK 1238
Cdd:PRK04778 316 PDFLEHAKEQNKEL------KEEID--RVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEE 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1239 AKQTL---ENERGELANEVKVLlqgkgdsehkrKKVEAQLQElqvkfnEGERVRTELADkvTKLQVELDNVTGL 1309
Cdd:PRK04778 388 ILKQLeeiEKEQEKLSEMLQGL-----------RKDELEARE------KLERYRNKLHE--IKRYLEKSNLPGL 442
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1477-1678 |
5.26e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1477 ISAKYAEERDRAEAEAREkeTKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkddvgksvhELEKSKRALEQQVE 1556
Cdd:COG2433 355 VEKKVPPDVDRDEVKARV--IRGLSIEEALEELIEKELPEEEPEAEREKEHEERELT---------EEEEEIRRLEEQVE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1557 EMKTQLEELEDELQATEDAKLRLEvnlqaMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsmavaARKKL 1636
Cdd:COG2433 424 RLEAEVEELEAELEEKDERIERLE-----RELSEARSEERREIRKDREISRLDREIERLERELEEERE-------RIEEL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2550219468 1637 EMDLKDLEAHIDSANKNRDEAIKQLRKLQaqmKDCMRELDDT 1678
Cdd:COG2433 492 KRKLERLKELWKLEHSGELVPVKVVEKFT---KEAIRRLEEE 530
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1030-1290 |
6.14e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1030 TEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAA 1109
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLR-------EELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1110 LARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQE 1189
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1190 VNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK 1269
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260
....*....|....*....|.
gi 2550219468 1270 KVEAQLQELQVKFNEGERVRT 1290
Cdd:COG4372 239 LDALELEEDKEELLEEVILKE 259
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1012-1754 |
7.02e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1012 AKEKKLLEDRIAEFTTNLTEEEEKsksLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQ--IAELQ 1089
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQ---LAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQekIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1090 AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESE-------RASRNKAEKQKR------ 1156
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyQQAVQALEKARAlcglpd 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1157 ----DLGEELEALKTElEDTLDST---------------------------------------AAQQELRSKREQevnil 1193
Cdd:COG3096 434 ltpeNAEDYLAAFRAK-EQQATEEvleleqklsvadaarrqfekayelvckiageversqawqTARELLRRYRSQ----- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1194 kKTLEEEAKTHEAQIQEMRQKHS--QAVEELAEQLEQTKRVK----ANLEKAKQTLENERGELANEVKVLLQGKGDSEHK 1267
Cdd:COG3096 508 -QALAQRLQQLRAQLAELEQRLRqqQNAERLLEEFCQRIGQQldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1268 RKKVEAQLQELQVKfnegERVRTELADKVTKLQ----VELDNVTGLLSQSDSKSSKLTKdFSALESQLQDTQELLQEENR 1343
Cdd:COG3096 587 LEQLRARIKELAAR----APAWLAAQDALERLReqsgEALADSQEVTAAMQQLLERERE-ATVERDELAARKQALESQIE 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1344 QKL----SLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATL----HAQVAD----MKKKMEDSVGCLETAEEVKRKL 1411
Cdd:COG3096 662 RLSqpggAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYFSALYgparHAIVVPdlsaVKEQLAGLEDCPEDLYLIEGDP 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1412 QKDLEGLSQRHEEKVAAYDKLEKTKTRlqqelddllvdldHQRQSACNL---EKKQKKFDQLLAEEKTISAKYAEER--- 1485
Cdd:COG3096 742 DSFDDSVFDAEELEDAVVVKLSDRQWR-------------YSRFPEVPLfgrAAREKRLEELRAERDELAEQYAKASfdv 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1486 ---DRAEAEAREKETKALSLA------RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEK--------SK 1548
Cdd:COG3096 809 qklQRLHQAFSQFVGGHLAVAfapdpeAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllAD 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1549 RALEQQVEEMKTQLEELED---ELQATEDAKLRLEVNLQAMK---AQFERdLQGRDEQSEEKKKQLVRQVREMEaeledE 1622
Cdd:COG3096 889 ETLADRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----E 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1623 RKQRSMAVAARKKLEM-----DLKD-LEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASReeilaQAKENEkkL 1696
Cdd:COG3096 963 VVQRRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR-----DAKQQT--L 1035
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1697 KSMEAEMIQLqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1754
Cdd:COG3096 1036 QELEQELEEL--GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1471-1620 |
7.63e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1471 LAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEdlmsskddvgksvhELEKSKRA 1550
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQ--------------KLEKRLLQ 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1551 LEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ--------SEEKKKQLVRQVREmEAELE 1620
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEILLEKVEE-EARHE 170
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1219-1632 |
7.72e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.45 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1219 VEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1298
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1299 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEenrqklslstklkqVEDEKNSFREQLEEEEEAKHNLEK 1378
Cdd:pfam19220 116 KTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQR--------------AEGELATARERLALLEQENRRLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1379 QIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDkLEKTKTRLQQELDDLLVDLDHQRQSAC 1458
Cdd:pfam19220 182 LSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLE-EAVEAHRAERASLRMKLEALTARAAAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1459 nlekkqkkfDQLLAEEKTisakyaEERDRAEAeAREKEtkalslaRALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVG 1538
Cdd:pfam19220 261 ---------EQLLAEARN------QLRDRDEA-IRAAE-------RRLKEASIERDTLERRLAGLEADLERRTQQFQEMQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1539 KSVHELEKSKRALEQQVEEMKTQLEELEDELQatedaklrlevNLQAMKAQFERDLqgrdeqsEEKKKQLVRQVREMEAE 1618
Cdd:pfam19220 318 RARAELEERAEMLTKALAAKDAALERAEERIA-----------SLSDRIAELTKRF-------EVERAALEQANRRLKEE 379
|
410
....*....|....
gi 2550219468 1619 LEDERKQRSMAVAA 1632
Cdd:pfam19220 380 LQRERAERALAQGA 393
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1543-1704 |
8.14e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDlqgrdeqseEKKKQLVRQVREMEA---EL 1619
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---------EEQLGNVRNNKEYEAlqkEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1620 EDERKQRSmavaarkklemdlkDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSM 1699
Cdd:COG1579 99 ESLKRRIS--------------DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*
gi 2550219468 1700 EAEMI 1704
Cdd:COG1579 165 REELA 169
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
858-1478 |
8.37e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 858 LLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEqlqaetelcaeaeelrarLTAKKQELEEI 937
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQS------------------LCKELDILQRE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 938 CHDLEARVEEEEERCQHLQAEKKKMQqniqeleeqLEEEESARQKLQLEKVTTEAKLKKLEEEqiiledqncKLAKEKKL 1017
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQE---------LQQRYAELCAAAITCTAQCEKLEKIHLQ---------ESAQSLKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1018 LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKqrqelektrrklegdstdlsdqiaelqaqiaelKM 1097
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP---------------------------------AR 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1098 QLAKKEEELQAALARVEEEAAQKNMALKKIR----ELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTL 1173
Cdd:TIGR00618 518 QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1174 DSTAAQQELRSKREQEVNILKKTLEeeaktHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEnergelane 1253
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQ-----PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH--------- 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1254 vkvLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQD 1333
Cdd:TIGR00618 664 ---ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDA 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1334 TQELLQEENRQKlslSTKLK-QVEDEKNSFREQLEEEEeakhnLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQ 1412
Cdd:TIGR00618 741 LNQSLKELMHQA---RTVLKaRTEAHFNNNEEVTAALQ-----TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1413 KDLEGLSQRHEEKVAAydKLEKTKTRLQQELDDLLVDLDHQRQsacnLEKKQKKFDQLLAEEKTIS 1478
Cdd:TIGR00618 813 PSDEDILNLQCETLVQ--EEEQFLSRLEEKSATLGEITHQLLK----YEECSKQLAQLTQEQAKII 872
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1125-1943 |
8.68e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1125 KKIRELESQISELQEDLESERASRNKAEKQKRDLGE---ELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEA 1201
Cdd:TIGR00606 217 EKACEIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVF 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1202 KTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL-LQGKGDSEHKRKKvEAQLQELQV 1280
Cdd:TIGR00606 297 QGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqLQADRHQEHIRAR-DSLIQSLAT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1281 kfnegeRVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTkdfSALESQLQDTQELLQEEnrqklslstkLKQVEDEKN 1360
Cdd:TIGR00606 376 ------RLELDGFERGPFSERQIKNFHTLVIERQEDEAKTA---AQLCADLQSKERLKQEQ----------ADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1361 SFREQLEEEeeaKHNLEKQIAtlhaQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQrhEEKVAAYDKLEKTKTRLQ 1440
Cdd:TIGR00606 437 GLGRTIELK---KEILEKKQE----ELKFVIKELQQLEGSSDRILELDQELRKAERELSK--AEKNSLTETLKKEVKSLQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1441 QELDdllvdldhqrqsacNLEKKQKKFDQLLAEEKtisakyaeerdraeaEAREKETKALSLARALEEAMEQKAELERLN 1520
Cdd:TIGR00606 508 NEKA--------------DLDRKLRKLDQEMEQLN---------------HHTTTRTQMEMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1521 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ 1600
Cdd:TIGR00606 559 SDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1601 SEekkkqlvrqVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRA 1680
Cdd:TIGR00606 639 SD---------LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1681 SREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalalEEKRRLEARIAQLEEELE 1760
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ----------RLKNDIEEQETLLGTIMP 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1761 EEQGNTELINDrlkKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKskykasitaleaKIAQL 1840
Cdd:TIGR00606 780 EEESAKVCLTD---VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD------------TVVSK 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1841 EEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRE 1920
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
810 820
....*....|....*....|....*..
gi 2550219468 1921 LEDATETADAMNR----EVSSLKNKLR 1943
Cdd:TIGR00606 925 KEELISSKETSNKkaqdKVNDIKEKVK 951
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1047-1302 |
9.12e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1047 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1126
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1127 IRELESQISELQEdlesERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQEL--RSKR-EQEVNILKKTLEEEAKT 1203
Cdd:COG1340 87 LNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1204 HE--AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLE--NERGELANEVKVLLQGKGDSEHKrkkveaQLQELQ 1279
Cdd:COG1340 163 KElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADelRKEADELHKEIVEAQEKADELHE------EIIELQ 236
|
250 260
....*....|....*....|...
gi 2550219468 1280 VKFNEGERVRTELADKVTKLQVE 1302
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKRE 259
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
880-1152 |
9.26e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.45 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 880 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 958
Cdd:pfam19220 124 ERQLAAETEQNRALEEENKALREEAQAAEKALQRAEgELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 959 KKKMQQNIQELEEQLEEEESARQKL------QLEKVTTE--AKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTtnlt 1030
Cdd:pfam19220 204 LDATRARLRALEGQLAAEQAERERAeaqleeAVEAHRAEraSLRMKLEALTARAAATEQLLAEARNQLRDRDEAIR---- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1031 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAL 1110
Cdd:pfam19220 280 AAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELT 359
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2550219468 1111 ARVEEEAAqknmalkkirELESQISELQEDLESERASRNKAE 1152
Cdd:pfam19220 360 KRFEVERA----------ALEQANRRLKEELQRERAERALAQ 391
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
993-1942 |
9.32e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.21 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 993 KLKKLEEEQIILEDQNCKLAKEKklLEDRIAEFTTNLTEE--EEKSKSLAKLKNKHEamitDLEERLRREEKQRQELEKT 1070
Cdd:TIGR01612 711 KIQNMETATVELHLSNIENKKNE--LLDIIVEIKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKY 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1071 RRKLEGDSTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVEEEAAQ-----KNMA---LKKIRELESQISELQEDLE 1142
Cdd:TIGR01612 785 KSKISEIKNHYNDQINIDNIKDEDAK-QNYDKSKEYIKTISIKEDEIFKiinemKFMKddfLNKVDKFINFENNCKEKID 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1143 SERAS----RNKAEKQKRDlgEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE--EEAKTHEAQIQEMRQKHS 1216
Cdd:TIGR01612 864 SEHEQfaelTNKIKAEISD--DKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEyiKICENTKESIEKFHNKQN 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1217 QAVEELAEQLEQTKRV----KANLEKAKQTLENERGELANEVKVLlqGKGDSEHKRKKVEAQLQELQV------------ 1280
Cdd:TIGR01612 942 ILKEILNKNIDTIKESnlieKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAKNNELIKYFNDLKAnlgknkenmlyh 1019
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1281 KFNEGERVRTELADKVTKLQVELDNV-----TGLLSQSDSKSSKLTKDFSALESQLQDTQELLQ---EENRQKLSLSTKL 1352
Cdd:TIGR01612 1020 QFDEKEKATNDIEQKIEDANKNIPNIeiaihTSIYNIIDEIEKEIGKNIELLNKEILEEAEINItnfNEIKEKLKHYNFD 1099
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1353 KQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETA----EEVKRKL--QKDLEGLSQRHEEKV 1426
Cdd:TIGR01612 1100 DFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQindlEDVADKAisNDDPEEIEKKIENIV 1179
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1427 AAYDK-----------------LEKTKTRLQ------------------QELDDLLVDLDHQRQSacnLEKKQKKFDQLL 1471
Cdd:TIGR01612 1180 TKIDKkkniydeikkllneiaeIEKDKTSLEevkginlsygknlgklflEKIDEEKKKSEHMIKA---MEAYIEDLDEIK 1256
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1472 AEEKTISAKYAEERD-RAEAEA--------------REKETKALSLAR----ALEEAMEQKAELERLNKQFRTEMEDLMS 1532
Cdd:TIGR01612 1257 EKSPEIENEMGIEMDiKAEMETfnishdddkdhhiiSKKHDENISDIRekslKIIEDFSEESDINDIKKELQKNLLDAQK 1336
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1533 SKDDVGKSVHE---------LEKSKRALEQqVEEMKTQLEE----LEDELQATED--AKLRLEVNLQAMKAQFERDLQGR 1597
Cdd:TIGR01612 1337 HNSDINLYLNEianiynilkLNKIKKIIDE-VKEYTKEIEEnnknIKDELDKSEKliKKIKDDINLEECKSKIESTLDDK 1415
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1598 D-EQSEEKKKQLVRQVREMEA-----------------------ELEDERKQRSMAVA---ARKKLEMDLKDLEAHIDSA 1650
Cdd:TIGR01612 1416 DiDECIKKIKELKNHILSEESnidtyfknadennenvlllfkniEMADNKSQHILKIKkdnATNDHDFNINELKEHIDKS 1495
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1651 NKNRDEAIKQLRKLQA------QMKDCMREL-------------DDTRASREEILAQAKE-----------NEKKLKSME 1700
Cdd:TIGR01612 1496 KGCKDEADKNAKAIEKnkelfeQYKKDVTELlnkysalaiknkfAKTKKDSEIIIKEIKDahkkfileaekSEQKIKEIK 1575
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1701 AEMIQLQEELAAAERAKRQA---QQERDELAD---EIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIN---- 1770
Cdd:TIGR01612 1576 KEKFRIEDDAAKNDKSNKAAidiQLSLENFENkflKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNlnsl 1655
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1771 ----DRLKKANLQIDQINTDLNLERSHAQKNENARQQlERQNKELKV--KLQEMEGTVKSKYKASITALEAKIAQLEEQL 1844
Cdd:TIGR01612 1656 qeflESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQ-HKKNYEIGIieKIKEIAIANKEEIESIKELIEPTIENLISSF 1734
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1845 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA 1924
Cdd:TIGR01612 1735 NTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKKSKSYLDDI 1814
|
1130
....*....|....*...
gi 2550219468 1925 teTADAMNREVSSLKNKL 1942
Cdd:TIGR01612 1815 --EAKEFDRIINHFKKKL 1830
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1641-1944 |
9.43e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1641 KDLEAHIDSANKNRDeaikqlrkLQAQMKDCMRELDDTRASREEILAQAKENEkklksmeaemiQLQEELAAAERAKRQA 1720
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETE-----------QLKQQLAQAPAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1721 QQERDELADEiANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANLQIDQINTDL-----NLERSHAQ 1795
Cdd:PRK11281 100 QAELEALKDD-NDEETRETLSTLSLRQLESRLAQ--------------TLDQLQNAQNDLAEYNSQLvslqtQPERAQAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1796 KNENAR--QQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNET-------KERQAACKQVRRTEKKLK 1866
Cdd:PRK11281 165 LYANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlqdllqKQRDYLTARIQRLEHQLQ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1867 dvLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANasrRKLQRELEDATETADAMNREVSSLKNKLRR 1944
Cdd:PRK11281 245 --LLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEIN---LQLSQRLLKATEKLNTLTQQNLRVKNWLDR 317
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
890-1614 |
9.49e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.95 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 890 TEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEIchdlearveEEEERCQHLQAEKKKMQQniQE 968
Cdd:PRK10246 198 TELEKLQAQASGVALLTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSL---------NWLTRLDELQQEASRRQQ--AL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 969 LEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQiilEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEA 1048
Cdd:PRK10246 267 QQALAAEEKAQPQLAALSLAQPARQLRPHWERI---QEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1049 MITDLEERLRREEKQR---QELEKTRRKLEGDSTDlSDQIAELQAQIAELKMQLAKKEEelqAALARVEEEAAQKNMALK 1125
Cdd:PRK10246 344 QQQSLNTWLAEHDRFRqwnNELAGWRAQFSQQTSD-REQLRQWQQQLTHAEQKLNALPA---ITLTLTADEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1126 KIRELESQISELQEDLeserasrnkAEKQKRdlgeelealKTELEDTLDSTAAQQELRskreqevnilkktleeeakthE 1205
Cdd:PRK10246 420 EQRPLRQRLVALHGQI---------VPQQKR---------LAQLQVAIQNVTQEQTQR---------------------N 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1206 AQIQEMRQKHSQAVEELAeqleqtkRVKA--NLEKAKQTLENERGELANEVKVLLQGKgdSEHKrkkVEAQLQELQVKFN 1283
Cdd:PRK10246 461 AALNEMRQRYKEKTQQLA-------DVKTicEQEARIKDLEAQRAQLQAGQPCPLCGS--TSHP---AVEAYQALEPGVN 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1284 EgeRVRTELADKVTKLQVEldnVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVED-----E 1358
Cdd:PRK10246 529 Q--SRLDALEKEVKKLGEE---GAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDiqpwlD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1359 KNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETaeevkrklQKDLEGLSQRHEEKVAAYDKLEKTKTR 1438
Cdd:PRK10246 604 AQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLT--------ALAGYALTLPQEDEEASWLATRQQEAQ 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1439 LQQelddllvdldhQRQSacNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEA---REKETKALSLARALEEAMEQKA- 1514
Cdd:PRK10246 676 SWQ-----------QRQN--ELTALQNRIQQLTPLLETLPQSDDLPHSEETVALdnwRQVHEQCLSLHSQLQTLQQQDVl 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1515 ELERLNK---QFRTEMED---------LMSSKDDvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQAtedaklrlevN 1582
Cdd:PRK10246 743 EAQRLQKaqaQFDTALQAsvfddqqafLAALLDE--ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQ----------H 810
|
730 740 750
....*....|....*....|....*....|..
