|
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 ... |
841-1921 |
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: 1405.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 841 SRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDL 920
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 921 EARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDR 1000
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1001 IAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK 1080
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1081 KEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1161 LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGK 1240
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1241 GDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1320
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1321 NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQR 1400
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1401 HEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALS 1480
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1481 LARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 1560
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1561 NLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQL 1640
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1641 RKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1720
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1721 LEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGT 1800
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1801 VKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLE 1880
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 12667788 1881 EAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
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: 1357.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKD---QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 332 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 12667788 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
95-764 |
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: 1345.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKD----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKEsgkkKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYR-FLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 330 GIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 410 ADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 490 EEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPK-FQKPKQLKDKADF 568
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsETALPGAFKTRKGMFRTVGQ 648
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 12667788 729 IPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
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: 1341.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 335 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14919 241 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14919 321 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 495 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYA 574
Cdd:cd14919 401 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 575 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQL 654
Cdd:cd14919 481 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 655 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFM 734
Cdd:cd14919 561 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFM 640
|
650 660 670
....*....|....*....|....*....|
gi 12667788 735 DGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14919 641 DGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-764 |
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: 1305.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtALPGAFKTRKGMFRTVG 647
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 12667788 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-764 |
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: 1248.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtaLPGAFKTRKGMFRTVG 647
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 12667788 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
95-764 |
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: 1205.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 332 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 12667788 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
95-764 |
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: 1149.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASShKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 241
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 242 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 321
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 322 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 482 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKpKQ 561
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 562 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAgMSETALpGAfKTRKG 641
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF-GA-RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 642 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 12667788 722 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
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: 1128.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGI 331
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 332 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 12667788 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
83-764 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1121.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 83 VEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM 162
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 163 QDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 242
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 243 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQE 321
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEEFKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 322 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:pfam00063 240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:pfam00063 320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 482 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQ 561
Cdd:pfam00063 400 HHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 562 lKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVagmsETALPGAFKTRKG 641
Cdd:pfam00063 477 -QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRTKKK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 642 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:pfam00063 552 RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 12667788 722 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:pfam00063 632 RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
76-776 |
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: 1024.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 76 NPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITD 155
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 156 TAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqGELERQLLQANPILEAFGNAKTVKNDNSSRF 235
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---GSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 236 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQ 314
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGcLTVDGID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 315 DKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNT-AAQKVSHLLGINVTDFTRGILTPR 393
Cdd:smart00242 238 DAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALTKRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:smart00242 318 IKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCINYAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTH 553
Cdd:smart00242 397 EKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECRFPKGTDQTFLEKLNQHHKKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 554 PKFQKPKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmsetalp 633
Cdd:smart00242 474 PHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 634 GAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 713
Cdd:smart00242 535 VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12667788 714 FQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERD 776
Cdd:smart00242 615 FDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1151 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 911.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 32 VWVPSDKSGFEPASLKEEVGEEAIVEL---VENGKKVKVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKERYY 106
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 107 SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKK 186
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 187 VIQYLAYVASSHKSkkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIR 266
Cdd:COG5022 172 IMQYLASVTSSSTV--EISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 267 QAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT-IPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISG 345
Cdd:COG5022 250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 346 VLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERM 425
Cdd:COG5022 330 ILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 426 FRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFg 505
Cdd:COG5022 409 FDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 506 LDLQPCIDLIEKpAGPPGILALLDEECWFPKATDKSFVEKVMQ--EQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADE 583
Cdd:COG5022 487 FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYDVEG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 584 WLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIigldqvagmsetalpgafkTRKGMFRTVGQLYKEQLAKLMATLRN 663
Cdd:COG5022 564 FLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENI-------------------ESKGRFPTLGSRFKESLNSLMSTLNS 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 664 TNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS----IPKGFMDGKQA 739
Cdd:COG5022 625 TQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 740 CVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKRQQQLTAMKVLQRNCAAY 819
Cdd:COG5022 705 VKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLR 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 820 LKLRNWQWWRLFTKVKPLLQVSRQEEEMMAKEEElvkVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcAEA 899
Cdd:COG5022 785 RLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLAC---IIKLQKTIKREKKLRETEEVEFSLKAEVLIQKF-------GRS 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 900 EELRAR-LTAKKQELEEIChdlEARVEEEEERCQHLQAEKKKMQQniqeleeqleeeeSARQKLQLEKVTTEAKLKKLEE 978
Cdd:COG5022 855 LKAKKRfSLLKKETIYLQS---AQRVELAERQLQELKIDVKSISS-------------LKLVNLELESEIIELKKSLSSD 918
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 979 EQIILEDQNCKLAKEKKLL------EDRIAEFTTNLTEEE--EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTR 1050
Cdd:COG5022 919 LIENLEFKTELIARLKKLLnnidleEGPSIEYVKLPELNKlhEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFK 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1051 RKLegdsTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVEEEAA---QKNMALKKIRELESQISELQEDLeserasr 1127
Cdd:COG5022 999 KEL----AELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTelsILKPLQKLKGLLLLENNQLQARY------- 1066
|
1130 1140
....*....|....*....|....