gi 2550219468 1583 LQAMKAQFerDLQGRDEQSEEKKKQLVRQVRE 1614
Cdd:PRK10246 811 QQHRPDGL--DLTVTVEQIQQELAQLAQQLRE 840
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1639-1733 |
1.00e-05 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 50.07 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1639 DLKDLEAHIDS-----ANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEI---LAQAKENEKKLKSMEAEMIQLQEEL 1710
Cdd:PRK05431 3 DIKLIRENPEAvkealAKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEI 82
|
90 100
....*....|....*....|...
gi 2550219468 1711 AAAERAKRQAQQERDELADEIAN 1733
Cdd:PRK05431 83 KALEAELDELEAELEELLLRIPN 105
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1077-1188 |
1.07e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1077 DSTDLSDQIAELQAQIAELKMQLAKKE---------EELQAALARVEEEAAQKNMALKKIRELESQ--ISelQEDLESER 1145
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVS--QQELDEAR 154
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2550219468 1146 ASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ 1188
Cdd:COG1566 155 AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAA 197
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
880-1254 |
1.21e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 880 EKQLA-AENRLTEMETLQSQLM--AEKLQLQEQLQAE--TELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQH 954
Cdd:COG4913 344 EREIErLERELEERERRRARLEalLAALGLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 955 LQAEKKKMQQNIQELEEQLEEEESA-RQKLQLekvtTEAKLK--------KLEEEQ---------------IILEDQNCK 1010
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRDAlAEALGL----DEAELPfvgelievRPEEERwrgaiervlggfaltLLVPPEHYA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1011 LAKE--------KKLLEDRIAEFTTNLTEEEEKSKSLA-KLKNK-HEA--------------MITDLEERLRRE------ 1060
Cdd:COG4913 500 AALRwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAgKLDFKpHPFrawleaelgrrfdyVCVDSPEELRRHpraitr 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1061 -----------EKQRQELEKTRRKLEGDSTD----LSDQIAELQAQIAELKMQLAKKEEELQA--ALARVEEEAAQKNMA 1123
Cdd:COG4913 580 agqvkgngtrhEKDDRRRIRSRYVLGFDNRAklaaLEAELAELEEELAEAEERLEALEAELDAlqERREALQRLAEYSWD 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1124 LKKIRELESQISELQEDLESERASRNKAEKqkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1203
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1204 HEAQIQEMRQKHSQAVEELAEQL---EQTKRVKANLEKAKQTLENERGELANEV 1254
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1543-1727 |
1.28e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALEQQVEEMKTQLEELEDELQA----------TEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVR 1610
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQqlSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1611 QVREMEAELEDE-----RKQRSMAVAARKKLEM-------DLKDLEAHIDSANKNRDEAIKQ-LRKLQAQMkdcmRELDD 1677
Cdd:COG3206 252 GPDALPELLQSPviqqlRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRiLASLEAEL----EALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1678 TRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL 1727
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1018-1736 |
1.45e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1018 LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITD---LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAE 1094
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1095 LKmQLAKKEEELQAALARVEEeaaQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALkteledTLD 1174
Cdd:PRK04863 598 LA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL------SQP 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1175 STAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHS-QAVeelaeqleqtkrVKANLEKAKQTLENERGELanE 1253
Cdd:PRK04863 668 GGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALYGPArHAI------------VVPDLSDAAEQLAGLEDCP--E 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1254 VKVLLQGKGDS-EHKRKKVEAQLQELQVKFNE--------------GERVRTELADkvtKLQVELDNVTGLLSQSDSKSS 1318
Cdd:PRK04863 734 DLYLIEGDPDSfDDSVFSVEELEKAVVVKIADrqwrysrfpevplfGRAAREKRIE---QLRAEREELAERYATLSFDVQ 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1319 KLTKDFSALESQL---------QDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEeeeeakhNLEKQIATLhaqvad 1389
Cdd:PRK04863 811 KLQRLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLE-------QAKEGLSAL------ 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1390 mkKKMEDSVGCLetaeevkrklqkDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLdhqrQSACNLEKKQKKFDQ 1469
Cdd:PRK04863 878 --NRLLPRLNLL------------ADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLE----PIVSVLQSDPEQFEQ 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1470 LlaeektisakyaeERDRAEAEAREKETKAlsLARALEEAMEQKAELERLNKQFRTEMEDLMSSKddvgksvheLEKSKR 1549
Cdd:PRK04863 940 L-------------KQDYQQAQQTQRDAKQ--QAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEK---------LRQRLE 995
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1550 ALEQQVEEMKTQLEELEDelQATEDAKLrlevnLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMA 1629
Cdd:PRK04863 996 QAEQERTRAREQLRQAQA--QLAQYNQV-----LASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDELHAR 1068
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1630 VAA----RKKLEMDLKDLEAHIDSANknrdeaiKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN--EKKLKSMEAEM 1703
Cdd:PRK04863 1069 LSAnrsrRNQLEKQLTFCEAEMDNLT-------KKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERRLHRRELAY 1141
|
730 740 750
....*....|....*....|....*....|....*.
gi 2550219468 1704 IQLQEELAAAERAK---RQAQQERDELADEIANSSG 1736
Cdd:PRK04863 1142 LSADELRSMSDKALgalRLAVADNEHLRDVLRLSED 1177
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1205-1413 |
1.49e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1205 EAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnevkvllqgkgDSEHKRKKVEAQLQELQVKFNE 1284
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1285 GervRTELADKVTKLQVELDNVTGLLSQSDSKS-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1363
Cdd:COG3883 84 R---REELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1364 EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQK 1413
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1461-1943 |
1.54e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1461 EKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKEtkalslaraleeamEQKAELERLNKQFRTEmedlmssKDDVGKS 1540
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQE--------------ERQETSAELNQLLRTL-------DDQWKEK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1541 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELE 1620
Cdd:pfam12128 303 RDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL----ENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1621 DERKQRSMAVAArkKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMrelddtrasrEEILAQAKENEKKLKSME 1700
Cdd:pfam12128 379 RRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL----------EAGKLEFNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1701 AEMIQLQEELAAAERAKRQ--AQQERDELADEIANSSGKGALALE-EKRRLEARIAQLEEELEEEQGNTELINDRLKKAN 1777
Cdd:pfam12128 447 GELKLRLNQATATPELLLQleNFDERIERAREEQEAANAEVERLQsELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1778 LQID-QINTDLNLERSHAQKNEN------ARQQLERQNKE----------------LKVKLQEMEgtvKSKYKASITALE 1834
Cdd:pfam12128 527 LQLFpQAGTLLHFLRKEAPDWEQsigkviSPELLHRTDLDpevwdgsvggelnlygVKLDLKRID---VPEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1835 AKIAQLEEQLDNETKERQAACKQVRRTEKKLkdvllqvdderrnaeqykdqaDKASTRLKQLKRQLEEAEEEAQRANASR 1914
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGEL---------------------EKASREETFARTALKNARLDLRRLFDEK 662
|
490 500 510
....*....|....*....|....*....|
gi 2550219468 1915 RKLQRELEDATETA-DAMNREVSSLKNKLR 1943
Cdd:pfam12128 663 QSEKDKKNKALAERkDSANERLNSLEAQLK 692
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1464-1774 |
1.60e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.68 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1464 QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLN---KQFRTEMEDLMSSKDDVGKS 1540
Cdd:pfam19220 54 EALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1541 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER------DLQGRDEQSEEKKKQLVRQVRE 1614
Cdd:pfam19220 134 NRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEqaaelaELTRRLAELETQLDATRARLRA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1615 MEAELEDERKQRSMAVAA-----------RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRe 1683
Cdd:pfam19220 214 LEGQLAAEQAERERAEAQleeaveahraeRASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIER- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1684 eilaqaKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQ 1763
Cdd:pfam19220 293 ------DTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVER 366
|
330
....*....|.
gi 2550219468 1764 GNTELINDRLK 1774
Cdd:pfam19220 367 AALEQANRRLK 377
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1104-1284 |
1.92e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1104 EELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldstaaqQELR 1183
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-------EARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1184 SKREQEVNILKKTLEEEAKTHEAQIQEMRQkhSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGD 1263
Cdd:COG1579 76 KKYEEQLGNVRNNKEYEALQKEIESLKRRI--SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|.
gi 2550219468 1264 SEHKRKKVEAQLQELQVKFNE 1284
Cdd:COG1579 154 LEAELEELEAEREELAAKIPP 174
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1512-1941 |
2.03e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1512 QKAELERLNKQFRTEMEDLMSSKD---DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKA 1588
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKelkNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1589 QFERDLQGRDEQSEEKKKqlvrqvreMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQM 1668
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNK--------LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1669 KDCMRELDDTRASR---EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEK 1745
Cdd:TIGR04523 183 LNIQKNIDKIKNKLlklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1746 RRLEARIAQLeeeleeeQGNTELINDRLKKANLQIDQINTDLnlERSHAQKNENARQQLERQNKELKVKLQEMEGTVkSK 1825
Cdd:TIGR04523 263 NKIKKQLSEK-------QKELEQNNKKIKELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI-SQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1826 YKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVL--------------LQVDDERRNAEQYKDQADKAST 1891
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsykqeiknleSQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1892 RLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1941
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1483-1725 |
2.23e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 48.10 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1483 EERDRAEAEAREKETKalsLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTql 1562
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1563 eeLEDELQATEDAKLRLEVNLQAMKaqferdlqGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDL-- 1640
Cdd:pfam00261 83 --LENRALKDEEKMEILEAQLKEAK--------EIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1641 -----KDLEAHIDSANKNRDEAIKQLRKLQAQMKdcmrelddtrasreEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1715
Cdd:pfam00261 153 vgnnlKSLEASEEKASEREDKYEEQIRFLTEKLK--------------EAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|
gi 2550219468 1716 AKRQAQQERD 1725
Cdd:pfam00261 219 KYKAISEELD 228
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1199-1928 |
2.75e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1199 EEAKTHEAQIQEMRQKHSQAVEELAE---QLEQTKRVKANLEKAKQTLENERgELANEVKVLLQGKGDSEHKRKKVEAQL 1275
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEeqyRLVEMARELEELSARESDLEQDY-QAASDHLNLVQTALRQQEKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1276 QELQVKFNEGERVRTELADKVTKLQVELDNVTgllSQSDSKSSKLTKDFSALESQ-------------LQDTQELLQEEN 1342
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAE---EEVDSLKSQLADYQQALDVQqtraiqyqqavqaLEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1343 ---------------------RQKLSLSTKLKQVEDEKNSF-----------------------REQLEEEEEAKHNLEk 1378
Cdd:COG3096 434 ltpenaedylaafrakeqqatEEVLELEQKLSVADAARRQFekayelvckiageversqawqtaRELLRRYRSQQALAQ- 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1379 QIATLHAQVADmkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAC 1458
Cdd:COG3096 513 RLQQLRAQLAE-----------LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1459 NLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLA--RALEEAMEQKAELERLNKQfrtemedlmsSKDd 1536
Cdd:COG3096 582 ELRQQL---EQLRARIKELAARAPAWLAAQDALERLREQSGEALAdsQEVTAAMQQLLEREREATV----------ERD- 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1537 vgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQAT-----------EDA--------KLR---LEVNLQAMK 1587
Cdd:COG3096 648 ------ELAARKQALESQIERLSqpggaedPRLLALAERLGGVllseiyddvtlEDApyfsalygPARhaiVVPDLSAVK 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1588 AQF-------------ERDLQGRDEQS----EEKKKQLV----RQVR--------------------EMEAELEDERKQR 1626
Cdd:COG3096 722 EQLagledcpedlyliEGDPDSFDDSVfdaeELEDAVVVklsdRQWRysrfpevplfgraarekrleELRAERDELAEQY 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1627 SMAVAARKKLEMDLKDLEA----HIDSA-NKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1701
Cdd:COG3096 802 AKASFDVQKLQRLHQAFSQfvggHLAVAfAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLP 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1702 EMIQLQEElAAAERAkRQAQQERDElADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQID 1781
Cdd:COG3096 882 QANLLADE-TLADRL-EELREELDA-AQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIF 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1782 QInTDLnLERSHAQKNENARQQLERQ---NKELKVKLQEMEgTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQV 1858
Cdd:COG3096 959 AL-SEV-VQRRPHFSYEDAVGLLGENsdlNEKLRARLEQAE-EARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTL 1035
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1859 RRTEKKLKDVLLQVDDE-----RRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETA 1928
Cdd:COG3096 1036 QELEQELEELGVQADAEaeeraRIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1054-1233 |
2.75e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.72 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1054 EERLRREEKQRQ-ELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlAKKEEELQAALARVEEEAAQKNMalkkirELES 1132
Cdd:COG2268 211 ETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEERRE-AETARAEAEAAYEIAEANAEREV------QRQL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1133 QISELQEDLESERASRNKAEKQ-KRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVniLKKTLEEEAKTHEAQIQEM 1211
Cdd:COG2268 284 EIAEREREIELQEKEAEREEAElEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG--KRALAEAWNKLGDAAILLM 361
|
170 180
....*....|....*....|...
gi 2550219468 1212 R-QKHSQAVEELAEQLEQTKRVK 1233
Cdd:COG2268 362 LiEKLPEIAEAAAKPLEKIDKIT 384
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1109-1318 |
2.88e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1109 ALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKR-- 1186
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1187 -----EQEVNILKKTLE----EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1257
Cdd:COG3883 94 alyrsGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1258 LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSS 1318
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1040-1174 |
3.20e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.92 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1040 AKLKNKHEAM---ITDLEERLRREEKQRQELEKtrrklegdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1116
Cdd:COG0542 400 ARVRMEIDSKpeeLDELERRLEQLEIEKEALKK-------------EQDEASFERLAELRDELAELEEELEALKARWEAE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1117 aaqknmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLD 1174
Cdd:COG0542 467 -----------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1016-1251 |
3.86e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1016 KLLEDRIAEFTtnlteeeEKSKSLAKLKNKHEAMITDLEERLRREEKQRQEL-EKTRRklegdstDLSDQIAELQAQIAE 1094
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIE-------DLRRQLDTLTVERAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1095 LKMQLAKKEEELQAALARVEEEAAQKnmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELED--- 1171
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1172 -------------------TLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAV----EELAE---- 1224
Cdd:pfam00038 146 elqaqvsdtqvnvemdaarKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALrsakEEITElrrt 225
|
250 260 270
....*....|....*....|....*....|...
gi 2550219468 1225 ------QLEQTKRVKANLEKAKQTLEnERGELA 1251
Cdd:pfam00038 226 iqsleiELQSLKKQKASLERQLAETE-ERYELQ 257
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1483-1739 |
4.06e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 48.83 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1483 EERDRAEAEareketKALSLAR-ALEEAMEQKA---ELERLNKQFRTEMEDLMsskddvgksvhelekskRALEQQVEEM 1558
Cdd:pfam13779 480 EDGDLSDAE------RRLRAAQeRLSEALERGAsdeEIAKLMQELREALDDYM-----------------QALAEQAQQN 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1559 KTQLEELEDELQATEDAKlrlevNLQAMKAQFERDLQ-GRDEQSEekkkQLVRQVREMEAELEDERKQRSMAVAARKKLE 1637
Cdd:pfam13779 537 PQDLQQPDDPNAQEMTQQ-----DLQRMLDRIEELARsGRRAEAQ----QMLSQLQQMLENLQAGQPQQQQQQGQSEMQQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1638 MdLKDLEAHIDSANKNRDEAIKQLRKLQAQmkdcmrelDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK 1717
Cdd:pfam13779 608 A-MDELGDLLREQQQLLDETFRQLQQQGGQ--------QQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAE 678
|
250 260
....*....|....*....|....