gi 12667788 1128 nKAEKQKRDLGEELEALKTELEDT 1151
Cdd:COG5022 1067 -KALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
95-764 |
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: 881.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLAYVASSHKSKKD--QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL-----SNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNT--DQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQ-GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 484 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLK 563
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 564 DKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriigldqvagmsetalpgafktrkgmf 643
Cdd:cd00124 478 KLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ-------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 644 rtvgqlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd00124 519 ------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 12667788 724 LTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd00124 593 LAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
95-764 |
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: 786.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVAS---------SHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 245
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 246 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETM 323
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVsmNPYD-YHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 324 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 403
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 404 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 484 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKP--- 559
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 560 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKTR 639
Cdd:cd14927 476 KKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY--------VGSDSTEDPKSGVKEK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 640 K---GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14927 548 RkkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 12667788 717 FRQRYEILTPNSIPK-GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14927 628 FKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
96-764 |
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: 763.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVASS-----HKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLIttNPYD-YPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 329 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKA 566
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 567 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MF 643
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FATADADSGKKKVAKKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14913 547 QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 12667788 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14913 627 LNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
95-764 |
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: 756.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKD-QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDgKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNK-YRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKeYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 333 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 493 QREGIEWNFIDFGLDLQPCIDLIEKPAGppgILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK---ADF 568
Cdd:cd14934 400 KREGIEWVFIDFGLDLQACIDLLEKPMG---IFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvselwkdvdriIGLDQVAGMSETALPGAFKTRKGM-FRTVG 647
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQKRGSsFMTVS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14934 543 NFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPN 622
|
650 660 670
....*....|....*....|....*....|....*..
gi 12667788 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14934 623 VIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
95-764 |
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: 755.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAkskGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL-EPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMG 330
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 331 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 411 DFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 491 EYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLK---DKA 566
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiGLDQVAGMSETAlpGAFKTRKGMFRTV 646
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAK--GGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 12667788 727 NSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
95-764 |
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: 729.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDILGFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 333 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14929 239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14929 319 AVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 493 QREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK--ADFC 569
Cdd:cd14929 398 RKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGmseTALPGAFKTRK--GMFRTVG 647
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD---SAIQFGEKKRKkgASFQTVA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14929 545 SLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPR 624
|
650 660 670
....*....|....*....|....*....|....*...
gi 12667788 728 SIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14929 625 TFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
96-764 |
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: 716.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSG-LIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKKdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET---QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFA 413
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 414 IEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd01380 319 RDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 493 QREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPK--FQKPKQLKDKadFCI 570
Cdd:cd01380 399 VKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA--FIV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwkdvdriigldqvagmsetalpgafKTRKgmfRTVGQLY 650
Cdd:cd01380 473 KHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------------KNRK---KTVGSQF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 651 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIP 730
Cdd:cd01380 517 RDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEW 596
|
650 660 670
....*....|....*....|....*....|....
gi 12667788 731 KGfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01380 597 LR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
96-764 |
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: 714.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVAS-SHKSKKDQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQtpgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 329 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK- 565
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 566 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MF 643
Cdd:cd14917 476 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAPIEKGKGKAKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14917 547 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 12667788 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14917 627 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
96-764 |
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: 696.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVAS-SHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtnNPYD-YAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK 565
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 566 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMF 643
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSSF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 12667788 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-764 |
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: 693.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVASSHKSKKD------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLkTDLLLEPYNKYR--FLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDK 565
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 566 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigLDQVAGMSETALPGAfKTRKGMF 643
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY-----AGAEAGDSGGSKKGG-KKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 12667788 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
97-764 |
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: 692.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 176
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 177 GAGKTENTKKVIQYLAYVASSHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 330 GIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 408
Cdd:cd14918 242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 409 QADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 489 QEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 568 --FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAfKTRKGMFRT 645
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-------ASAEADSGAKKGA-KKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:cd14918 549 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 12667788 726 PNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14918 629 ASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-764 |
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: 684.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKD 564
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAlpgafKTRKGM 642
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGG-----KKKGSS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14912 551 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 12667788 723 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14912 631 VLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-764 |
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: 681.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 565 K--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqvAGMSETALPGAFK--TRK 640
Cdd:cd14910 476 KveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG----------AAAAEAEEGGGKKggKKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 641 G-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 719
Cdd:cd14910 546 GsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 12667788 720 RYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14910 626 RYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
96-764 |
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: 676.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVASSHKskkdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--HLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 333 EEEQMGLLRVISGVLQLGNIVFKK-ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14883 236 EEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEAR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14883 316 DNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 492 YQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAGMSETALPGAfKTRKGMfRTVGQLYK 651
Cdd:cd14883 472 HYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSR-GTSKGK-PTVGDTFK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14883 549 HQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSA 628
|
650 660 670
....*....|....*....|....*....|...
gi 12667788 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14883 629 DHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-764 |
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: 673.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLIttNPYD-FAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMSETALPGAFKTRKGM 642
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 12667788 723 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
96-764 |
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: 653.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVasshkSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGA 252
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV-----SGGSESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 332 PEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG---RDYVQKAQTKE 408
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFVEKVMQEQGTHPKFQKPKQLKD--K 565
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEEK--PPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 566 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalpgafKTRKGMFRT 645
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 12667788 726 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
96-764 |
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: 650.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVASshkskkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 335 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd01383 234 DQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd01383 314 DALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 495 EGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPkqlKDKAdFCIIHYA 574
Cdd:cd01383 394 DGIDWTKVDF-EDNQECLDLIEKK--PLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RGGA-FTIRHYA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 575 GKVDYKADEWLMKNMDPLNDNIATLL----HQSSDKFVSELWKDVDRIigldqvagmsetALPGAFKTRKGMFRTVGQLY 650
Cdd:cd01383 467 GEVTYDTSGFLEKNRDLLHSDLIQLLsscsCQLPQLFASKMLDASRKA------------LPLTKASGSDSQKQSVATKF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 651 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIp 730
Cdd:cd01383 535 KGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV- 613
|
650 660 670
....*....|....*....|....*....|....
gi 12667788 731 KGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01383 614 SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
95-764 |
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: 635.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLAYVASshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDVVGIS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 333 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPD---NTAAQKVSHLLGINVTDFTRGiLTPRIKVGRD-YVQKAQTKE 408
Cdd:cd01384 239 EEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgIITKPLDPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 409 QADFAIEALAKATYERMFRWLVLRINKAL--DKTKRqgaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd01384 318 AATLSRDALAKTIYSRLFDWLVDKINRSIgqDPNSK---RLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEKpaGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKqlKDKA 566
Cdd:cd01384 395 MEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSRT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalPGAFKTRKgmFRTV 646
Cdd:cd01384 470 DFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR---------------EGTSSSSK--FSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 12667788 727 NsIPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd01384 613 E-VLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
95-764 |
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: 619.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHSW------IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLMFTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 334 EEQMGLLRVISGVLQLGNIVFKK--ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd01381 235 EEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGAS--FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01381 315 DVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 490 EEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAdF 568
Cdd:cd01381 395 EEYDKEGINWQHIEF-VDNQDVLDLIaLKPM---NIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTS-F 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdVDRIIGLDQVAGMSetalpgafkTRKgmfR--TV 646
Cdd:cd01381 470 GINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF-------LKQLFNEDISMGSE---------TRK---KspTL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01381 531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 12667788 727 NSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-764 |
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: 596.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLAYVASSHkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG-----AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01382 156 VSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL---------------KDPLLDDVGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 334 EEQMGLLRVISGVLQLGNIVFKKERNT-------DQASMPDNTAAqkvSHLLGINVTDF-----TRGILTPRIKVGRDYV 401
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYA---AELLGLDQDELrvsltTRVMQTTRGGAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 482 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKP-- 559
Cdd:cd01382 376 ERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPrk 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 560 ------KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagMSETALP 633
Cdd:cd01382 453 sklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTN---------NNKDSKQ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 634 gafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 713
Cdd:cd01382 524 ---KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTS 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 12667788 714 FQEFRQRYEILTPNSIPKgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01382 601 FHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
95-764 |
0e+00 |
|
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: 567.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASShkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAgeHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQAS---MPDNTAAQKVSHLLGINVTDFTRGILTPRIKV-GRDYVQKAQTKEQ 409
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 410 ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 490 EEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFC 569
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKK--QPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTEFI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalpGAFKTRKGmfrTVGQL 649
Cdd:cd14872 470 VKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-----------------GDQKTSKV---TLGGQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtPNSI 729
Cdd:cd14872 530 FRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTI 608
|
650 660 670
....*....|....*....|....*....|....*.
gi 12667788 730 PKGFM-DGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14872 609 AKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
95-764 |
0e+00 |
|
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: 562.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVAsshksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-----QRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAIT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01387 155 SQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQ---ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd01387 235 EEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd01387 315 LDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 491 EYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlkDKADFCI 570
Cdd:cd01387 394 EYIREQIDWTEIAF-ADNQPVINLISKK--PVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPEFTI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldQVAGMSETALP----GAFKTRKGMFRTV 646
Cdd:cd01387 469 KHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPrlgkGRFVTMKPRTPTV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01387 540 AARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVA 619
|
650 660 670
....*....|....*....|....*....|....*....
gi 12667788 727 NSIPKGfMDGKQACVLMIKALELD-SNLYRIGQSKVFFR 764
Cdd:cd01387 620 LKLPRP-APGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
95-764 |
2.35e-178 |
|
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: 556.70 E-value: 2.35e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQ----DREDQS 169
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 170 ILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------------GELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 237 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 317 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmpDNTAAQKVSH---LLGINVTDFTRGILTPR 393
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-KPAGPPGILALLDeECWFPKAT--DKSFVEKVMQEQ 550
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 551 GT-------------HPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwkdvDR 617
Cdd:cd14890 476 GRksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS------------RR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 618 IIgldqvAGMSetalpgafktrkgmfrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGV 697
Cdd:cd14890 543 SI-----REVS-----------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 698 LEGIRICRQGFPNRVVFQEFRQRYEILTPNSipkgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
95-762 |
2.51e-174 |
|
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: 545.54 E-value: 2.51e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY------KGKKRHEMPPHIYAITDTAYRSMMQDRE-- 166
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 167 --DQSILCTGESGAGKTENTKKVIQYLAYVASshKSKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKFI 239
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS--ATTHGQNATERenvrdRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 240 RINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKD 317
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 318 MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-KKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKV 396
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 397 GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAS-FIGILDIAGFEIFDLNSFEQLCINYTNEK 475
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 476 LQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQG 551
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 552 THPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmseta 631
Cdd:cd14901 472 KHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS--------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 632 lpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 711
Cdd:cd14901 531 -------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 712 VVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNL-----YRIGQSKVF 762
Cdd:cd14901 598 FPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-764 |
4.15e-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: 543.51 E-value: 4.15e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVasshkSKKDQGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL-----SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHvTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01385 156 VEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCY-TLEGEDEKYEFERLKQAMEMVGF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 332 PEEEQMGLLRVISGVLQLGNIVFKKER-NTDQASMPDNTAAQK-VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01385 235 LPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKLPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 410 ADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd01385 315 AIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 486 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPkQLKDK 565
Cdd:cd01385 394 KLEQEEYKKEGISWHNIEY-TDNTGCLQLISKK--PTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVMEP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 566 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriIGLDQVAGMSETALPGAFKT-----RK 640
Cdd:cd01385 470 A-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAVFRWAVLRAFFRAmaafrEA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 641 GMFR-----------------------------TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQ 691
Cdd:cd01385 542 GRRRaqrtaghsltlhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQ 621
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12667788 692 LRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnsIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01385 622 LRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
95-764 |
4.35e-173 |
|
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: 542.44 E-value: 4.35e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLAYVAsshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLsgAGEHLKTDLLLEPYNKYRFL-SNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 329 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASM--PDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14903 230 IGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14903 310 KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVMqeqGTHPKFQK----PKql 562
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPR-- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdrIIGLDQVAGMSETALPGAFKTRKGM 642
Cdd:cd14903 460 TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 12667788 723 ILTPNSiPKGFMDGKQACVLMIKALELDS-NLYRIGQSKVFFR 764
Cdd:cd14903 617 LFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
96-764 |
1.13e-170 |
|
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: 534.93 E-value: 1.13e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVasshkSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSNGHVTIPG----QQDKDMFQETMEAMRIMG 330
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDivnnSGNREKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 331 IPEEEQMGLLRVISGVLQLGNIVFK---KERNTDQASM-PDNTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQ 405
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADEL-QEALTSHSVVTRgETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 406 TKEQADFAIEALAKATYERMFRWLVLRINKAL--DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd01379 316 TVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 484 MFILEQEEYQREGIEWNFIDFGlDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPkFQKPKql 562
Cdd:cd01379 396 IFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpgafktrkgm 642
Cdd:cd01379 469 SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-------------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 643 frTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd01379 517 --TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 12667788 723 ILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd01379 595 FLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
95-764 |
2.17e-170 |
|
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: 534.27 E-value: 2.17e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKK-RHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLayvasSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14897 81 GESGAGKTESTKYMIKHL-----MKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD-------KDMFQETMEAM 326
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLTNIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14897 236 KLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 407 KEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14897 316 LRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKql 562
Cdd:cd14897 396 YVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFKK--PLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASP-- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagmsetalpgafktrkgm 642
Cdd:cd14897 471 GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 643 frtvgQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14897 522 -----SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYK 596
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 12667788 723 ILTPNSiPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14897 597 EICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
95-726 |
1.00e-167 |
|
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: 528.11 E-value: 1.00e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD--------- 244
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL--VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN------------------- 305
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGAdakpisidmssfephlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 306 -----GHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQ---KVSHL 377
Cdd:cd14888 238 yltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 378 LGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFE 457
Cdd:cd14888 318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKA 537
Cdd:cd14888 398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFVPGG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 538 TDKSFVEKVMQEQGTHPKFQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD-VD 616
Cdd:cd14888 475 KDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAyLR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 617 RIIGLdqvagmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14888 553 RGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670
....*....|....*....|....*....|
gi 12667788 697 VLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
95-764 |
1.86e-167 |
|
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: 526.67 E-value: 1.86e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLAYVASSH---KSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 330 GIPEEEQMGLLRVISGVLQLGNIVFKkerNTDQASMPDNTAAQKVSHLLGINVTDFTRgILTPRIKVGR-DYVQKAQTKE 408
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTD-ALTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 409 QADFAIEALAKATYERMFRWLVLRINKALdkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDkaDF 568
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWkdvdriiglDQVAGMSETALPGAFKTRKGmfRTVGQ 648
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRR--PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 12667788 729 IPKGFMDGKqaCVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-764 |
7.68e-166 |
|
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: 522.40 E-value: 7.68e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEM---PPHIYAITDTAYRSMMQDR----ED 167
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 168 QSILCTGESGAGKTENTKKVIQYLA----YVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMF 319
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 320 QETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFkkERNTDQ----ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIK 395
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 396 VGRDYV-QKAQTKEQADFAIEALAKATYERMFRWLVLRINKAldkTKRQG------------ASFIGILDIAGFEIFDLN 462
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINAC---HKQQTsgvtggaasptfSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 463 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKS 541
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 542 FVEKVMQEQ-GTHPKFQKPKQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriig 620
Cdd:cd14892 473 LLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK--------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 621 ldqvagmsetalpgafktrkgmFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 700
Cdd:cd14892 536 ----------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEV 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 701 IRICRQGFPNRVVFQEFRQRYEILTPNS-IPKGFMDGKQACVLMIKALE-----LDSNLYRIGQSKVFFR 764
Cdd:cd14892 587 VRIRREGFPIRRQFEEFYEKFWPLARNKaGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
97-764 |
1.19e-153 |
|
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: 489.42 E-value: 1.19e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM----QDREDQSILC 172
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 173 TGESGAGKTENTKKVIQYLAYVAsshkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGA 252
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHvtipGQQD-----KDMFQETMEAMR 327
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA----GCKRevqywKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKkerntdqasmPDNTAAQKVSH-------------------LLG--INVTDFT 386
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFE----------MDDDEALKVENdsngwlkaaagqfgvseedLLKtlTCTVTFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 387 RGiltprikvgrDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQG--ASFIGILDIAGFEIFDLNSF 464
Cdd:cd14889 302 RG----------EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVE 544
Cdd:cd14889 372 EQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVD 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 545 KVMQEQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK-DVDRIIGLDQ 623
Cdd:cd14889 449 KLNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMP 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 624 VAGMSETALPGAFKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 703
Cdd:cd14889 527 RAKLPQAGSDNFNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRI 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12667788 704 CRQGFPNRVVFQEFRQRYEIL--TPNsIPKgfmdGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14889 604 RREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
95-727 |
1.90e-149 |
|
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: 477.99 E-value: 1.90e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH--------EMPPHIYAITDTAYRSMMQDR 165
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 166 EDQSILCTGESGAGKTENTKKVIQYL--------------AYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsqqeqnseevlTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 232 SSRFGKFIRINFD-VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLS---NG 306
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYlkkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 307 HVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQA--SMPDNTAAQKVSHLLGINVTD 384
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 385 FTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------DKTKRQGASFIGILDIAGFE 457
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP 535
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 536 KATDKSFVEKVMQEQGTHPKFQKPKQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDV 615
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 616 DRiigldqvagmSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCN 695
Cdd:cd14907 557 DG----------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 12667788 696 GVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
96-730 |
4.85e-146 |
|
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: 467.09 E-value: 4.85e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY-----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 164 ----DREDQSILCTGESGAGKTENTKKVIQYLAYV-----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 235 FGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlktdlllepynkyrflsnghvtipGQQ 314
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------------AAR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 315 DKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD-QASMPDNTAAQKV------SHLLGINVTDFTR 387
Cdd:cd14900 217 KRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 388 GILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGAS-FIGILDIAGFEIFDLNS 463
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 464 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFV 543
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 544 EKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndniatLLHQSSdkfvselwkdVDriigldq 623
Cdd:cd14900 454 SKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 624 vagmsetalpgafktrkgMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 703
Cdd:cd14900 509 ------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRV 569
|
650 660
....*....|....*....|....*..