gi 2550219468 1718 RQAQ--QERDELADEIANSSGKGA 1739
Cdd:pfam13779 679 RQQAlrRRLEELQDELKELGGKEP 702
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
671-695 |
4.37e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 45.80 E-value: 4.37e-05
10 20
....*....|....*....|....*
gi 2550219468 671 YKEQLAKLMATLRNTNPNFVRCIIP 695
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1077-1261 |
4.86e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 47.80 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1077 DSTDLSDQIAELQAQIAelkmqlakkeeELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEkqkr 1156
Cdd:pfam00529 52 DPTDYQAALDSAEAQLA-----------KAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQ---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1157 dlgEELEALKTELEDTlDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK-RVKAN 1235
Cdd:pfam00529 117 ---AQLAQAQIDLARR-RVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELsGAQLQ 192
|
170 180
....*....|....*....|....*..
gi 2550219468 1236 LEKAKQTLENERGELAN-EVKVLLQGK 1261
Cdd:pfam00529 193 IAEAEAELKLAKLDLERtEIRAPVDGT 219
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1459-1811 |
6.06e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1459 NLEKKQKKFDQLLAEEKTISA---KYAEERDRAEAEAREKEtkALSLARALEEAMEQKAElERLNKqfrteMEDLMSSKD 1535
Cdd:COG3096 276 HANERRELSERALELRRELFGarrQLAEEQYRLVEMARELE--ELSARESDLEQDYQAAS-DHLNL-----VQTALRQQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1536 DVGKSVHELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQ------------- 1595
Cdd:COG3096 348 KIERYQEDLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQTRAIQyqqavqalekara 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1596 -------------GRDEQSEEKKKQLVRQVREMEAEL---EDERKQ----------------RSMAVAARKKLEMDLKDL 1643
Cdd:COG3096 428 lcglpdltpenaeDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQfekayelvckiageveRSQAWQTARELLRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1644 EAHIDSANKNRDEaIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQE 1723
Cdd:COG3096 508 QALAQRLQQLRAQ-LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1724 RDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKanlqidqiNTDLNLERSHAQKnenARQQ 1803
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER--------EREATVERDELAA---RKQA 655
|
....*...
gi 2550219468 1804 LERQNKEL 1811
Cdd:COG3096 656 LESQIERL 663
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1402-1685 |
6.78e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 47.71 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1402 ETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTR----LQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLA--EEK 1475
Cdd:pfam05667 215 ELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRiaeqLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTtdTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1476 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQK--AELERLNKQFrtemEDLMSSKDDVGKSVHELEKSKRALEQ 1553
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQreEELEELQEQL----EDLESSIQELEKEIKKLESSIKQVEE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1554 QVEEMKTQLEELEDELQATE-------DAKLRLEvNLQAMKAQFERDLQGRDEQSEEKKKQLV---RQVREMEAELEDER 1623
Cdd:pfam05667 371 ELEELKEQNEELEKQYKVKKktldllpDAEENIA-KLQALVDASAQRLVELAGQWEKHRVPLIeeyRALKEAKSNKEDES 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1624 KQ------------RSMAVAARKKLEMdLKDLEAHIDSANK--NRD-------EAIKQLRKlqaQMKDCMRELDDTRASR 1682
Cdd:pfam05667 450 QRkleeikelrekiKEVAEEAKQKEEL-YKQLVAEYERLPKdvSRSaytrrilEIVKNIKK---QKEEITKILSDTKSLQ 525
|
...
gi 2550219468 1683 EEI 1685
Cdd:pfam05667 526 KEI 528
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1460-1619 |
7.29e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1460 LEKKQKKFDQLLAEEKTISAKYAE---ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD- 1535
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAEledELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1536 -DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVRE 1614
Cdd:COG1579 92 eALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
....*
gi 2550219468 1615 MEAEL 1619
Cdd:COG1579 172 IPPEL 176
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1501-1608 |
7.58e-05 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 45.00 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1501 SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE 1580
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90 100
....*....|....*....|....*...
gi 2550219468 1581 VNLQAMKAQFERDLQGRDEQSEEKKKQL 1608
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRDREIEKLKERL 149
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1487-1895 |
7.61e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1487 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 1542
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDleqdyqaasdhlnlvqtalrqqekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1608
Cdd:COG3096 355 DLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQTRAIQYQQAvQALEKARALcglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1609 -VRQVREMEAELEDERKQRSMAV-AARKKLEMDlkdleahiDSANKNRDEAIKQLRKLQAQMkdcmrELDDTRASREEIL 1686
Cdd:COG3096 435 tPENAEDYLAAFRAKEQQATEEVlELEQKLSVA--------DAARRQFEKAYELVCKIAGEV-----ERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1687 AQAKEnekkLKSMEAEMIQLQEELAAAERAKRQaQQERDELADEIANSSGK---GALALEE-KRRLEARIAqleeeleee 1762
Cdd:COG3096 502 RRYRS----QQALAQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQqldAAEELEElLAELEAQLE--------- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1763 qgntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKVKLQEMEgtvkSKYKASITALEAkIAQLEE 1842
Cdd:COG3096 568 -----------------------ELEEQAAEAVEQ---RSELRQQLEQLRARIKELA----ARAPAWLAAQDA-LERLRE 616
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 1843 QLDNETKERQAACKQVRRTEKKLKdvllQVDDERRNAEQYKDQADKASTRLKQ 1895
Cdd:COG3096 617 QSGEALADSQEVTAAMQQLLERER----EATVERDELAARKQALESQIERLSQ 665
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1599-1754 |
8.37e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.97 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1599 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQ-----LRKLQAQMKDCMR 1673
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1674 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSSGKGALALEEkrRLEARIA 1753
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL-KARAKAAKAQEKVNEALSGIDSDDATSALE--RMEEKIE 175
|
.
gi 2550219468 1754 Q 1754
Cdd:COG1842 176 E 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1488-1736 |
1.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1488 AEAEAREKETKALSLARALEEAMEQKAELERlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELED 1567
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1568 EL-------QATEDAKLRLEVNLQA-------MKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsmAVAAR 1633
Cdd:COG3883 87 ELgeraralYRSGGSVSYLDVLLGSesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1634 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1713
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260
....*....|....*....|...
gi 2550219468 1714 ERAKRQAQQERDELADEIANSSG 1736
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1096-1242 |
1.03e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1096 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEdleserasrnkaekQKRDLGEELEALK---TELEDT 1172
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA--------------EVEELEAELEEKDeriERLERE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1173 LDSTAAQQELRSKREQEVNIlkktLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKANLEKAKQT 1242
Cdd:COG2433 450 LSEARSEERREIRKDREISR----LDREIERLERELEEERER----IEELKRKLERLKELWKLEHSGELV 511
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1072-1360 |
1.03e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.54 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1072 RKLEGDSTDlsdqIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKnmaLKKirELESQISE------LQEDLESER 1145
Cdd:PLN03229 422 KKREAVKTP----VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LKK--EIDLEYTEaviamgLQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1146 ASRNKAEKQK----RDLGEELEALKTELEDTLDSTAAQQELRSKRE--QEVNILKKTLEEEAKTHEAQiQEMRQKhSQAV 1219
Cdd:PLN03229 493 EEFSKANSQDqlmhPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKK-FKEV 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1220 EELAEQLEQTKRVKANLEKA------------KQTLENERGELANEVKVLLQGKG-DSEHKRKKveaQLQELQVKFNEGE 1286
Cdd:PLN03229 571 MDRPEIKEKMEALKAEVASSgassgdeldddlKEKVEKMKKEIELELAGVLKSMGlEVIGVTKK---NKDTAEQTPPPNL 647
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1287 RVRTE-LADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSL---STKLKQVEDEKN 1360
Cdd:PLN03229 648 QEKIEsLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEalnSSELKEKFEELE 725
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1010-1172 |
1.07e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1010 KLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ 1089
Cdd:PHA02562 196 QIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1090 --------------------------AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLES 1143
Cdd:PHA02562 276 kvikmyekggvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT 355
|
170 180 190
....*....|....*....|....*....|....*.
gi 2550219468 1144 ERASRNKAEK-------QKRDLGEELEALKTELEDT 1172
Cdd:PHA02562 356 LVDKAKKVKAaieelqaEFVDNAEELAKLQDELDKI 391
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1408-1643 |
1.10e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1408 KRKLQKDLEGLSQrheekVAAYDKLEKTKTR-LQQELDDLLVDLDH---------------QRQSACNLEKKQKKFDQLL 1471
Cdd:PHA02562 152 RRKLVEDLLDISV-----LSEMDKLNKDKIReLNQQIQTLDMKIDHiqqqiktynknieeqRKKNGENIARKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1472 AEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKqfrtemEDLMSSKDDV----GKSVHELEKS 1547
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK------VIKMYEKGGVcptcTQQISEGPDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1548 KRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAqfeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRS 1627
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250
....*....|....*.
gi 2550219468 1628 MAVAARKKLEMDLKDL 1643
Cdd:PHA02562 376 DNAEELAKLQDELDKI 391
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1485-1750 |
1.12e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.23 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1485 RDRAEAEAREKETKALSLARALEEAMEQkaeLERLNKQFRTEMEDLMS-SKDDVGKSVHELEKSKRALEQQVEEMKTQLE 1563
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEALDK---LRSYLPKLNPLREEKKKvSVKSLEELIKDVEEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1564 ELEDELQATEDAKLRLEVnLQAMKAQFERDLQGR---------DEQSEEKKKQLVRQVremEAELEDERKQRSMAVAArk 1634
Cdd:PRK05771 111 ELENEIKELEQEIERLEP-WGNFDLDLSLLLGFKyvsvfvgtvPEDKLEELKLESDVE---NVEYISTDKGYVYVVVV-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1635 klemdlkdleahidSANKNRDEAIKQLRKLQAQMKdcmrELDDTRASREEIlaqaKENEKKLKSMEAEMIQLQEELAAae 1714
Cdd:PRK05771 185 --------------VLKELSDEVEEELKKLGFERL----ELEEEGTPSELI----REIKEELEEIEKERESLLEELKE-- 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 2550219468 1715 rakrqaqqERDELADEIANSSGkgaLALEEKRRLEA 1750
Cdd:PRK05771 241 --------LAKKYLEELLALYE---YLEIELERAEA 265
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1205-1441 |
1.17e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1205 EAQIQEMRQKHSQAVEELAEQLEQtkrVKANLEKAKQTLENERGElanevkvllQGKGDSEHKRKKVEAQLQELQVKFNE 1284
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1285 gerVRTELADkvtkLQVELDNVTGLLSQSDSKSSKLTKD--FSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF 1362
Cdd:COG3206 231 ---ARAELAE----AEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1363 REQLEEE-EEAKHNLEKQIATLHAQVADMKKKMEdsvgclETAEEVKR--KLQKDLEGLSQRHEEKVAAYDKLEKtktRL 1439
Cdd:COG3206 304 RAQLQQEaQRILASLEAELEALQAREASLQAQLA------QLEARLAElpELEAELRRLEREVEVARELYESLLQ---RL 374
|
..
gi 2550219468 1440 QQ 1441
Cdd:COG3206 375 EE 376
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1062-1297 |
1.42e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1062 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAEL-KMQLAKKE-EELQAA---LARVEEEAAQKNMALKKIRELE----S 1132
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELeAAALQPGEeEELEEErrrLSNAEKLREALQEALEALSGGEggalD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1133 QISELQEDLesERASRnkAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQ-EVNilkktlEEE-AKTHE--AQI 1208
Cdd:COG0497 245 LLGQALRAL--ERLAE--YDPSLAELAERLESALIELEE------AASELRRYLDSlEFD------PERlEEVEErlALL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1209 QEMRQKHSQAVEEL-------AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLlqgkgdSEhKRKK--------VEA 1273
Cdd:COG0497 309 RRLARKYGVTVEELlayaeelRAELAELENSDERLEELEAELAEAEAELLEAAEKL------SA-ARKKaakklekaVTA 381
|
250 260 270
....*....|....*....|....*....|.
gi 2550219468 1274 QLQEL-------QVKFNEGERVRTELADKVT 1297
Cdd:COG0497 382 ELADLgmpnarfEVEVTPLEEPGPNGADQVE 412
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1095-1242 |
1.51e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1095 LKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQ--ISELQEDLESE-RASRNKAEKQKRDLGEELEALKTELED 1171
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1172 TLDStaaQQELrSKREQEVNILKKTLEEEAKTHEAQIQEMRQK--------HSQAVEELAEQLEQ------TKRVKANLE 1237
Cdd:PRK12704 105 LEKR---EEEL-EKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEILLEKVEEearheaAVLIKEIEE 180
|
....*
gi 2550219468 1238 KAKQT 1242
Cdd:PRK12704 181 EAKEE 185
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1395-1944 |
1.56e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1395 EDSVGCLETAEEVKRKLQKDLEglSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEE 1474
Cdd:TIGR00606 159 EDSNWPLSEGKALKQKFDEIFS--ATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1475 KTISAKYAEERDRAEAEAREKE---TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD---------------- 1535
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDeqlndlyhnhqrtvre 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1536 ------DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKK--- 1606
Cdd:TIGR00606 317 kerelvDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKnfh 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1607 QLVRQVREMEAEL---------EDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDE---AIKQLRKLQAQMKDCMrE 1674
Cdd:TIGR00606 397 TLVIERQEDEAKTaaqlcadlqSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDRIL-E 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1675 LDDTRASREEILAQAKENEKkLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANS------SGKGALALEEKRRL 1748
Cdd:TIGR00606 476 LDQELRKAERELSKAEKNSL-TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRtqmemlTKDKMDKDEQIRKI 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1749 EARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDL---NLERSHAQKNENA-RQQLERQNKEL------------- 1811
Cdd:TIGR00606 555 KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLaklNKELASLEQNKNHiNNELESKEEQLssyedklfdvcgs 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1812 ---KVKLQEMEGTVK--SKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQA 1886
Cdd:TIGR00606 635 qdeESDLERLKEEIEksSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1887 DKASTRLKqlKRQLEEAEEEAQRANASRRKLqreledatetadamnREVSSLKNKLRR 1944
Cdd:TIGR00606 715 ESELKKKE--KRRDEMLGLAPGRQSIIDLKE---------------KEIPELRNKLQK 755
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1648-1952 |
1.58e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1648 DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRE-EILAQAK---ENEKKLKSMEAEMIQLQEElaaaERAKRQAQQE 1723
Cdd:pfam17380 291 EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAiyaEQERMAMERERELERIRQE----ERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1724 RDELADEIANSSGKGALALEEKRRLEaRIAQLEEELEEEQGNTELINDRLKKANLQIDQINTdlnlERSHAQKNENARQQ 1803
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA----EQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1804 LERQNKELKVKLQEMEgtvKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRT-EKKLKDVLLQ-VDDERRNAEQ 1881
Cdd:pfam17380 442 EERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRKLL 518
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1882 YKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETA---DAMNREVSSLK----NKLRRGDLPFVVP 1952
Cdd:pfam17380 519 EKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMMRqiveSEKARAEYEATTP 596
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
981-1416 |
1.66e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 981 QKLQLEKVTTEAKLKKLE---EEQIILEDQNCKLAKEKKLLEDRIAEFTTnLTEEEEKSKSLAKLKNKHEAMITDLEErl 1057
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEIENEMGIEMDIKAEMET-FNISHDDDKDHHIISKKHDENISDIRE-- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1058 rreekqrqeleKTRRKLEGDS--TDLSDQIAELQAQIAELKMQLAKKEEELQ--AALARVEEEAAQKNMaLKKIRELESQ 1133
Cdd:TIGR01612 1306 -----------KSLKIIEDFSeeSDINDIKKELQKNLLDAQKHNSDINLYLNeiANIYNILKLNKIKKI-IDEVKEYTKE 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1134 ISELQEDLESERASRNKAEKQKRDlGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKK-----TLEEEAKTHEAQI 1208
Cdd:TIGR01612 1374 IEENNKNIKDELDKSEKLIKKIKD-DINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEesnidTYFKNADENNENV 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1209 Q------EMRQKHSQAV----------------EELAEQLEQTKRVKANLEKAKQTLENER---GELANEVKVLL----- 1258
Cdd:TIGR01612 1453 LllfkniEMADNKSQHIlkikkdnatndhdfniNELKEHIDKSKGCKDEADKNAKAIEKNKelfEQYKKDVTELLnkysa 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1259 --------QGKGDSE---------HKRKKVEAQLQELQVKFNEGERVRTElaDKVTK----------LQVELDNV-TGLL 1310
Cdd:TIGR01612 1533 laiknkfaKTKKDSEiiikeikdaHKKFILEAEKSEQKIKEIKKEKFRIE--DDAAKndksnkaaidIQLSLENFeNKFL 1610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1311 SQSD--SKSSKLTKDFSALESQLQ----DTQEllqeenrqklslsTKLKQVEDEKNSFREQLEEEEEAKHNLEKQ----- 1379
Cdd:TIGR01612 1611 KISDikKKINDCLKETESIEKKISsfsiDSQD-------------TELKENGDNLNSLQEFLESLKDQKKNIEDKkkeld 1677
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2550219468 1380 -----IATLHAQVADMKKKMEdsVGCLETAEEVKRKLQKDLE 1416
Cdd:TIGR01612 1678 eldseIEKIEIDVDQHKKNYE--IGIIEKIKEIAIANKEEIE 1717
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1325-1533 |
1.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1325 SALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETA 1404
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1405 EEVKRKLQ-----KDLEGLSQRHE--EKVAAYDK-----LEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLA 1472
Cdd:COG3883 99 GGSVSYLDvllgsESFSDFLDRLSalSKIADADAdlleeLKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1473 EEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS 1533
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
991-1339 |
1.75e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 991 EAKLKKLEEEQ------IILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR 1064
Cdd:PRK01156 325 HAIIKKLSVLQkdyndyIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1065 QELEKTRRKLEGDSTDLSDQIAELQAQIAEL---KMQLAKKEEELQA-------------------------ALARVEEE 1116
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALrenLDELSRNMEMLNGqsvcpvcgttlgeeksnhiinhyneKKSRLEEK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1117 AAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeLEALKTELEDTLDSTAAQQE--------------- 1181
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDkhdkyeeiknryksl 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1182 ----LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1257
Cdd:PRK01156 559 kledLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEI 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1258 LQGKGDSEHKRKKVE------AQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQL 1331
Cdd:PRK01156 639 QENKILIEKLRGKIDnykkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
....*...