gi 12667788 704 CRQGFPNRVVFQEFRQRYEILTPNSIP 730
Cdd:cd14900 570 ARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
95-764 |
3.42e-144 |
|
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: 462.59 E-value: 3.42e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERyySGLI----YTYSGLFCVVINPYKNLPiysEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE---D 167
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 168 QSILCTGESGAGKTENTKKVIQYL------------AYVASSHKSKKDQG-ELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttravggkkasgQDIEQSSKKRKLSVtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 235 FGKFIRINFDVNGY-IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPG 312
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 313 QQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKK----ERNTDQASMPDNTAAQKVSHLLGINVTDFTRG 388
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 389 ILTPRIkVGRDYVQKAQ-TKEQADFAIEALAKATYERMFRWLVLRINKALDKtKRQGASFIGILDIAGFEIFDL-NSFEQ 466
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 467 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKV 546
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 547 MQEQGTHPKFQKPKQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHqSSDKFVselwkdvdriigldqva 625
Cdd:cd14891 471 HKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKFS----------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 626 gmsetalpgafktrkgmfrtvgqlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICR 705
Cdd:cd14891 532 --------------------------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLK 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 706 QGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIK-ALELDSNLYRIGQSKVFFR 764
Cdd:cd14891 586 VGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
95-764 |
4.12e-142 |
|
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: 457.10 E-value: 4.12e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14904 156 CETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 332 PEEEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQTKEQA 410
Cdd:cd14904 236 DNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRI-EEALCNRSVVTRnESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 491 EYQREGIEWNFIDFGlDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKPKQlkDKAD 567
Cdd:cd14904 394 EYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV--KRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvaGMSETALPGAFKTRKGMfRTVG 647
Cdd:cd14904 468 FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKAP-KSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14904 538 SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPP 617
|
650 660 670
....*....|....*....|....*....|....*...
gi 12667788 728 SIPKGfmDGKQACVLMIKALELDSNL-YRIGQSKVFFR 764
Cdd:cd14904 618 SMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
95-764 |
1.77e-140 |
|
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: 452.31 E-value: 1.77e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLayvaSSHKSKKDQGELeRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL----SSLYQDQTEDRL-RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQ--ASMPDNTAAQKVSHLLGINvTDFTRGILTPRIKV-GRDYVQKAQTKEQA 410
Cdd:cd14896 235 EELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPVEGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14896 314 IDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 490 EEYQREGIEWNFIDfGLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlkDKADFC 569
Cdd:cd14896 394 EECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLPVFT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGmsetalpgafktrkgmfrTVGQL 649
Cdd:cd14896 469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------------TLASR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI 729
Cdd:cd14896 531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610
|
650 660 670
....*....|....*....|....*....|....*
gi 12667788 730 PkGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14896 611 E-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
95-747 |
1.32e-138 |
|
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: 449.73 E-value: 1.32e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYK--------GKKRHEMPPHIYAITDTAYRSMMQ-D 164
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 165 REDQSILCTGESGAGKTENTKKVIQYLAYV----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT---IPGQQDKD 317
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSfarKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 318 --MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKE-RNTDQASMPDNTAAQ--KVSHLLGINVTDFTRGILTP 392
Cdd:cd14902 241 aqLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 393 RIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD--------KTKRQGASFIGILDIAGFEIFDLNSF 464
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVE 544
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDK--SNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 545 KVMQEQGThpkfqkpkqlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSelwkdvdrIIGLDQV 624
Cdd:cd14902 478 KFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV--------AIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 625 AGMSETALPGAFKTRKGMFRT--VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 702
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 12667788 703 ICRQGFPNRVVFQEFRQRYEIL-----TPNSIPK-GFMDGKQA--CVLMIKAL 747
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFkcflsTRDRAAKmNNHDLAQAlvTVLMDRVL 670
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
95-764 |
2.17e-134 |
|
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: 436.65 E-value: 2.17e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK--GKKRHE-------MPPHIYAITDTAYRSMMQD- 164
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 165 REDQSILCTGESGAGKTENTKKVIQYLAYVASSHK-SKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKF 238
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgAPNEGEELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 239 IRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--------HLKTDLLLEPYNKYRFLSNGHVTI 310
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 311 PGQ-QDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQK----VSHLLGINVTDF 385
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 386 TRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSF 464
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFV 543
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 544 EKVM--------QEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdniatllhqssdkfvselwkd 614
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 615 vdriigldqvagmsetalpgafKTRKGMFRTvGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 694
Cdd:cd14908 536 ----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 695 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnSIPK----GFMDGKQACVLMIKALELDSNLYR--------------- 755
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKDLVKGVlspamvsmknipedt 671
|
730
....*....|.
gi 12667788 756 --IGQSKVFFR 764
Cdd:cd14908 672 mqLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
93-807 |
1.00e-132 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 436.77 E-value: 1.00e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 93 NEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHE-MPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 172 CTGESGAGKTENTKKVIQYLAYVASSHKSKKDQgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFASSKSGNMDLKIQ----NAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:PTZ00014 264 GSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 332 PEEEQMGLLRVISGVLQLGNIVF--KKERNTDQASM--PDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:PTZ00014 344 SESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:PTZ00014 424 KDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDK 565
Cdd:PTZ00014 503 RESKLYKDEGISTEELEY-TSNESVIDLLcGKGK---SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 566 aDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRKGMFrt 645
Cdd:PTZ00014 579 -NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQL-- 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:PTZ00014 640 IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 726 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR---AGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKR 802
Cdd:PTZ00014 720 LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN 799
|
....*
gi 12667788 803 QQQLT 807
Cdd:PTZ00014 800 IKSLV 804
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
96-764 |
1.01e-130 |
|
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: 427.06 E-value: 1.01e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPiyseeivEMYKGKKRHE-------MPPHIYAITDTAYRSMMQ----- 163
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 164 --DREDQSILCTGESGAGKTENTKKVIQYLAYVASSHK----SKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 237
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTatssSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 238 FIRINF-----DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNG--HV 308
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGqcYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 309 TIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD---------------QASMPDNTAAQK 373
Cdd:cd14895 235 RNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 374 ---VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTK--------- 441
Cdd:cd14895 315 ldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 442 -RQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEkpAG 520
Cdd:cd14895 395 nKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE--QR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 521 PPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIAT 598
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 599 LLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalpgafKTRKGMFRTV--GQLYKEQLAKLMATLRNTNPNFVRCIIPNH 676
Cdd:cd14895 550 VLGKTSDAHLRELFEFFKASESAELSLGQPKL------RRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 677 EKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELdsnlyri 756
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------- 696
|
....*...
gi 12667788 757 GQSKVFFR 764
Cdd:cd14895 697 GKTRVFLR 704
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
95-764 |
3.74e-126 |
|
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: 413.63 E-value: 3.74e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKyrflSNGHVTIPGQQDKDM------FQETMEAMR 327
Cdd:cd01386 156 IQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAAMK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGI------------LTPRIK 395
Cdd:cd01386 232 TLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 396 VGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEifdlN----------SFE 465
Cdd:cd01386 312 ESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGFQ----NpahsgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 466 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAG------------PPGILALLDEECW 533
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 534 FPKATDKSFVEKVMQEQG--THPKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNIATLLHQSSDKF 607
Cdd:cd01386 467 YPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 608 vselwkdvdriigldqvagmsetalpgAFKTRKGMFRTVgqlyKEQLAKLMATLRNTNPNFVRCIIPNHE------KKAG 681
Cdd:cd01386 547 ---------------------------AAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkderSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 682 KLDPHLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGF-----MDGKQACVLMIKALELD 750
Cdd:cd01386 596 PAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 12667788 751 SNLYRIGQSKVFFR 764
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
95-762 |
5.65e-124 |
|
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: 405.91 E-value: 5.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDLRIQ----TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLsNGHVT-IPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFL-NPKCLdVPGIDDVADFEEVLESLKSMGLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 333 EEEQMGLLRVISGVLQLGNIVFKKErntDQASMPDntAA----------QKVSHLLGINVTDFTRGILTPRIKVGRDYVQ 402
Cdd:cd14876 236 EEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 483 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFqKPKQL 562
Cdd:cd14876 390 IVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRKGM 642
Cdd:cd14876 466 DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------KIAKGS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 643 FrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14876 530 L--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFK 607
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 12667788 723 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVF 762
Cdd:cd14876 608 FLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
95-762 |
2.48e-123 |
|
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: 404.62 E-value: 2.48e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDRE--DQSI 170
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 171 LCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERieqRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIpgqqDKDMFQETMEAMR 327
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS---HLLGINVTDFTRGILTPRIKVGRDYV--Q 402
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRtsaLLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQL 562
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgafktrkgm 642
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPV---------- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 643 fRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14880 544 -LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 12667788 723 ILTPN--SIPKGFMDGKQAcvlmikalELDSNLYRIGQSKVF 762
Cdd:cd14880 623 LLRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
95-760 |
3.25e-121 |
|
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: 400.51 E-value: 3.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDREDQSILC 172
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 173 TGESGAGKTENTKKVIQYLAYVASSHKSKK-----DQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRsSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 247 GYIVGANIETYLLEKSR-AIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP-YNKYRFL--------------SNGHVTI 310
Cdd:cd14906 161 GKIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 311 PGQQDKD-MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQAS--MPDNTAA-QKVSHLLGINVTDFT 386
Cdd:cd14906 241 NNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 387 RGILTPRIKV-GRDYVQ-KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDK----------TKRQGASFIGILDIA 454
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 455 GFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWF 534
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 535 PKATDKSFVEKVMQEQGTHPKFQkpKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKd 614
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYY--QRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 615 vdriigldqvagMSETALPGAFKTRKGMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 694
Cdd:cd14906 555 ------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRN 621
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 695 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSK 760