gi 2550219468 1332 QDTQELLQ 1339
Cdd:PRK01156 719 NDINETLE 726
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1047-1730 |
1.76e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1047 EAMITDLEERLRREEKQRQE-LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakKEEELQAALARvEEEAAQKNMALK 1125
Cdd:NF041483 505 ERVRTEAIERATTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAAREL--REETERAIAAR-QAEAAEELTRLH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1126 KirELESQISELQEDLeseRASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE------------------------ 1181
Cdd:NF041483 582 T--EAEERLTAAEEAL---ADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEqeaerlrteaaadasaaraegenv 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1182 ---LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQK-HSQAVEELAEQLEQTKRVKAnleKAKQTLENERGELANEVKvl 1257
Cdd:NF041483 657 avrLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQERE-- 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1258 lQGKGDSEH----KRKKVEAQLQELQVKFNEGERVRTEL--ADKVTKLQVElDNVTGLLSQSDSKSSKLTkdfSALESQL 1331
Cdd:NF041483 732 -RAREQSEEllasARKRVEEAQAEAQRLVEEADRRATELvsAAEQTAQQVR-DSVAGLQEQAEEEIAGLR---SAAEHAA 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1332 QDTQELLQEENRQKLS--LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIAT-------LHAQVADMKKKM--EDSVGC 1400
Cdd:NF041483 807 ERTRTEAQEEADRVRSdaYAERERASEDANRLRREAQEETEAAKALAERTVSEaiaeaerLRSDASEYAQRVrtEASDTL 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1401 LETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAK 1480
Cdd:NF041483 887 ASAEQDAARTRADAREDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1481 YAE-ERDRAEAeareketkALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVheLEKSKRALEQQVEEMK 1559
Cdd:NF041483 967 TGEaERLRAEA--------AETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRT--LDEARKDANKRRSEAA 1036
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1560 TQLEELEDElQATEDAKLRLEVNLQAMKAQFERDLQGrDEQSEEKKKQLVRQVREMEAE----LEDERKQ--------RS 1627
Cdd:NF041483 1037 EQADTLITE-AAAEADQLTAKAQEEALRTTTEAEAQA-DTMVGAARKEAERIVAEATVEgnslVEKARTDadellvgaRR 1114
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1628 MAVAARKKLEMDLKDLEAHIDSAN-KNRDEAIKQLR----KLQAQMKDCMRELDDTRASREEILAQA------------K 1690
Cdd:NF041483 1115 DATAIRERAEELRDRITGEIEELHeRARRESAEQMKsageRCDALVKAAEEQLAEAEAKAKELVSDAnseaskvriaavK 1194
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2550219468 1691 ENEKKLKSMEAEMIQLQEElaaAERAKRQAQQERDELADE 1730
Cdd:NF041483 1195 KAEGLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEE 1231
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1011-1136 |
1.77e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1011 LAKEKKL-LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLrreekqrQELEKTRRKLEGDSTDLSDQIAELQ 1089
Cdd:PRK09039 71 LERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1090 AQIAELKMQLAKKEEELQAALARVEEEAAQ-------KNMAL-KKIRELESQISE 1136
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKiadlgrrLNVALaQRVQELNRYRSE 198
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1639-1733 |
1.97e-04 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 46.15 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1639 DLKDLEAHIDS-----ANKNRDEAIKQLRKLQAQMKDCMRELDDTRASR----EEIlAQAKENEKKLKSMEAEMIQLQEE 1709
Cdd:COG0172 3 DIKLIRENPEAvkealAKRGFDLDVDELLELDEERRELQTEVEELRAERnalsKEI-GKAKKKGEEAEALIAEVKELKEE 81
|
90 100
....*....|....*....|....
gi 2550219468 1710 LAAAERAKRQAQQERDELADEIAN 1733
Cdd:COG0172 82 IKELEEELKELEEELDELLLSIPN 105
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
994-1228 |
2.39e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 994 LKKLEEEQII-LEDQNCKLAKEK--KLLEDRI-AEFTTN-LTEEEEKSKSLAKLKNKHEamITDLEERLRREEKQRQELE 1068
Cdd:PRK05771 22 LEALHELGVVhIEDLKEELSNERlrKLRSLLTkLSEALDkLRSYLPKLNPLREEKKKVS--VKSLEELIKDVEEELEKIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1069 KTRRKLEGDSTDLSDQIAELQAQIAELK--------MQLAKKEEELQAALARVEEEaaqknmalkKIRELESQISELQED 1140
Cdd:PRK05771 100 KEIKELEEEISELENEIKELEQEIERLEpwgnfdldLSLLLGFKYVSVFVGTVPED---------KLEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1141 LESERASRN-----KAEKQKRDLGEELEALKTELEDTLDSTAAQQELrSKREQEVNILKKTLEEEakthEAQIQEMRQKH 1215
Cdd:PRK05771 171 YISTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSELI-REIKEELEEIEKERESL----LEELKELAKKY 245
|
250
....*....|...
gi 2550219468 1216 SQAVEELAEQLEQ 1228
Cdd:PRK05771 246 LEELLALYEYLEI 258
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1013-1169 |
2.65e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1013 KEKKL--LEDRIAEFTTNLTEEEEKSKSLaklknkhEAMITDLEERLRREEKQRQelektrrKLEGDSTDLSDQIAELQA 1090
Cdd:PRK09039 51 KDSALdrLNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERS-------RLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550219468 1091 QIAELKMQLAKKEEELQAALARVEEeaaqknmalkkireLESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL 1169
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVEL--------------LNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1020-1291 |
2.83e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1020 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERL-RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQ 1098
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKReERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1099 LAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRD--LGEELEALKTELEDTLDST 1176
Cdd:pfam02029 114 SWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEnfAKEEVKDEKIKKEKKVKYE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1177 AAQQELRSKREQEVnilkKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQlEQTKRVKAnlEKAKQTLENERGELANEVKV 1256
Cdd:pfam02029 194 SKVFLDQKRGHPEV----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREE-EAEVFLEA--EQKLEELRRRRQEKESEEFE 266
|
250 260 270
....*....|....*....|....*....|....*
gi 2550219468 1257 LLQgkgdseHKRKKVEAQLQELQVKFNEGERVRTE 1291
Cdd:pfam02029 267 KLR------QKQQEAELELEELKKKREERRKLLEE 295
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
879-1213 |
2.85e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 879 REKQLAAENRLtEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 958
Cdd:pfam07888 59 KEKERYKRDRE-QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 959 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKS 1038
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1039 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD-------QIAEL---QAQIAELKMQLAKKEEELQA 1108
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrTQAELhqaRLQAAQLTLQLADASLALRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1109 ALAR--VEEEAAQKNMALKK--IRELESQISELQEDLESERASRNKaekqkrdlgeeleaLKTELEDTLDSTAAQQELRS 1184
Cdd:pfam07888 298 GRARwaQERETLQQSAEADKdrIEKLSAELQRLEERLQEERMEREK--------------LEVELGREKDCNRVQLSESR 363
|
330 340
....*....|....*....|....*....
gi 2550219468 1185 KREQEVNILKKTLEEEAKTHEAQIQEMRQ 1213
Cdd:pfam07888 364 RELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1541-1928 |
2.92e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.79 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1541 VHELEKSKRAleqqVEEMKTQLEELE-DELQATED---AKLRLEvnlqamkaqfERDLQGRDEQSEEKKkqlvrqvreme 1616
Cdd:pfam05701 69 LEELESTKRL----IEELKLNLERAQtEEAQAKQDselAKLRVE----------EMEQGIADEASVAAK----------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1617 AELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQ-------LRKLQAQMKDCMRELDDTRASREeiLAQA 1689
Cdd:pfam05701 124 AQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRaeeavsaSKEIEKTVEELTIELIATKESLE--SAHA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1690 KENEKKLKSMEAEMIQLQEELAAaERAKRQAQQERDELADEIANS-------SGKGALALEEKRRLEARIAQLEEELEEE 1762
Cdd:pfam05701 202 AHLEAEEHRIGAALAREQDKLNW-EKELKQAEEELQRLNQQLLSAkdlksklETASALLLDLKAELAAYMESKLKEEADG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1763 QGNTELINDRLKKA-----------NLQIDQINTDLNLERSHAqknENARQQLERQNKELkVKLQEMEGtvkskyKASIT 1831
Cdd:pfam05701 281 EGNEKKTSTSIQAAlasakkeleevKANIEKAKDEVNCLRVAA---ASLRSELEKEKAEL-ASLRQREG------MASIA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1832 aleakIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRAN 1911
Cdd:pfam05701 351 -----VSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVE 425
|
410
....*....|....*..
gi 2550219468 1912 ASRRKLQRELEDATETA 1928
Cdd:pfam05701 426 SRLEAVLKEIEAAKASE 442
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1057-1188 |
3.07e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1057 LRRE-EKQRQELEKTRRKLegdsTDLSDQIA-------ELQAQIAELKMQLAKKEEE---LQAALARVEEEAAqknmalk 1125
Cdd:PRK09039 44 LSREiSGKDSALDRLNSQI----AELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGAGA------- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1126 kirELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL---EDTLDstAAQQELRSKREQ 1188
Cdd:PRK09039 113 ---AAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALD--ASEKRDRESQAK 173
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1078-1234 |
3.23e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.52 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1078 STDLSDQIAELQAQIAELKMQLA--KKEEELQAALARVEEEAAQKNMALKKIRELESQIS--ELQEDLESERASRNKAEK 1153
Cdd:pfam09731 282 NDDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRES 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1154 QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNIlKKTLEEEAKTHEAQIQEMRQK---HSQAVEELAEQLEQTK 1230
Cdd:pfam09731 362 YEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDI-KEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENR 440
|
....
gi 2550219468 1231 RVKA 1234
Cdd:pfam09731 441 KAQQ 444
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
963-1259 |
3.31e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.19 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 963 QQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKL 1042
Cdd:pfam15905 38 QPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKD-QKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1043 KNKHEAMITDLEERLRrEEKQRQELEKTRRKLEGDSTDLSDQIAELqaqiaelkMQLAKK-EEELQAALARVEEEAAQKN 1121
Cdd:pfam15905 117 KTSLSASVASLEKQLL-ELTRVNELLKAKFSEDGTQKKMSSLSMEL--------MKLRNKlEAKMKEVMAKQEGMEGKLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1122 MALKKIRELESQISELQE---DLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE 1198
Cdd:pfam15905 188 VTQKNLEHSKGKVAQLEEklvSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLE 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1199 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQ 1259
Cdd:pfam15905 268 EKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
992-1181 |
3.59e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.90 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 992 AKLKKLEEEQIILE----DQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR-QE 1066
Cdd:pfam04012 15 EGLDKAEDPEKMLEqairDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEkKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1067 LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARveEEAAQKNMALKK----------IRELEsQISE 1136
Cdd:pfam04012 95 LEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTslgslstssaTDSFE-RIEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2550219468 1137 LQEDLESERASRNKAEkQKRDLGEELEALKTELEDTLDSTAAQQE 1181
Cdd:pfam04012 172 KIEEREARADAAAELA-SAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1521-1944 |
3.64e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1521 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQferdlqgrdeq 1600
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQ----------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1601 seEKKKQLVRQVREMEAELEderkQRSMAVA-ARKKLEMdlkdLEAHIDSANKNRDEaikqlrkLQAQMKDCMRELD--D 1677
Cdd:PRK04863 348 --EKIERYQADLEELEERLE----EQNEVVEeADEQQEE----NEARAEAAEEEVDE-------LKSQLADYQQALDvqQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1678 TRASREEILAQAKENEKKL-KSMEAEMIQLQEELAAAERAKRQAQQERDEL------ADEIANSSGKgalALEEKRRLEA 1750
Cdd:PRK04863 411 TRAIQYQQAVQALERAKQLcGLPDLTADNAEDWLEEFQAKEQEATEELLSLeqklsvAQAAHSQFEQ---AYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1751 RIAQLEEELEEEQGNTELINDRLKKANLQidQINTDLN-LERSHAQknenaRQQLERQNKELKVKLQEMEgtvkskykAS 1829
Cdd:PRK04863 488 EVSRSEAWDVARELLRRLREQRHLAEQLQ--QLRMRLSeLEQRLRQ-----QQRAERLLAEFCKRLGKNL--------DD 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1830 ITALEAKIAQLEEQLD--NETKERQAAckqvRRTEkkLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEA 1907
Cdd:PRK04863 553 EDELEQLQEELEARLEslSESVSEARE----RRMA--LRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS 626
|
410 420 430
....*....|....*....|....*....|....*..
gi 2550219468 1908 QRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1944
Cdd:PRK04863 627 QDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1558-1747 |
3.71e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1558 MKTQLEELEDeLQATEDAKLRLEVNLQAMKAQFERdlqgrdeqSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLE 1637
Cdd:COG1579 2 MPEDLRALLD-LQELDSELDRLEHRLKELPAELAE--------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1638 MDLKDLEAHIDSANKNRD-EAI-KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1715
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEyEALqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|..
gi 2550219468 1716 AKRQAQQERDELADEIANSSGKGALALEEKRR 1747
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1027-1291 |
4.36e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1027 TNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIA-------ELQAQIAELKMQL 1099
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQelrekrdELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1100 AKKEEELQAALARVEE---EAAQKNMALKKIRELESQISELQEDLESERASRNKAEK---QKRDLGEELEALKTELEDTL 1173
Cdd:COG1340 81 DELNEKLNELREELDElrkELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKElveKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1174 DSTAAQQELRSKREQ--EVNILKKTLEEEAKTHEAQIQEMRQKH---SQAVEELAEQLEQTKRVKANLEKAKQTLENERG 1248
Cdd:COG1340 161 KLKELRAELKELRKEaeEIHKKIKELAEEAQELHEEMIELYKEAdelRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2550219468 1249 ELANEVKVLLQGKGDSEHKRKK--VEAQLQELQVKFNEGERVRTE 1291
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLKKGEKLTTE 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1356-1602 |
4.39e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1356 EDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLekt 1435
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1436 kTRLQQELDDLLVdldhqrqsacnlekkqkKFDQLLAeektiSAKYAEERDRAEAEAREKETKalslARALEEAMEQKAE 1515
Cdd:COG3883 92 -ARALYRSGGSVS-----------------YLDVLLG-----SESFSDFLDRLSALSKIADAD----ADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1516 LERLNKQFRTEMEDLMSSKDdvgksvhELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQ 1595
Cdd:COG3883 145 LEAKKAELEAKLAELEALKA-------ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
....*..
gi 2550219468 1596 GRDEQSE 1602
Cdd:COG3883 218 AAAAAAA 224
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
881-1214 |
5.48e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 881 KQLAAENRLTEMETLQSQL------MAEKLQLQEQLQAETELCAEAE----ELRARLTAKKQELEEI--CHDLEARVEEE 948
Cdd:pfam05557 123 AELELQSTNSELEELQERLdllkakASEAEQLRQNLEKQQSSLAEAEqrikELEFEIQSQEQDSEIVknSKSELARIPEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 949 EERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlekvtteaKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTN 1028
Cdd:pfam05557 203 EKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE--------REEKYREEAATLELEKEKLEQELQSWVKLAQDTGLN 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1029 LTEEEEKSKSLAKLKNK---HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA---KK 1102
Cdd:pfam05557 275 LRSPEDLSRRIEQLQQReivLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLlltKE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1103 EEELQAALARVEEEAAQKNMALKK---IRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELedTLDSTAAQ 1179
Cdd:pfam05557 355 RDGYRAILESYDKELTMSNYSPQLlerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL--QALRQQES 432
|
330 340 350
....*....|....*....|....*....|....*
gi 2550219468 1180 QELRSKREQEVNILKKTLEEeaktHEAQIQEMRQK 1214
Cdd:pfam05557 433 LADPSYSKEEVDSLRRKLET----LELERQRLREQ 463
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1677-1975 |
5.61e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1677 DTRASREEILAQAKENEKKLKSMEAEMIQLQEElAAAERAKRQAQQERDELADEIANSSGKgaLALEEKRRLEAriaQLE 1756
Cdd:NF012221 1532 DNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALET---NGQ 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1757 EELEEEQGNTELINDRLKKANLQIDQINTDLNlershaQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAK 1836
Cdd:NF012221 1606 AQRDAILEESRAVTKELTTLAQGLDALDSQAT------YAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQR 1679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1837 IAQLEEQLDNETKERQAAckqVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAeeeaqrANASRRK 1916
Cdd:NF012221 1680 HVDNQQKVKDAVAKSEAG---VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAA------ANDAQSR 1750
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1917 LQRELEDATETADAMNREVSSLknKLRRGDLPfvvprrmARKGA-GDG-SDEEVDGKADGA 1975
Cdd:NF012221 1751 GEQDASAAENKANQAQADAKGA--KQDESDKP-------NRQGAaGSGlSGKAYSVEGVAE 1802
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
990-1133 |
5.93e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 990 TEAKLKKLEEEQIILEDQNcKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEK 1069
Cdd:PRK01156 617 IDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKA 695
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1070 TRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKeEELQAALARVEE--EAAQKNMALKKIRELESQ 1133
Cdd:PRK01156 696 NRARLESTIEILRTRINELSDRINDINETLESM-KKIKKAIGDLKRlrEAFDKSGVPAMIRKSASQ 760
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
860-1094 |
6.24e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 860 QVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcaeaEELRARLTAKKQELEEich 939
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI----------AELRAELEAQKEELAE--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 940 dlearveeeeercqHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeqiiLEDQNCKLAKEKKLLE 1019
Cdd:COG4942 109 --------------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1020 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAE 1094
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAA 238
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
926-1510 |
6.29e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 926 RLTAKKQELEEICHDLEARVEEEeercQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILE 1005
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1006 D---QNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDleerlrREEKQRQELeKTRRKLEGDSTDLS 1082
Cdd:PRK01156 239 SalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIND------PVYKNRNYI-NDYFKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1083 DQIAELQAQIAELKmQLAKKEEELQAALARVEEEAAQKNmalkkirELESQISELQEDLESERASRNKAEKQKRDLGE-- 1160
Cdd:PRK01156 312 QILSNIDAEINKYH-AIIKKLSVLQKDYNDYIKKKSRYD-------DLNNQILELEGYEMDYNSYLKSIESLKKKIEEys 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1161 -ELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQkHSQAVEELAEQL------------- 1226
Cdd:PRK01156 384 kNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRE-NLDELSRNMEMLngqsvcpvcgttl 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1227 --EQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEA-QLQELQVKFNEGERVRTELADKVTKLQvEL 1303
Cdd:PRK01156 463 geEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARADLEDIKIKIN-EL 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1304 DNVTGLLSQSDSKSSKLtkDFSALESQLQDTQELLQEENrqklslSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATL 1383
Cdd:PRK01156 542 KDKHDKYEEIKNRYKSL--KLEDLDSKRTSWLNALAVIS------LIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1384 HAQVADMKKKMEDSVGCLET----AEEVKR---KLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQS 1456
Cdd:PRK01156 614 KSYIDKSIREIENEANNLNNkyneIQENKIlieKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA 693
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1457 ACNLEKKQKKFDQLLAEEKTISAKYAEERDRaeAEAREKETKALSLARALEEAM 1510
Cdd:PRK01156 694 KANRARLESTIEILRTRINELSDRINDINET--LESMKKIKKAIGDLKRLREAF 745
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1548-1720 |
6.86e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1548 KRALEQQVEEMKTQ----LEELEDELQATEDAKLrLEVN--LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELED 1621
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1622 ERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDcmrelddtrASREEILAQAKEnekKLKSMEA 1701
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEILLEKVEE---EARHEAA 172
|
170
....*....|....*....
gi 2550219468 1702 EMIQLQEELAAAErAKRQA 1720
Cdd:PRK12704 173 VLIKEIEEEAKEE-ADKKA 190
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1559-1850 |
7.04e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1559 KTQLEELEDELQATEDAKLRLEvnlqAMKAQFERDLQGRdeqsEEKKKQLVRQVRemeAELEDERkQRSMAVAARKKLEM 1638
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFE----ARQARLEREKAAR----EARHKKAAEARA---AKDKDAV-AAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1639 DLKDLEAHIDSANKNRDEAIKQLRKLQAqmkdcmrelddtRASREEILAQAKENEKKLKsmeaemIQlqeelAAAERAK- 1717
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQA------------RARQAEKQAAAAADPKKAA------VA-----AAIARAKa 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1718 RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIdqintdlnlershaqkn 1797
Cdd:PRK05035 560 KKAAQQAANAEAEEEVDPKKAAVA-AAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAI----------------- 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 1798 enARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKE 1850
Cdd:PRK05035 622 --ARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
854-1152 |
7.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 854 KVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETL---QSQLMAEKLQLQEQLQAETELCAEAEELRARLTAK 930
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 931 KQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKlqlekvttEAKLKKLEEEQIILEDQNCK 1010
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--------AEALKKEAEEAKKAEELKKK 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1011 LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDqiaELQA 1090
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE---ELDE 1787
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 1091 QIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELEsqISELQEDLESERASRNKAE 1152
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME--DSAIKEVADSKNMQLEEAD 1847
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1058-1429 |
7.64e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1058 RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISEL 1137
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1138 QEDLESERASRNKAEkqkrdlgEELEALKTE---LEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQK 1214
Cdd:COG4372 86 NEQLQAAQAELAQAQ-------EELESLQEEaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1215 hsqaVEELAEQLEQTKRVKANLEKAKQTLE-NERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA 1293
Cdd:COG4372 159 ----LESLQEELAALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1294 DKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAK 1373
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1374 HNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAY 1429
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1684-1858 |
7.80e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1684 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEEKRRLEARIAQLEEELEEEQ 1763
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-------LEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1764 GNTElindrLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKykasITALEAKIAQLEEQ 1843
Cdd:COG1579 87 NNKE-----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----KAELDEELAELEAE 157
|
170
....*....|....*
gi 2550219468 1844 LDNETKERQAACKQV 1858
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1022-1247 |
8.13e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1022 IAEFTTNLTEEEEKSKSLAKlknkhEAMITDLEE--------RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA 1093
Cdd:pfam15709 302 TFVVTGNMESEEERSEEDPS-----KALLEKREQekasrdrlRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMRE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1094 ELKMQLAKKEEELQAALARVEEEAAQknmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTL 1173
Cdd:pfam15709 377 ELELEQQRRFEEIRLRKQRLEEERQR--------QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAE 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1174 DSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVkANLEKAKQTLENER 1247
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARL-ALEEAMKQAQEQAR 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1325-1754 |
9.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1325 SALESQLQ-DTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEeeakHNLEKQIATLHAQVADMKKKmedsvgcLET 1403
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAE-------LEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1404 AEEVKRKLQKDLEgLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAE 1483
Cdd:COG4717 114 LREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1484 ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMED-----------------------------LMSSK 1534
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaaleerlkearlllliaaallallglggsLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1535 DDVGK------SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQL 1608
Cdd:COG4717 273 LTIAGvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1609 VRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIdsanknrdEAIKQLRKLQAQMKDCMRELDDTRASREEILAQ 1688
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL--------EQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1689 AKENEkklksMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGAL--ALEEKRRLEARIAQ 1754
Cdd:COG4717 425 LDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRE 487
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
993-1166 |
1.06e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 993 KLKKLEEEQIILEDQNCKL-AKE------KKLLEDRIAEFTTNLT----EEEEKSKSLAKLKNKHEAmITDLEERLRREE 1061
Cdd:smart00787 110 DVKLLMDKQFQLVKTFARLeAKKmwyewrMKLLEGLKEGLDENLEglkeDYKLLMKELELLNSIKPK-LRDRKDALEEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1062 KQRQELEKTRRKLEGDSTD-LSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkirELESQISELQED 1140
Cdd:smart00787 189 RQLKQLEDELEDCDPTELDrAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKS-------ELNTEIAEAEKK 261
|
170 180
....*....|....*....|....*.
gi 2550219468 1141 LESERASRNKAEKQKRDLGEELEALK 1166
Cdd:smart00787 262 LEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1068-1298 |
1.09e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1068 EKTRRKLEGDSTDLSDQIAELQAQiaelKMQLAKKEEELQAALARVEEeaaqknmalkkirelesqiseLQEDLEseras 1147
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEEL----ERELEQKAEEAEALLKEAEK---------------------LKEELE----- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1148 rnkaeKQKRDLGEELEALKTELEDtldstAAQQELRSKREQEVNILKKTLEEEAKTHEA----QIQEMRQKHSQAVEELA 1223
Cdd:PRK00409 555 -----EKKEKLQEEEDKLLEEAEK-----EAQQAIKEAKKEADEIIKELRQLQKGGYASvkahELIEARKRLNKANEKKE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1224 EQLEQTKRVKANLEKakqtlenerGElanEVKVL-LQGKGDSEHKRKKVEAQLQE----LQVKFNEGERVRTELADKVTK 1298
Cdd:PRK00409 625 KKKKKQKEKQEELKV---------GD---EVKYLsLGQKGEVLSIPDDKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKK 692
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1050-1189 |
1.09e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 42.67 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1050 ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK-KIR 1128
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELA 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1129 ELESQISELQEDLES-------ERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQE 1189
Cdd:pfam12795 160 ALKAQIDMLEQELLSnnnrqdlLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1554-1942 |
1.11e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1554 QVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLvRQVREMEAELEDERKQRSMAVAAR 1633
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI-RLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1634 KK----LEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEaemiQLQEE 1709
Cdd:pfam05557 82 KKyleaLNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE----QLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1710 LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLeARIAQLEEELeeeqgntelinDRLKKANLQIDQINTDLNL 1789
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKEL-----------ERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1790 ershaqknenarqqLERQNKELKVKLQEMEgtvksKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEK-KLKDV 1868
Cdd:pfam05557 226 --------------LKEEVEDLKRKLEREE-----KYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDlSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1869 LLQVDDERRNAEQYKDQADKASTR---------LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLK 1939
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEkarreleqeLAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYD 366
|
...
gi 2550219468 1940 NKL 1942
Cdd:pfam05557 367 KEL 369
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1489-1900 |
1.15e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.69 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1489 EAEAREKETKALSLARALEE--AMEQKAELERLNKQFRTEMEDLMSSK-DDVGKSVHELE---------KSKRAL---EQ 1553
Cdd:pfam06160 14 ELEERKNELMNLPVQEELSKvkKLNLTGETQEKFEEWRKKWDDIVTKSlPDIEELLFEAEelndkyrfkKAKKALdeiEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1554 QVEEMKTQLEELEDELQA--TEDAKLRLEVN-LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELE--DERKQRSM 1628
Cdd:pfam06160 94 LLDDIEEDIKQILEELDEllESEEKNREEVEeLKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSqfEELTESGD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1629 AVAARK---KLEMDLKDLEAHIDS-------ANKNRDEAIKQLRKLQAQMKDCMRELDDtrasrEEILAQAKENEKKLKS 1698
Cdd:pfam06160 174 YLEAREvleKLEEETDALEELMEDipplyeeLKTELPDQLEELKEGYREMEEEGYALEH-----LNVDKEIQQLEEQLEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1699 MEAEMIQLqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANL 1778
Cdd:pfam06160 249 NLALLENL--ELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEH--------------AEEQNKELKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1779 QIDQINTDLNL---ERSHAQKNENARQQLERQNKELKVKLQEMEGT---VKSKYK---ASITALEAKIAQLEEQLDNETK 1849
Cdd:pfam06160 313 ELERVQQSYTLnenELERVRGLEKQLEELEKRYDEIVERLEEKEVAyseLQEELEeilEQLEEIEEEQEEFKESLQSLRK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1850 ERQAACKQVRRTEKKLKDVLLQVddERRN----AEQYKDQADKASTRLKQLKRQL 1900
Cdd:pfam06160 393 DELEAREKLDEFKLELREIKRLV--EKSNlpglPESYLDYFFDVSDEIEDLADEL 445
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
929-1411 |
1.16e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 929 AKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEE-SARQKLQLEKVtteakLKKLEEEQIILEDQ 1007
Cdd:pfam05622 7 EEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTpGGKKYLLLQKQ-----LEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1008 NCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAmitdLEERLRREEKQRQELEKTRRKLEgDSTDLSDQIAE 1087
Cdd:pfam05622 82 RDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDI----LRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1088 LQAQIAELKMQLAKKEEELQAAlarveeeaaqkNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKT 1167
Cdd:pfam05622 157 LEERNAEYMQRTLQLEEELKKA-----------NALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1168 EledtldstaaQQELRSKREqevnILKKTLEE-----EAKTHEAQIQEMRQKHSQAVEELAEQLeQTKRVKANLEKakqt 1242
Cdd:pfam05622 226 E----------KERLIIERD----TLRETNEElrcaqLQQAELSQADALLSPSSDPGDNLAAEI-MPAEIREKLIR---- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1243 lenergeLANEVKVL-LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKssklT 1321
Cdd:pfam05622 287 -------LQHENKMLrLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSK----A 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1322 KDFSALESQLQDTQELLQEENRQklsLSTKLKQVEDEKNSFREQLEEEEEakhNLEkqiATLHAQVADMKKKMEDSVGCL 1401
Cdd:pfam05622 356 EDSSLLKQKLEEHLEKLHEAQSE---LQKKKEQIEELEPKQDSNLAQKID---ELQ---EALRKKDEDMKAMEERYKKYV 426
|
490
....*....|
gi 2550219468 1402 ETAEEVKRKL 1411
Cdd:pfam05622 427 EKAKSVIKTL 436
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1476-1930 |
1.21e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.74 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1476 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV 1555
Cdd:COG5278 72 TGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALM 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1556 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKK 1635
Cdd:COG5278 152 DEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1636 LEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1715
Cdd:COG5278 232 LELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1716 AKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQ 1795
Cdd:COG5278 312 AAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1796 KNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDE 1875
Cdd:COG5278 392 VLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1876 RRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1930
Cdd:COG5278 472 AALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1071-1200 |
1.27e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1071 RRKLEGDSTdlSDQIAELQAQIAELKMQlakkeeelQAALARVEEEAAQKnmalkKIRELESQISELQEDLESERAsRNK 1150
Cdd:COG0542 401 RVRMEIDSK--PEELDELERRLEQLEIE--------KEALKKEQDEASFE-----RLAELRDELAELEEELEALKA-RWE 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1151 AEKQkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEE 1200
Cdd:COG0542 465 AEKE---LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1131-1347 |
1.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1131 ESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELrskreqevnilkKTLEEEAKTHEAQIQE 1210
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE------LQAEL------------EALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1211 MRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER-GELANEVKVLLQ-GKGDSE------HKRKKVEAQLQELQVKF 1282
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKiADADADlleelkADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1283 NEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1347
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| Cortex-I_coil |
pfam09304 |
Cortexillin I, coiled coil; Members of this family are predominantly found in the ... |
1071-1174 |
1.36e-03 |
|
Cortexillin I, coiled coil; Members of this family are predominantly found in the actin-bundling protein Cortexillin I from Dictyostelium discoideum. They adopt a structure consisting of an 18-heptad-repeat alpha-helical coiled-coil, and are a prerequisite for the assembly of Cortexillin I.