Cdd:cd14906 622 VGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
95-764 |
2.37e-113 |
|
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: 376.46 E-value: 2.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYS-GLIYTYSGLFCVVINPYKNLPIYSEEIVEMY-KGKKRHEMPPHIYAITDTAYRSM-MQDREDQSIL 171
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 172 CTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQ----LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKidenLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLSNGHVTI----PGQ--QDKDMF 319
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVrrgvDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 320 QETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILtprIKVGRD 399
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 400 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD-KTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQ 478
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 479 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQE-QGTHPKFQ 557
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKSPYFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 558 KPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriigLDQVAGMSEtalpgafk 637
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LSTEKGLAR-------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 638 tRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 717
Cdd:cd14875 536 -RK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 12667788 718 RQRYEILTPNSIPKGFMDGK--QACVLMI----KALELDSNLYRIGQSKVFFR 764
Cdd:cd14875 612 CRYFYLIMPRSTASLFKQEKysEAAKDFLayyqRLYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-764 |
2.92e-111 |
|
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: 369.99 E-value: 2.92e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH-----EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 169 SILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-----VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMR 327
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 328 IMgIPEEEQMGLLRVISGVLQLGNIVFKKERN--TDQASMPDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTM 484
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 485 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPAgpPGILALLDEECWFPKATDKSFVE---KVMQEQGTHPKfqKPKQ 561
Cdd:cd14886 394 FKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPN--LSIFSFLEEQCLIQTGSSEKFTSsckSKIKNNSFIPG--KGSQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 562 LKdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLdqvagmsetalpgafktRKG 641
Cdd:cd14886 469 CN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-----------------MKG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 642 MFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14886 528 KF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRN 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 12667788 722 EILT--PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14886 606 KILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
95-721 |
4.18e-107 |
|
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: 360.18 E-value: 4.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 164 DREDQSILCTGESGAGKTENTKKVIQYLA------------YVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 232 SSRFGKFIRINF-DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-----AGEHLKTDLLLEPYNKYRFLSN 305
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 306 GHVTI--PGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-----KKERNT--DQASMPDNTAA----- 371
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 372 QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------------- 437
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 438 DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEK 517
Cdd:cd14899 401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 518 PagPPGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 594
Cdd:cd14899 480 R--PIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 595 NIATLLHQSSDKFVSELWKDVDRiiglDQVAGMSETALPGAFKTRKGMFRT----VGQLYKEQLAKLMATLRNTNPNFVR 670
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSND----EDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVR 633
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 12667788 671 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14899 634 CIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
95-764 |
4.17e-101 |
|
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: 342.78 E-value: 4.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYS--------GLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 167 DQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 246
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG-LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvtiPGQQDKDMF--QETME 324
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDPESTdlRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 325 AMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTA--------AQKVSHLL-------GINVTDFTRGI 389
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 390 LT--------PRIKVGRDYV------------QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR------- 442
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 443 ------QGASFIGILDIAGFEIF---DLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQPC 511
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 512 IDLIEKPA---------------------GPPGILALLDE------ECWFPKATDKSFVEKVMQEQGTHPKFQK--PKQL 562
Cdd:cd14887 463 STLTSSPSstspfsptpsfrsssafatspSLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLhQSSDKFVSElwkdvdriIGLDQVAGMSetalpgAFKTRKgm 642
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKKNSGVR------AISSRR-- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 643 fRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14887 606 -STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYE 684
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 12667788 723 ILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14887 685 TKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
92-763 |
2.08e-97 |
|
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: 329.51 E-value: 2.08e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 92 LNEASVLHNLKERYYSGLIYTY---SGLfcVVINPYKNLPIYSEEIVEMYK-------GKKRHEMPPHIYAITDTAYRSM 161
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 162 MQDREDQSILCTGESGAGKTENTKKVI-QYLAYVASSHKSKKdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK----LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVT--IPGQQDK 316
Cdd:cd14879 155 LQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHPLplGPGSDDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 317 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF--KKERNTDQASMpDNTAA-QKVSHLLGINVTDFtRGILTPR 393
Cdd:cd14879 235 EGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSLTYK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 394 IK-VGRD----YVQKAQTKEQADfaieALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFD---LNSFE 465
Cdd:cd14879 313 TKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRSstgGNSLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 466 QLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIEKPAGppGILALLDEEC-WFPKATD 539
Cdd:cd14879 389 QFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGKPG--GLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 540 KSFVEKVMQEQGTHPKF---QKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLndniatllhqSSDkFVSelwkdvd 616
Cdd:cd14879 461 EQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 617 riigldqvagmsetalpgafktrkgMFRTVGQLyKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14879 523 -------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLG 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 697 VLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgFMDGKQACVLMIKALELDSNLYRIGQSKVFF 763
Cdd:cd14879 577 LPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
96-726 |
4.32e-97 |
|
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: 326.47 E-value: 4.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNlpIYSEEIVEMYKGKKRHeMPPHIYAITDTAYRSMMQdREDQSILCTGE 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvnGYIVGANIE 255