Pssm-ID: 312712 [Multi-domain] Cd Length: 107 Bit Score: 40.37 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1071 RRKLEGDSTDLSDQIAELQAQIAELKM---QLAKKEEELQAALARVEEEAAQKNmalKKIRELESQISELQEDLESERAS 1147
Cdd:pfam09304 4 KERLEASKNSLANKLAGLENSLESEKTsreQLIKQKDELESLLASLEQENAERE---KRLRELEAKLDEALKNLELEKLA 80
|
90 100
....*....|....*....|....*..
gi 2550219468 1148 RNKAEKQKRDLGEELEALKTELEDTLD 1174
Cdd:pfam09304 81 RMELESRLSKTEKDKAILELKLAEALD 107
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1079-1156 |
1.44e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 1.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1079 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKR 1156
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1481-1661 |
1.44e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1481 YAEERDRAEAEAREKEtkalslARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1560
Cdd:PRK12705 26 KKRQRLAKEAERILQE------AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1561 qLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVrqVREMEAELEDERKQRSMAVAARKKLEMDL 1640
Cdd:PRK12705 100 -LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLL--LKLLDAELEEEKAQRVKKIEEEADLEAER 176
|
170 180
....*....|....*....|.
gi 2550219468 1641 KDLEAHIDSANKNRDEAIKQL 1661
Cdd:PRK12705 177 KAQNILAQAMQRIASETASDL 197
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1190-1518 |
1.46e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1190 VNILKKTLEEEAKTHEAQIQEMRQKHSQaveelaEQLEQTKRVKA-NLEKAKQTLENERgelANEVKVLLQGKGDSEHKR 1268
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQ------ERLRQEKEEKArEVERRRKLEEAEK---ARQAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1269 KKVEAQLQ----ELQVKFNEGERVRTEladkvtKLQVELDNVTGLlsqsdsksskltkdfsaleSQLQDTQELLQEENRQ 1344
Cdd:pfam17380 342 MAMEREREleriRQEERKRELERIRQE------EIAMEISRMREL-------------------ERLQMERQQKNERVRQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1345 KLSLSTKLKQVEDEKN-SFREQLEEEEEAKHNLEKqiatlhAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHE 1423
Cdd:pfam17380 397 ELEAARKVKILEEERQrKIQQQKVEMEQIRAEQEE------ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1424 E---KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR------- 1493
Cdd:pfam17380 471 ErkrKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRkqqemee 550
|
330 340
....*....|....*....|....*....
gi 2550219468 1494 ----EKETKALSLARALEEAMEQKAELER 1518
Cdd:pfam17380 551 rrriQEQMRKATEERSRLEAMEREREMMR 579
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
1053-1181 |
1.50e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 43.30 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1053 LEERLRREEKQR--QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlakKEEELQAALARVEEEAAQKNMALKKIREL 1130
Cdd:PRK00247 288 AEQRAQYREKQKekKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKT---RTAEKNEAKARKKEIAQKRRAAEREINRE 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1131 ESQisELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1181
Cdd:PRK00247 365 ARQ--ERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQV 413
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1074-1683 |
1.54e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1074 LEGDSTDLSDQIAELQAQIaelkmqlakkeeelqaalarvEEEAAQKNMALKKIRELESQIselqedleserasrNKAEK 1153
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQI---------------------ADDEKSHSITLKEIERLSIEY--------------NNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1154 QKRDLGEELEALKTELE--DTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEaqiqemrqkhSQAVEELAEQLEQTKR 1231
Cdd:PRK01156 233 DYNNLKSALNELSSLEDmkNRYESEIKTAESDLSMELEKNNYYKELEERHMKII----------NDPVYKNRNYINDYFK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1232 VKANLEKAKQTLENERGELanevkvllqgkgDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLS 1311
Cdd:PRK01156 303 YKNDIENKKQILSNIDAEI------------NKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1312 QSDSKSSKL------TKDFSALESQLQDTQELLQEE-NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLH 1384
Cdd:PRK01156 371 SIESLKKKIeeysknIERMSAFISEILKIQEIDPDAiKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1385 AQVAdmkkkmeDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVaayDKLEKTKTRLQQElddllvdLDHQRQSACNLEKkq 1464
Cdd:PRK01156 451 GQSV-------CPVCGTTLGEEKSNHIINHYNEKKSRLEEKI---REIEIEVKDIDEK-------IVDLKKRKEYLES-- 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1465 KKFDQLLAEEKTISAKYAEERD--RAEAEAREKETKALSLARALE----EAMEQKAE--LERLNKQFRTEMEDLMSSKDD 1536
Cdd:PRK01156 512 EEINKSINEYNKIESARADLEDikIKINELKDKHDKYEEIKNRYKslklEDLDSKRTswLNALAVISLIDIETNRSRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1537 VGKSVHELEKSKRALEQQVEEMKT----QLEELEDELQATEDAKLRLEVNLQAMKA------QFERDLQGRDEQsEEKKK 1606
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIEKlrgkidNYKKQIAEIDSI-IPDLK 670
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1607 QLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRELDDTRASRE 1683
Cdd:PRK01156 671 EITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS----DRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
877-1257 |
1.59e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 877 KVREKQlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQ 956
Cdd:pfam12128 475 RAREEQ---EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 957 AEKKKMQQNIQELEEQLEEEESARQ-------KLQLEKV----------TTEAKLKKLEE----EQIILEDQNCKLAKEK 1015
Cdd:pfam12128 552 GKVISPELLHRTDLDPEVWDGSVGGelnlygvKLDLKRIdvpewaaseeELRERLDKAEEalqsAREKQAAAEEQLVQAN 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1016 KLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE----EKQRQELEKTRRKLEGDSTDLSDQIaelQAQ 1091
Cdd:pfam12128 632 GELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERkdsaNERLNSLEAQLKQLDKKHQAWLEEQ---KEQ 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1092 IAELKMQLAKK----EEELQAALARVEEEAAQKNMALKkireleSQISELQEDLESERASRNKAEKQKRDLGEELEALKT 1167
Cdd:pfam12128 709 KREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAK------AELKALETWYKRDLASLGVDPDVIAKLKREIRTLER 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1168 ELEDTldstaaqqelrSKREQEV----NILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL 1243
Cdd:pfam12128 783 KIERI-----------AVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKAS 851
|
410
....*....|....
gi 2550219468 1244 ENERGELANEVKVL 1257
Cdd:pfam12128 852 EKQQVRLSENLRGL 865
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1073-1227 |
1.61e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.48 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1073 KLEGDSTDLSDQIAELQAQIA----ELKMQLAKKEEELQAALARVEEEAAQK---------NMALKKIRELESQISELQE 1139
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGpvaqELVDRLEKETEALRERLQKDLEEVRAKlepyleelqAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1140 DLEsERASRnKAEKQKRDLGEELEALKTELEDTLDSTAAQ-----QELRSKREQEVNILKKTLEEEAKTHEAQ----IQE 1210
Cdd:pfam01442 81 ELR-KRLNA-DAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQE 158
|
170
....*....|....*..
gi 2550219468 1211 MRQKHSQAVEELAEQLE 1227
Cdd:pfam01442 159 LREKLEPQAEDLREKLD 175
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1416-1653 |
1.66e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 43.67 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1416 EGLSQRHEEKVAAYDK--LEKTKTRLQQELddllvdldhQRQSAcNLEKKQKKFDQllAEEKTISAKYAEERDRAEAEAR 1493
Cdd:NF012221 1549 KHAKQDDAAQNALADKerAEADRQRLEQEK---------QQQLA-AISGSQSQLES--TDQNALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1494 EKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMssKDDVGKSvheLEKSKRALEQQVEEMKTQleeLEDELQATE 1573
Cdd:NF012221 1617 AVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQEQ---LDDAKKISGKQLADAKQR---HVDNQQKVK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1574 DAKLRLEVNL-QAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAElEDERKQRSMAVAARKKLEMDLKDLEAHIDSANK 1652
Cdd:NF012221 1689 DAVAKSEAGVaQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQ-QAESDANAAANDAQSRGEQDASAAENKANQAQA 1767
|
.
gi 2550219468 1653 N 1653
Cdd:NF012221 1768 D 1768
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1078-1300 |
1.71e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1078 STDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQIS-------ELQEDLESERASRNK 1150
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQelrekrdELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1151 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSK-----REQEVNILKKTLE----EEAKTHEAQIQEMRQKHSQAvEE 1221
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEierleWRQQTEVLSPEEEkelvEKIKELEKELEKAKKALEKN-EK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550219468 1222 LAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQ 1300
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1071-1318 |
1.94e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1071 RRKLEGDSTDLS----------DQIAELQAQIAELKMQL----------AKKEEELQA-ALARVEEEAAQKNMALKKIRE 1129
Cdd:PHA02562 152 RRKLVEDLLDISvlsemdklnkDKIRELNQQIQTLDMKIdhiqqqiktyNKNIEEQRKkNGENIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1130 LESQISELQEDL-------ESERASRNKAEKQKRDLGEELEALKTEL----EDTLDSTAAQQelrskREQEVNILKKtLE 1198
Cdd:PHA02562 232 IKAEIEELTDELlnlvmdiEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQ-----ISEGPDRITK-IK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1199 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRV---KANLEKAKQTLENERGELanevkvllqgkgdsehkrKKVEAQL 1275
Cdd:PHA02562 306 DKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKA------------------KKVKAAI 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2550219468 1276 QELQVKF----NEGERVRTELADKVTKLQ------VELDNVTGLLSQSDSKSS 1318
Cdd:PHA02562 368 EELQAEFvdnaEELAKLQDELDKIVKTKSelvkekYHRGIVTDLLKDSGIKAS 420
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1056-1188 |
2.06e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1056 RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKkeeeLQAALARVEEEAAQKNMALKKIRELESQIS 1135
Cdd:pfam00529 76 RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ----AQIDLARRRVLAPIGGISRESLVTAGALVA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1136 ELQEDLESERASRNKAEKQKRDLGEELEAL--KTELEDTLDSTAAQQELRSKREQ 1188
Cdd:pfam00529 152 QAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEAEAELKLAKLD 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1624-1918 |
2.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1624 KQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1703
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1704 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRlkKANLQIDQI 1783
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1784 NTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEK 1863
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1864 KLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQ 1918
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
981-1269 |
2.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 981 QKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE 1060
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1061 EKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAalARVEEEAAQKNMALKKIRELESQISELQED 1140
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA--LEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1141 LESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVE 1220
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2550219468 1221 ELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK 1269
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1219-1352 |
2.22e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1219 VEELAEQLEQTKRVKANLEkakQTLENERGELANevkvllqgkgdSEHKRKKVEAQLqelqvkfNEGERVRTELADKVTK 1298
Cdd:PRK09039 62 IAELADLLSLERQGNQDLQ---DSVANLRASLSA-----------AEAERSRLQALL-------AELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2550219468 1299 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELL-------QEENRQKLSLSTKL 1352
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQAKIADLGRRL 181
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1474-1624 |
2.29e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.18 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1474 EKTISAKYAEERDRAEAEAREKETKAL-SLARALEEAMEQ------------KAELERLNKQFRTEM----------EDL 1530
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKRCQALLqELSAPLEEKISQgsysvpggyqlyLEDREKLVEKYRQVPrkgvkaeevlQEF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1531 MSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDL-QGRDEQSEEKKKQLV 1609
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLrQLKEKMEEERENLLK 255
|
170
....*....|....*
gi 2550219468 1610 RQVREMEAELEDERK 1624
Cdd:cd16269 256 EQERALESKLKEQEA 270
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1096-1246 |
2.43e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1096 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDS 1175
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQ 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1176 TAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEmrqkhsQAVEELAEQL------EQTKRVKANLEKAKQTLENE 1246
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPE------QARKLLLKLLdaeleeEKAQRVKKIEEEADLEAERK 177
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1511-1659 |
2.53e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.74 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1511 EQKAELERLNKQfrtEMEDLMSSKDDVgksVHELEKSKRALEQ---QVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK 1587
Cdd:pfam05911 677 DLKTEENKRLKE---EFEQLKSEKENL---EVELASCTENLEStksQLQESEQLIAELRSELASLKESNSLAETQLKCMA 750
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 1588 AQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIK 1659
Cdd:pfam05911 751 ESYE-DLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDADQEDKK 821
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1653-1806 |
2.55e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1653 NRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEnekKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIA 1732
Cdd:PRK09039 50 GKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRA---SLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELD 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1733 NSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLerSHAQKNenarQQLER 1806
Cdd:PRK09039 127 SEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV--ALAQRV----QELNR 194
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
886-1175 |
2.75e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 886 ENRLTEMETLQSQLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQN 965
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELK---ELAEKRDELNAQVKELREEAQE----LREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 966 IQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEdriaefttnlteeeeKSKSLAKLKNK 1045
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVE---------------KIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1046 HEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK 1125
Cdd:COG1340 152 AKKAL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1126 KIRELESQISELQEDLESERASRNKAEKQKRDlgEELEALKTELEDTLDS 1175
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKK 278
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
903-1128 |
2.80e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 903 KLQLQEQLQAETELCAEAEELRARLTAKKQELEEIchDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQK 982
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEF--RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 983 LQLEKVTTEAKLKKLEEEQIILEdqnckLAKEKKLLEDRIAEFTTNLTEE--------EEKSKSLAKLKNKHEAMITDLE 1054
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNhpdvialrAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1055 ERLRREEKQRQELEKTRRKLEGDStdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIR 1128
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1124-1427 |
2.89e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1124 LKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELE----------ALKTELEDTLDSTAAQQELRSKREQEvniL 1193
Cdd:pfam17380 274 LLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVErrrkleeaekARQAEMDRQAAIYAEQERMAMERERE---L 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1194 KKTLEEEAKTHEAQIQE----MRQKHSQAVEELA-EQLEQTKRVKANLEKAKQT--LENERGELANEVKVLLQGKGDSEH 1266
Cdd:pfam17380 351 ERIRQEERKRELERIRQeeiaMEISRMRELERLQmERQQKNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1267 KRKKVEAQLQElQVKFNEGERVRTELADKVTKLQVELDNvtgllsQSDSKSSKLTKDFSALESQL--------------Q 1332
Cdd:pfam17380 431 EARQREVRRLE-EERAREMERVRLEEQERQQQVERLRQQ------EEERKRKKLELEKEKRDRKRaeeqrrkilekeleE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1333 DTQELLQEENRQKLSlstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQ 1412
Cdd:pfam17380 504 RKQAMIEEERKRKLL----EKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMR 579
|
330
....*....|....*
gi 2550219468 1413 KDLEGLSQRHEEKVA 1427
Cdd:pfam17380 580 QIVESEKARAEYEAT 594
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1321-1751 |
2.90e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1321 TKDFSALESQLQDTQELLQeenrqklslSTKLKQVEDEKNSFREQLEEeeeakhnLEKQIATLHAQVADMKKKMEDSVGC 1400
Cdd:PRK04778 78 TNSLPDIEEQLFEAEELND---------KFRFRKAKHEINEIESLLDL-------IEEDIEQILEELQELLESEEKNREE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1401 LETAEEVKRKLQKDLegLSQRHEEKVAaYDKLEKtktRLQqelddllvdldhqrqsacNLEKKQKKFDQLlaeekTISAK 1480
Cdd:PRK04778 142 VEQLKDLYRELRKSL--LANRFSFGPA-LDELEK---QLE------------------NLEEEFSQFVEL-----TESGD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1481 YAEERDRAEaEAREKETkalslarALEEAMEQ-KAELERLNKQFRTEMEDL------MSSKDDVGKSVhELEKSKRALEQ 1553
Cdd:PRK04778 193 YVEAREILD-QLEEELA-------ALEQIMEEiPELLKELQTELPDQLQELkagyreLVEEGYHLDHL-DIEKEIQDLKE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1554 QVEEMKTQLEELEdeLQATEDAKLRLEVNLQAMKAQFERDLQGRDEqSEEKKKQLVRQVREMEAELEDerkqrsmavaar 1633
Cdd:PRK04778 264 QIDENLALLEELD--LDEAEEKNEEIQERIDQLYDILEREVKARKY-VEKNSDTLPDFLEHAKEQNKE------------ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1634 KKLEMDLKDLEAHI-DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAA 1712
Cdd:PRK04778 329 LKEEIDRVKQSYTLnESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQG 408
|
410 420 430
....*....|....*....|....*....|....*....
gi 2550219468 1713 AERAKRQAQQERDELADEIANSsgkgalaleeKRRLEAR 1751
Cdd:PRK04778 409 LRKDELEAREKLERYRNKLHEI----------KRYLEKS 437
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1700-1867 |
2.99e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1700 EAEMIQLQEELAAAERAKRQAQQERDELadeianssgkgalaleekRRLEARIAQLEEELEEEQGNTELINDRLKKANLQ 1779
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRL------------------QALESELAISRQDYDGATAQLRAAQAAVKAAQAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1780 IDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSK---YKASITALEAKIAQLEEQLDNETKERQAACK 1856
Cdd:pfam00529 119 LAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLdqiYVQITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
170
....*....|.
gi 2550219468 1857 QVRRTEKKLKD 1867
Cdd:pfam00529 199 ELKLAKLDLER 209
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
979-1240 |
3.04e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 979 ARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLED-------------RIAEFTTN----LTEEEEKSKSLAK 1041
Cdd:TIGR01612 1556 AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflKISDIKKKindcLKETESIEKKISS 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1042 LK-NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSdqiaELQAQIAELKMQLAKKEEELQAALARVEEEAAQK 1120
Cdd:TIGR01612 1636 FSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIA 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1121 NMalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSkreqevNILkKTLEEE 1200
Cdd:TIGR01612 1712 NK-----EEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIA------GCL-ETVSKE 1779
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2550219468 1201 AKTHEaqiqEMRQKHSQAVEELAEQLEQTKRVKANLEKAK 1240
Cdd:TIGR01612 1780 PITYD----EIKNTRINAQNEFLKIIEIEKKSKSYLDDIE 1815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
877-1166 |
3.20e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 877 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEeeeercqhlQ 956
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA---------E 1684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 957 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEaKLKKLEEEQIILEDQNCKLAKEKKlledRIAEfttNLTEEEEKS 1036
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDK----KKAE---EAKKDEEEK 1756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1037 KSLAKLKNKHEAMITDLEERLRR--EEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAlarVE 1114
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSA---IK 1833
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1115 EEAAQKNMALKKIRELESQI----SELQEDLESErASRNKAEKQKRDLGEELEALK 1166
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKfnknNENGEDGNKE-ADFNKEKDLKEDDEEEIEEAD 1888
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1674-1913 |
3.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1674 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalaleekrRLEARIA 1753
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------------EAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1754 QLeeeleeeqgnTELINDRLK---KANLQIDQINTDLN-------LERSHAQK--NENARQQLERQnKELKVKLQEMegt 1821
Cdd:COG3883 83 ER----------REELGERARalyRSGGSVSYLDVLLGsesfsdfLDRLSALSkiADADADLLEEL-KADKAELEAK--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1822 vKSKYKASITALEAKIAQLEEQ---LDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKR 1898
Cdd:COG3883 149 -KAELEAKLAELEALKAELEAAkaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250
....*....|....*
gi 2550219468 1899 QLEEAEEEAQRANAS 1913
Cdd:COG3883 228 AAAAAAAAAAAAAAA 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1158-1545 |
3.30e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1158 LGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANle 1237
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1238 kakqtleneRGELANEVKVLLQGKGDSEHKRKKVEAQLQELqvkfnegervrtelADKVTKLQVELDNVTgllsQSDSKS 1317
Cdd:pfam07888 110 ---------SEELSEEKDALLAQRAAHEARIRELEEDIKTL--------------TQRVLERETELERMK----ERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1318 SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDS 1397
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1398 VGCLETAEEVKRKLQKDLEGL-SQR-------HEEKVAAYD---KLEKTKTRLQQELDDLLVDLDHQRQSAcnlEKKQKK 1466
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSMaAQRdrtqaelHQARLQAAQltlQLADASLALREGRARWAQERETLQQSA---EADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1467 FDQLLAEEKTISAKYAEER---DRAEAE-AREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVH 1542
Cdd:pfam07888 320 IEKLSAELQRLEERLQEERmerEKLEVElGREKDCNRVQLSESRRELQELKASLRVAQK----EKEQLQAEKQELLEYIR 395
|
...
gi 2550219468 1543 ELE 1545
Cdd:pfam07888 396 QLE 398
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1599-1803 |
3.59e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1599 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMREL--D 1676
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1677 DTRASREEILAQAK---------ENEKKLKSMEAEMIQ----LQEELAAAERAKRQAQQERDELADEIANSSGKGALALE 1743
Cdd:COG3883 99 GGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEelkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1744 EKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQ 1803
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1078-1302 |
3.60e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1078 STDLSDQIAELQAQIAE--------------LKMQLaKKEEELQAALARveeeaaqknmalkKIRELESQISELQEDLES 1143
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAkeksvrqqqqqrasLLAQL-KKQEEAISQASR-------------KLRETQNTLNQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1144 ERASRNKAEKQK----RDLGEELEAL-----KTELEDTLDSTAAQQE---------LRSKREQEVNILKKTLEEEAkthe 1205
Cdd:PRK11637 108 LNASIAKLEQQQaaqeRLLAAQLDAAfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQTREELA---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1206 AQIQEMRQKHSQAVEELAEQLEQtkrvkanlekaKQTLENERGELANEVKVLlqgkgdsEHKRKKVEAQLQELQVkfNEg 1285
Cdd:PRK11637 184 AQKAELEEKQSQQKTLLYEQQAQ-----------QQKLEQARNERKKTLTGL-------ESSLQKDQQQLSELRA--NE- 242
|
250
....*....|....*..
gi 2550219468 1286 ervrTELADKVTKLQVE 1302
Cdd:PRK11637 243 ----SRLRDSIARAERE 255
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1453-1612 |
3.74e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1453 QRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARalEEAMEQKAELERLNKQFRTEMEDlms 1532
Cdd:PRK00409 532 LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK--KEADEIIKELRQLQKGGYASVKA--- 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1533 skddvgksvHELEKSKRALEQQVEEMKTQL---EELEDELQATEDAKLR--------------LEVNLQA----MKAQfE 1591
Cdd:PRK00409 607 ---------HELIEARKRLNKANEKKEKKKkkqKEKQEELKVGDEVKYLslgqkgevlsipddKEAIVQAgimkMKVP-L 676
|
170 180
....*....|....*....|.
gi 2550219468 1592 RDLQGRDEQSEEKKKQLVRQV 1612
Cdd:PRK00409 677 SDLEKIQKPKKKKKKKPKTVK 697
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1084-1179 |
3.87e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 41.19 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1084 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalkkIRELESQISELQEDLESERASRNKAEKQkrDLGEELE 1163
Cdd:COG4223 1 EIAALEAAVAELPAQLTALEQRLAALEAAPAAAAA--------TAALEARLAALRAALAAAREAVAAAAAA--ALEARLA 70
|
90
....*....|....*.
gi 2550219468 1164 ALKTELEDTLDSTAAQ 1179
Cdd:COG4223 71 ALEAKAAAPEAEAAAA 86
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
1040-1233 |
3.91e-03 |
|
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related beta giardin proteins. During mitosis the SF-assemblin-based cytoskeleton is reorganized; it divides in prophase and is reduced to two dot-like structures at each spindle pole in metaphase. During anaphase, the two dots present at each pole are connected again. In telophase there is an asymmetrical outgrowth of new fibres. It has been suggested that SF-assemblin is involved in re-establishing the microtubular root system characteriztic of interphase cells after mitosis.
Pssm-ID: 284187 [Multi-domain] Cd Length: 247 Bit Score: 41.07 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1040 AKLKNKHEAmITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQI--AELQAQIAELKMQLAKKEEELQAALARVEEEA 1117
Cdd:pfam06705 5 VKLSNMNER-VSGFHDKMENEIEVKRVDEDTRVKMIKEAIAHLEKLiqTESKKRQESFEDIQEEFKKEIDNMQETIKEEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1118 AQKNMALKK-IRELESQISELQEDLESERASRNKAekqkrdlgeeLEALKTELEDTL-DSTAAQQELRSKREQEVNILKK 1195
Cdd:pfam06705 84 DDMAANFRKaLAELNDTINNVETNLQNEIAIHNDA----------IEALRKEALKSLnDLETGIATENAERKKMYDQLNK 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 2550219468 1196 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVK 1233
Cdd:pfam06705 154 KVAEGFARISAAIDTEKNARDSAVSAATTELTNTKLVE 191
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
904-1239 |
3.98e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 904 LQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQqniqeleeqleEEESARQKL 983
Cdd:pfam05622 62 LLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMD-----------ILRESSDKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 984 QLEKVTTEAKLKKLEEeqiiLEDqnckLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEA---MITDLEERLRRE 1060
Cdd:pfam05622 131 KKLEATVETYKKKLED----LGD----LRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETykrQVQELHGKLSEE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1061 EKQRQELEKTRRKLEG--------------DSTDLSDQIAEL---QAQIAELKMQLAKKEE---------------ELQA 1108
Cdd:pfam05622 203 SKKADKLEFEYKKLEEklealqkekerliiERDTLRETNEELrcaQLQQAELSQADALLSPssdpgdnlaaeimpaEIRE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1109 ALARVEEEaaQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQ 1188
Cdd:pfam05622 283 KLIRLQHE--NKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEEL---QKALQEQGSKAED 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 1189 EVNILKKTLEEEAKTHEAQIQemRQKHSQAVEELAEQLEQTKRVK-ANLEKA 1239
Cdd:pfam05622 358 SSLLKQKLEEHLEKLHEAQSE--LQKKKEQIEELEPKQDSNLAQKiDELQEA 407
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1544-1748 |
4.18e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1544 LEKSK-RALEQQVEEMKTQLEELEDELQATEDaklrLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDE 1622
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNK----NIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1623 RKQRSMAVAARKKLEMDLKDLEAHIDSANK----------------NRDEAIKQLRKLQAQMKDC---MRELDDTRASRE 1683
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELqhsLEKLDTAIDELE 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1684 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRL 1748
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1463-1632 |
4.20e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1463 KQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVH 1542
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAQFERDLqgrdeqsEEKKKQLVRQVREmEAELEDE 1622
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELY--RVAGLTPEQARKLLLKLLDAEL-------EEEKAQRVKKIEE-EADLEAE 175
|
170
....*....|
gi 2550219468 1623 RKQRSMAVAA 1632
Cdd:PRK12705 176 RKAQNILAQA 185
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1035-1221 |
4.34e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1035 KSKSLAKLKNKHEAMITDLEERLRREE--------KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL 1106
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEaikkeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1107 QaalarveeeaaqknmalKKIRELESQISELQEDLESerasrnkAEKQKrdlgEELEALKTELEDTLDSTAAQQelrskR 1186
Cdd:PRK12704 106 E-----------------KREEELEKKEKELEQKQQE-------LEKKE----EELEELIEEQLQELERISGLT-----A 152
|
170 180 190
....*....|....*....|....*....|....*
gi 2550219468 1187 EQEVNILKKTLEEEAKtHEAQIQeMRQKHSQAVEE 1221
Cdd:PRK12704 153 EEAKEILLEKVEEEAR-HEAAVL-IKEIEEEAKEE 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
881-1118 |
4.34e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 881 KQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKK 960
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNE---EYNELQAELEALQAEIDK----LQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 961 K----MQQNIQELEEQLEEEES-----ARQKLQLEKVTTEAKLKKLEEeqiiLEDQNCKLAKEKKLLEDRIAEFTTNLTE 1031
Cdd:COG3883 90 EraraLYRSGGSVSYLDVLLGSesfsdFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1032 EEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKtrrklegdstdlsdQIAELQAQIAELKMQLAKKEEELQAALA 1111
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA--------------ELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*..
gi 2550219468 1112 RVEEEAA 1118
Cdd:COG3883 232 AAAAAAA 238
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
983-1154 |
4.61e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 40.27 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 983 LQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEK 1062
Cdd:pfam15619 16 LQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1063 QRQELEKTRRKLEGDSTDLS-DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAA----QKNMALKKIRELESQISEL 1137
Cdd:pfam15619 96 ELLRLRDQLKRLEKLSEDKNlAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfrrQLAAEKKKHKEAQEEVKIL 175
|
170
....*....|....*..
gi 2550219468 1138 QEDLESERASRNKAEKQ 1154
Cdd:pfam15619 176 QEEIERLQQKLKEKERE 192
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1068-1305 |
4.99e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.59 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1068 EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQI----------SEL 1137
Cdd:pfam15742 33 EKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVlkqaqsiksqNSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1138 QEDLESERASRNKAEKQKRDLGEELE-ALKTELEDTLDSTAAQQELRSKREQEVnilkktlEEEAKTHEAQIQEMRQKHS 1216
Cdd:pfam15742 113 QEKLAQEKSRVADAEEKILELQQKLEhAHKVCLTDTCILEKKQLEERIKEASEN-------EAKLKQQYQEEQQKRKLLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1217 QAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK---KVEAQLQELQvkfNEGERVRTELA 1293
Cdd:pfam15742 186 QNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKsnqELSEKLSSLQ---QEKEALQEELQ 262
|
250
....*....|..
gi 2550219468 1294 DKVTKLQVELDN 1305
Cdd:pfam15742 263 QVLKQLDVHVRK 274
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
1005-1110 |
5.26e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 41.57 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1005 EDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRklegdstdlsdQ 1084
Cdd:smart00435 276 EKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKK-----------Q 344
|
90 100
....*....|....*....|....*.
gi 2550219468 1085 IAELQAQIAELKMQLAKKEEELQAAL 1110
Cdd:smart00435 345 IERLEERIEKLEVQATDKEENKTVAL 370
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1268-1599 |
5.50e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1268 RKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1347
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1348 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVA 1427
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1428 AydKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALE 1507
Cdd:COG4372 179 A--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1508 EAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK 1587
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330
....*....|..
gi 2550219468 1588 AQFERDLQGRDE 1599
Cdd:COG4372 337 AELADLLQLLLV 348
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1083-1300 |
5.58e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1083 DQIAELQAQIAELKMQLAkkeeelqaalarVEEEAAQknmalkkirELESQISELQEDLESerasrnkaekqkrdlgeeL 1162
Cdd:PRK09039 53 SALDRLNSQIAELADLLS------------LERQGNQ---------DLQDSVANLRASLSA------------------A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1163 EALKTELEDTLDSTAAQQELRSKREQEvniLKKTLEEEAKTHEaqiQEMRQkhsqaVEELAEQLEQTKRVKANLEKAKQt 1242
Cdd:PRK09039 94 EAERSRLQALLAELAGAGAAAEGRAGE---LAQELDSEKQVSA---RALAQ-----VELLNQQIAALRRQLAALEAALD- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1243 lenergelanevkvllqgkgDSEHKRKKVEAQLQELqvkfneGERVRTELADKVTKLQ 1300
Cdd:PRK09039 162 --------------------ASEKRDRESQAKIADL------GRRLNVALAQRVQELN 193
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
981-1421 |
5.61e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 41.59 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 981 QKLQLEKvttEAKLKKLEEEQII-------LEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDL 1053
Cdd:pfam15070 7 KQLQTER---DQYAENLKEEGAVwqqkmqqLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAGPSEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1054 EERLRRE-EKQRQELEKTRRKLEG---DSTDLSDQIAELQAQIAELKMQL---AKKEEELQAALARVEEEAAQKNMALKK 1126
Cdd:pfam15070 84 EQRLQEEaEQLQKELEALAGQLQAqvqDNEQLSRLNQEQEQRLLELERAAerwGEQAEDRKQILEDMQSDRATISRALSQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1127 IRELESQISELQED--------------LESERASRNKAEKQKRDLGEELEALKTELEdtLDSTAAqQELRSKREQEVNi 1192
Cdd:pfam15070 164 NRELKEQLAELQNGfvkltnenmeltsaLQSEQHVKKELAKKLGQLQEELGELKETLE--LKSQEA-QSLQEQRDQYLA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1193 lkkTLEEEAKTHEAQIQEMRQKHSQAVE--ELAEQLEQTK-RVKANLEKAKQTLENERGELANEVKvllqgkgdsehKRK 1269
Cdd:pfam15070 240 ---HLQQYVAAYQQLASEKEELHKQYLLqtQLMDRLQHEEvQGKVAAEMARQELQETQERLEALTQ-----------QNQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1270 KVEAQLQELQVKfNEGERVRTELADKvtklqveldnvtgllsqsDSKSSKLT--KDFsalesqlqDTQELLQEenrqklS 1347
Cdd:pfam15070 306 QLQAQLSLLANP-GEGDGLESEEEEE------------------EAPRPSLSipEDF--------ESREAMVA------F 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2550219468 1348 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLetAEEVKRKLQKDLEGLSQR 1421
Cdd:pfam15070 353 FNSALAQAEEERAELRRQLKEQKRRCRRLAQQAAPAQEEPEHEAHAPGTGGDSV--PVEVHQALQVAMEKLQSR 424
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1052-1398 |
5.75e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1052 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA-----ELKMQLAKKEEELQAALARVE--EEAAQKNM-- 1122
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSyeedsELKPSGQGGLDEEEAFLDRTAkrEERRQKRLqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1123 ALKKIRELESQISELQEDLESERASRNKAEKqkrdlgeelealkteledtldSTAAQQELRSKREQEVNILKKTLEEEAK 1202
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEEN---------------------SSWEKEEKRDSRLGRYKEEETEIREKEY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1203 THEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA--NEVKVLL-QGKGDSEHKRKKVEAQLQELQ 1279
Cdd:pfam02029 141 QENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvkYESKVFLdQKRGHPEVKSQNGEEEVTKLK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1280 VKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQE-----ENRQKLSLSTKLKQ 1354
Cdd:pfam02029 221 VTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEElkkkrEERRKLLEEEEQRR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2550219468 1355 VEDEKnsfrEQLEEEEEAKHNLEKQIATLHAQVADMKKKM-EDSV 1398
Cdd:pfam02029 301 KQEEA----ERKLREEEEKRRMKEEIERRRAEAAEKRQKLpEDSS 341
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
905-1247 |
5.79e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 905 QLQEQLQAETELCAEAEELRARLTAKKQELEEIchdlEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQ 984
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQL----EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 985 LEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR 1064
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1065 QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESE 1144
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1145 RASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAE 1224
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330 340
....*....|....*....|...
gi 2550219468 1225 QLEQTKRVKANLEKAKQTLENER 1247
Cdd:COG4372 348 VGLLDNDVLELLSKGAEAGVADG 370
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1521-1731 |
5.96e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.40 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1521 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATED-AKLRLEVNLQAMKAQFERD-----L 1594
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEErLAEALEKLEEAEKAADESErgrkvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1595 QGRDEQSEEKKKQLVRQVRemEAELEDERKQRSMAVAARKklemdLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRE 1674
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLK--EAKEIAEEADRKYEEVARK-----LVVVEGDLERAEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2550219468 1675 LDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1731
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDEL 213
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1632-1945 |
6.02e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1632 ARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELa 1711
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1712 aaeRAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQleeeleeeqgntelindrlkkanLQIDQINTDLNLER 1791
Cdd:COG1340 81 ---DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER-----------------------LEWRQQTEVLSPEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1792 shaqknenaRQQLERQNKELKVKLQEMEgtVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQ 1871
Cdd:COG1340 135 ---------EKELVEKIKELEKELEKAK--KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1872 VDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA--TETADAMNREVSSLKNKLRRG 1945
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALkrEKEKEELEEKAEEIFEKLKKG 279
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1547-1742 |
6.23e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1547 SKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdEQSEEkkkqlvrQVREMEAELEDERkqr 1626
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEA----ESSRE-------QLQELEEQLATER--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1627 smavAARKKLEMDLKDLEAHIDSankNRDEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSMEAEM 1703
Cdd:pfam09787 107 ----SARREAEAELERLQEELRY---LEEELRRSKATLQSRIKDREAEIEKLRNqltSKSQSSSSQSELENRLHQLTETL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2550219468 1704 IQLQEELAA--AERAKRQAQQERDELADEIANSSGKGALAL 1742
Cdd:pfam09787 180 IQKQTMLEAlsTEKNSLVLQLERMEQQIKELQGEGSNGTSI 220
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
888-1247 |
6.38e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 888 RLTEMETLQSQLMAEKLQLQEQLQA----ETELCAEAEELRARLTAKKQELEE---IChDLEARVEEEEERCQHLQAEKK 960
Cdd:PRK10246 427 RLVALHGQIVPQQKRLAQLQVAIQNvtqeQTQRNAALNEMRQRYKEKTQQLADvktIC-EQEARIKDLEAQRAQLQAGQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 961 -----KMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEEQIILEDQNCKLAKEKKLLED---RIAEFTTNLTEE 1032
Cdd:PRK10246 506 cplcgSTSHPAVEAYQALEPGVNQSRLDALEK-----EVKKLGEEGAALRGQLDALTKQLQRDESeaqSLRQEEQALTQQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1033 -EEKSKSLAKLKNKHEamitDLEERLRREEKQRQELEKTRRKLEgdstdLSDQIAELQAQIAELKMQLAKKEEELQAALA 1111
Cdd:PRK10246 581 wQAVCASLNITLQPQD----DIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1112 RveeeaaqknMALkKIRELESQISELQEDlESERASRNKAEKQKRDLGEELEALKTELE-----DTLDSTAAQQELRSKR 1186
Cdd:PRK10246 652 G---------YAL-TLPQEDEEASWLATR-QQEAQSWQQRQNELTALQNRIQQLTPLLEtlpqsDDLPHSEETVALDNWR 720
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2550219468 1187 EQEVNILkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQT--------------KRVKANLEKAKQTLENER 1247
Cdd:PRK10246 721 QVHEQCL--SLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASvfddqqaflaalldEETLTQLEQLKQNLENQR 793
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
875-1245 |
6.43e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 875 LVKVREKQLAAENRLTEMETLQSQLMAEklqLQEQLQAETELCAEAEELRARL-TAKKQ-------------ELEEICHD 940
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQILEE---LDELLESEEKNREEVEELKDKYrELRKTllanrfsygpaidELEKQLAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 941 LEARVEEEEERC---QHLQAEK--KKMQQNIQELEEQLEEEESARQKL------QLEKVttEAKLKKLEEEQIILEDQNc 1009
Cdd:pfam06160 158 IEEEFSQFEELTesgDYLEAREvlEKLEEETDALEELMEDIPPLYEELktelpdQLEEL--KEGYREMEEEGYALEHLN- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1010 kLAKEKKLLEDRIAEFTTNL--TEEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAE 1087
Cdd:pfam06160 235 -VDKEIQQLEEQLEENLALLenLELDEAEEALEEIEER----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1088 LQAQIAELKM--QLAKKEEELQAAL-ARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEA 1164
Cdd:pfam06160 310 LKEELERVQQsyTLNENELERVRGLeKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1165 L-KTELEdtldstaAQQELrSKREQEVNILKKTLEeeaKTH----EAQIQEMRQKHSQAVEELAEQLEQT----KRVKAN 1235
Cdd:pfam06160 390 LrKDELE-------AREKL-DEFKLELREIKRLVE---KSNlpglPESYLDYFFDVSDEIEDLADELNEVplnmDEVNRL 458
|
410
....*....|
gi 2550219468 1236 LEKAKQTLEN 1245
Cdd:pfam06160 459 LDEAQDDVDT 468
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1534-1669 |
6.49e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1534 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1613
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2550219468 1614 EMEAELEDERKQRSMAVAARkklemDLKDLEAHIDSANKNRDEAIKQLRKLQAQMK 1669
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1459-1668 |
7.06e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1459 NLEKKQKKFDQLLAEEKTISAkyAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKddvg 1538
Cdd:COG3206 190 ELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP---- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1539 kSVHELEKSKRALEQQVEEMKTQLEELEDELQAtedaklrlevnLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAE 1618
Cdd:COG3206 264 -VIQQLRAQLAELEAELAELSARYTPNHPDVIA-----------LRAQIAALRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1619 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQM 1668
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1599-1735 |
7.12e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1599 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRD------------EAIKQLRKLQA 1666
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaaltkgneelarEALAEKKSLEK 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550219468 1667 QMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSS 1735
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA-KAQEAVQTSLGSLSTSSATDS 165
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1543-1728 |
7.16e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1543 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKlrlevnlqamkaqferdlqgRDEQSEEKKKQLVRQVREMEAELEDE 1622
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1623 RKQRSMAVAARKKLEmdlkdleahiDSANKNRDEAIKqlrKLQAQMKdcmRELDDTRASREEILAQAKENEKKLKSMEAE 1702
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 2550219468 1703 MIQLQEELAAAERAKRQAQQERDELA 1728
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
978-1240 |
7.22e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 978 SARQKL--QLEKVTTEAKLKKLEEEQI-ILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKlknKHEAMITDLE 1054
Cdd:PHA02562 150 PARRKLveDLLDISVLSEMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA---RKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1055 ERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA--KKEEE--------------LQAALARVEEEAA 1118
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKmyekggvcptctqqISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1119 QKNMALKKIRELESQISELQEdLESErasRNKAEKQKRDLGEELEALKTELedtldstaaqqelrskreqevnilkKTLE 1198
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEE-IMDE---FNEQSKKLLELKNKISTNKQSL-------------------------ITLV 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2550219468 1199 EEAKTHEAQIQEM---RQKHSQAVEELAEQLEQTKRVKANLEKAK 1240
Cdd:PHA02562 358 DKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1104-1211 |
7.24e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.21 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1104 EELQAALARVEEEAAqknmaLKKIRELESQISELQEDLESERASRNKAEKQ----KRDlGEELEALKteledtldstaaq 1179
Cdd:PRK05431 12 EAVKEALAKRGFPLD-----VDELLELDEERRELQTELEELQAERNALSKEigqaKRK-GEDAEALI------------- 72
|
90 100 110
....*....|....*....|....*....|....*
gi 2550219468 1180 qelrskreQEVNILK---KTLEEEAKTHEAQIQEM 1211
Cdd:PRK05431 73 --------AEVKELKeeiKALEAELDELEAELEEL 99
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1023-1163 |
7.39e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.99 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1023 AEFTTNLTE--EEEKSKSlAKLKNKHEAMITDLEERLRRE--------EKQRQELEKTRRKLEGDSTDLSDQIAELQAQI 1092
Cdd:pfam03148 203 EKFTQDNIEraEKERAAS-AQLRELIDSILEQTANDLRAQadavnfalRKRIEETEDAKNKLEWQLKKTLQEIAELEKNI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1093 AELKMQLAKKEEELQAALARVEEEAAQKNMAL----------KKIRELESQISELQEDLESERASRNKAEKQKRDLGEEL 1162
Cdd:pfam03148 282 EALEKAIRDKEAPLKLAQTRLENRTYRPNVELcrdeaqyglvDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDI 361
|
.
gi 2550219468 1163 E 1163
Cdd:pfam03148 362 A 362
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1237-1385 |
8.09e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1237 EKAKQTLenerGELANEVKVLLQGkgdSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNvtgLLSQSDSK 1316
Cdd:PRK00409 505 EEAKKLI----GEDKEKLNELIAS---LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKE 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2550219468 1317 SSKLTKdfSALESQLQDTQELLQEENRQKLSLstKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1385
Cdd:PRK00409 575 AQQAIK--EAKKEADEIIKELRQLQKGGYASV--KAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
989-1922 |
8.14e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 989 TTEAKLKKLEEEQIILEDQncklAKEKKLLEDriAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQ-RQEL 1067
Cdd:NF041483 322 TKEAEALKAEAEQALADAR----AEAEKLVAE--AAEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAaAEEA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1068 EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK----KEEELQAALARVEEEAAQ----------------KNMALKKI 1127
Cdd:NF041483 396 ERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKeyraKTVELQEEARRLRGEAEQlraeavaegerirgeaRREAVQQI 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1128 RELESQISEL-----QEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE-LRSKREQEVNILKKTLEEEA 1201
Cdd:NF041483 476 EEAARTAEELltkakADADELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAErLRAEAEEQAEEVRAAAERAA 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1202 K-THEAQIQEMRQKHSQAVEELAE-QLEQTKRVKA---NLEKAKQTLENERGELANEVKVLlqgKGDSEHKRKKVEAQLQ 1276
Cdd:NF041483 556 ReLREETERAIAARQAEAAEELTRlHTEAEERLTAaeeALADARAEAERIRREAAEETERL---RTEAAERIRTLQAQAE 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1277 ElqvkfnEGERVRTELADKVTKLQVELDNVT-GLLSQSDSKSSKLTKDF------------SALESQLQDTQELL---QE 1340
Cdd:NF041483 633 Q------EAERLRTEAAADASAARAEGENVAvRLRSEAAAEAERLKSEAqesadrvraeaaAAAERVGTEAAEALaaaQE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1341 E-NRQKL----SLSTKLKQVEDEKNSFREQLEEE-EEAKHNLEKQIATLHAQVADMKKKMEDSVGcleTAEEVKRKLQKD 1414
Cdd:NF041483 707 EaARRRReaeeTLGSARAEADQERERAREQSEELlASARKRVEEAQAEAQRLVEEADRRATELVS---AAEQTAQQVRDS 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1415 LEGLSQRHEEKV-----AAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKfdqlLAEEKTISAKYAEERDRAE 1489
Cdd:NF041483 784 VAGLQEQAEEEIaglrsAAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRR----EAQEETEAAKALAERTVSE 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1490 A--EAREKETKALSLA-RALEEAMEQKAELERLNKQFRTEM-EDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 1565
Cdd:NF041483 860 AiaEAERLRSDASEYAqRVRTEASDTLASAEQDAARTRADArEDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAER 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1566 EDELQATEDAKLRLEVNLQAMK------AQFER------DLQGRDEQSEEKKKQLVRQVREmEAELEDERkqrsMAVAAR 1633
Cdd:NF041483 940 LRDEARAEAERVRADAAAQAEQliaeatGEAERlraeaaETVGSAQQHAERIRTEAERVKA-EAAAEAER----LRTEAR 1014
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1634 KKLEMDLKDLEAhidSANKNRDEAIKQLRKLQAQMKDCMRELddTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1713
Cdd:NF041483 1015 EEADRTLDEARK---DANKRRSEAAEQADTLITEAAAEADQL--TAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAE 1089
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1714 ERAKRQAQQERDEL-ADEIANSSGKGALALEEKrrleariaqleeeleeeqgnTELINDRLKKanlQIDQINtdlnlERS 1792
Cdd:NF041483 1090 ATVEGNSLVEKARTdADELLVGARRDATAIRER--------------------AEELRDRITG---EIEELH-----ERA 1141
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1793 HAQKNENARQQLERQNKELKVKLQEMegtvkskykasiTALEAKIAQLEEQLDNE-TKERQAAckqVRRTEKKLKDVLLQ 1871
Cdd:NF041483 1142 RRESAEQMKSAGERCDALVKAAEEQL------------AEAEAKAKELVSDANSEaSKVRIAA---VKKAEGLLKEAEQK 1206
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 2550219468 1872 VDDERRNAEQYKDQADKASTRL-KQLKRQLEEAEEEAQRANASRRKLQRELE 1922
Cdd:NF041483 1207 KAELVREAEKIKAEAEAEAKRTvEEGKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1488-1754 |
8.76e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.09 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1488 AEAEAREKETKALSLARALEEA----MEQKaELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLE 1563
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEArqarLERE-KAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1564 EledelqatedaklrlevNLQAMKAQFERDLQGRDEQSEEKkkqlvrqvremEAELEDERKQRSMAVAAR---KKLEMDL 1640
Cdd:PRK05035 515 D-----------------NSAVIAAREARKAQARARQAEKQ-----------AAAAADPKKAAVAAAIARakaKKAAQQA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1641 KDLEAHIDSANK----NRDEAIKQLRKLQAQMKD-----CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1711
Cdd:PRK05035 567 ANAEAEEEVDPKkaavAAAIARAKAKKAAQQAASaepeeQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA 646
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2550219468 1712 AAE----RAK-RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQ 1754
Cdd:PRK05035 647 AVAaaiaRAKaRKAAQQQANAEPEEAEDPKKAAVA-AAIARAKAKKAA 693
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
877-1206 |
8.84e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 877 KVREKQLAAENRLTEMETLQSQLMAEKLQlqEQLQAETELCAEAEELRARLTAKKQELeeichdleARVEEEEERCQHLQ 956
Cdd:PLN03229 440 KLKEQILKAKESSSKPSELALNEMIEKLK--KEIDLEYTEAVIAMGLQERLENLREEF--------SKANSQDQLMHPVL 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 957 AEK-KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlkkleeeqiILEDQNCKLAKEKKLLEDRIAEfTTNLTEEEEK 1035
Cdd:PLN03229 510 MEKiEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAK---------ALSEKKSKAEKLKAEINKKFKE-VMDRPEIKEK 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1036 SKSL-AKLKNKHEAMITDLEERLRRE-EKQRQELEKTRRKLEgDSTDLsdQIAELQAQIAELKMQLAkkEEELQAALARV 1113
Cdd:PLN03229 580 MEALkAEVASSGASSGDELDDDLKEKvEKMKKEIELELAGVL-KSMGL--EVIGVTKKNKDTAEQTP--PPNLQEKIESL 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1114 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeLEALKTELEDTLDSTAAQQELRSKREQevniL 1193
Cdd:PLN03229 655 NEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEK------IEALEQQIKQKIAEALNSSELKEKFEE----L 724
|
330
....*....|...
gi 2550219468 1194 KKTLEEEAKTHEA 1206
Cdd:PLN03229 725 EAELAAARETAAE 737
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1748-1947 |
9.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1748 LEARIAQLEEELEEEQGNTELIN-DRLKKANLQIDQI---NTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVK 1823
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeekEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1824 -SKYKASITALEAKIAQLEEQLDnETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKAstRLKQLKRQLee 1902
Cdd:COG4717 127 lLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEEL-- 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2550219468 1903 aeeeaQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGDL 1947
Cdd:COG4717 202 -----EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
905-1438 |
9.32e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.04 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 905 QLQEQLQAETELCAEAEELRARLTAKKQELEE-----ICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESA 979
Cdd:pfam15964 71 QLKALLQQQTKKENELSPRRRKLSPSRTSEDEssslpTVHDLVPIINDQSQYIHHLEAEVKFCKEELSEMKQRVQVVVLE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 980 RQKLQ--LEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMitdleERL 1057
Cdd:pfam15964 151 NEKLQqeLKSQTQEETLREQTLLDSSGNMQNSWCTPEDSRVHQTSKRPASHNLAERLKSATTGEDEKWRLEL-----EKL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1058 RREEKQRQELektrrkLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA---------LARVEEEA----AQKNMAL 1124
Cdd:pfam15964 226 KLLYEAKTEV------LESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAStssrvgglcLKCAQHEAvlaqTHTNVHM 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1125 KKIRELESQISELQEDLESERASRNKAEKQKRDLGEEL-EALKTELEDTLDSTAAQ---QELRSKREQEVNILKKTLEEE 1200
Cdd:pfam15964 300 QTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVkQAVQMTEEANFEKTKALiqcEQLKSELERQKERLEKELASQ 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1201 AKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEA----QLQ 1276
Cdd:pfam15964 380 QEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGemryQLN 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1277 ELQVKFNEGERVRTELADK-----------VTKLQVELDNVTGLLSQSDSKSS-------KLTKDFSALESQLQDTQell 1338
Cdd:pfam15964 460 QTKMKKDEAEKEHREYRTKtgrqleikdqeIEKLGLELSESKQRLEQAQQDAArareeclKLTELLGESEHQLHLTR--- 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1339 QEENRQKLSLSTKLK-------QVEDEKNSFREQLEEEEEAKHNleKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKL 1411
Cdd:pfam15964 537 LEKESIQQSFSNEAKaqalqaqQREQELTQKMQQMEAQHDKTVN--EQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKS 614
|
570 580
....*....|....*....|....*..
gi 2550219468 1412 QKDLEGLSQrheEKVAAYDKLEKTKTR 1438
Cdd:pfam15964 615 RSEVEQLSQ---EKEYLQDRLEKLQKR 638
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1011-1333 |
9.66e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.81 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1011 LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE------EKQRQELEKTRRKLEGDSTDLSDQ 1084
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDEcwkkikRKKNSALSEALNGFKYEANFKSRL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1085 IAELQAQI---------AELKMQLAKKEEELQAALARVEEEAAQKnMALKKIRELESQISELQEDLESERASRNKAEKQK 1155
Cdd:pfam13166 167 LREIEKDNfnagvllsdEDRKAALATVFSDNKPEIAPLTFNVIDF-DALEKAEILIQKVIGKSSAIEELIKNPDLADWVE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1156 RDL-------------GEEL-EALKTELEDTLDSTAAQQ---------ELRSKREQEVNIL----------------KKT 1196
Cdd:pfam13166 246 QGLelhkahldtcpfcGQPLpAERKAALEAHFDDEFTEFqnrlqklieKVESAISSLLAQLpavsdlasllsafeldVED 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1197 LEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQtKRVKANLEKAKQTLE--NERGELANEVKVLLqgKGDSEHKRKKVEAQ 1274
Cdd:pfam13166 326 IESEAEVLNSQLDGLRRALEAKRKDPFKSIEL-DSVDAKIESINDLVAsiNELIAKHNEITDNF--EEEKNKAKKKLRLH 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2550219468 1275 L-QELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdSKSSKLTKDFSALESQLQD 1333
Cdd:pfam13166 403 LvEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLE-------AEIKKLREEIKELEAQLRD 455
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1077-1154 |
9.67e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 40.31 E-value: 9.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2550219468 1077 DSTDLSDQIAELQAQIAELKMQLakkeEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQ 1154
Cdd:COG0845 55 DPPDLQAALAQAQAQLAAAQAQL----ELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARAN 128
|
|
| |