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDlllepYNKYRF-LSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSEKYKMTCSAMKSLGIANFKSI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 335 EQMGLlrvisGVLQLGNIVFKKERNTDQASmpdNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14898 225 EDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 415 EALAKATYERMFRWLVLRINKALDKTkrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 495 EGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKvMQEQGTHpkfqkpkQLKDKADFCII--H 572
Cdd:cd14898 374 EGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVK-IKKYLNG-------FINTKARDKIKvsH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 573 YAGKVDYKADEWLMKNMDplndniatllhqssdkfvselwKDVDRIIGLDQVAgmsetalpgafktRKGMFRTVGQLYKE 652
Cdd:cd14898 442 YAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN-------------DEGSKEDLVKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 653 QLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
95-764 |
3.30e-96 |
|
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: 325.82 E-value: 3.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEivemYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYlaYVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14937 77 ESGSGKTEASKLVIKY--YLSGV----KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd14937 151 EIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMHDM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 335 EQmGLLRVISGVLQLGNIVFK---KERNTDQASMPDNT--AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd14937 231 KD-DLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 410 ADFAIEALAKATYERMFRWLVLRINKALDKTKrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14937 310 SVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKET 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 490 EEYQREGIEWNFIDFGLDlQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKaDFC 569
Cdd:cd14937 389 ELYKAEDILIESVKYTTN-ESIIDLLR---GKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK-NFV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagMSETAlpgafkTRKGMfrtVGQL 649
Cdd:cd14937 464 IKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSESL------GRKNL---ITFK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRVVFQEFRQRYEILTPNSI 729
Cdd:cd14937 525 YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTS 603
|
650 660 670
....*....|....*....|....*....|....*
gi 12667788 730 PKGFMDGKQACVLMIKAlELDSNLYRIGQSKVFFR 764
Cdd:cd14937 604 KDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
95-764 |
1.32e-93 |
|
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: 318.68 E-value: 1.32e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 172 CTGESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 250
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-----FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH----VTIPGQQDKDMFQETMEAM 326
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 407 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14878 316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 484 MFILEQEEYQREGIEWNFIDFGLDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKP 559
Cdd:cd14878 396 LFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPS---GFLSLLDEESQMIWSVEPNLPKKLqslLESSNTNAVYSPM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 560 KQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriigldqvagmsetal 632
Cdd:cd14878 473 KDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL--------------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 633 pgaFKTRkgmFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 712
Cdd:cd14878 532 ---FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRL 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 12667788 713 VFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14878 606 SFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
95-716 |
7.94e-82 |
|
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: 285.26 E-value: 7.94e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHE-------MPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 167 DQSILCTGESGAGKTENTKKVIQYLAYVasshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-- 244
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEev 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 245 -------VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSN----------G 306
Cdd:cd14884 157 entqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPdeshqkrsvkG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 307 HVTIPG----------QQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKkerntdqasmpdntaaqKVSH 376
Cdd:cd14884 237 TLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------AAAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 377 LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA----------- 445
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysine 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 446 SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKpagppgIL 525
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK------IF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 526 ALLDE-----ECWFPKATDKSFV-----EKVMQEQGTH------PKFQK---PKQLKDKADFCIIHYAGKVDYKADEWLM 586
Cdd:cd14884 453 RRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINNWID 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 587 KNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNP 666
Cdd:cd14884 533 KNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDM 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 12667788 667 NFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14884 590 YYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
96-750 |
1.01e-81 |
|
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: 283.16 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYknlpiyseeiveMYKGKKRH-------EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 169 SILCTGESGAGKTENTKKVIQYLAYVASshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFd 244
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQET 322
Cdd:cd14881 141 TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 323 MEAMRIMGIPeeeQMGLLRVISGVLQLGNIVFKkERNTDQASMPDNTAAQKVSHLLGINVTDFTRGiLTPRIK-VGRDYV 401
Cdd:cd14881 221 KACLGILGIP---FLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKaldkTKRQGAS--------FIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14881 296 KSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 474 EKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIEkpAGPPGILALLDEECwFPKATDKSFVEKVMQEQGT 552
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 553 HPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdvdriigldqvagmsetal 632
Cdd:cd14881 448 NPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 633 pgAFKTRKGMFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 712
Cdd:cd14881 502 --GFATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRM 572
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 12667788 713 VFQEFRQRYEILTPNSIPKGFMDGKQAC--VLMIKALELD 750
Cdd:cd14881 573 RFKAFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQP 612
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
95-729 |
1.83e-69 |
|
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: 247.09 E-value: 1.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYkgkkrhemppHIYAITDTAYRSMMQDRED-QSILCT 173
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDVNgYIVGAN 253
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 254 IE-TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14874 143 LKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 333 EEEQMGLLRVISGVLQLGNIVFKKERNTD---QASMPDNTAAQK-VSHLLGINVTDFTRgILTPRIKVGrdyvqKAQTKE 408
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLVN-FLLPKSEDG-----TTIDLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 489 QEEYQREGIEWNF-IDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlKDKAD 567
Cdd:cd14874 375 LVDYAKDGISVDYkVPNSIENGKTVELLFKK--PYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KERLE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmsetalpgAFKTRKgMFRTVG 647
Cdd:cd14874 452 FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-------------------SSNTSD-MIVSQA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14874 512 QFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPG 591
|
..
gi 12667788 728 SI 729
Cdd:cd14874 592 DI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
96-717 |
2.46e-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: 248.08 E-value: 2.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASShKSKKdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLS-RSKY----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 334 EEQMGLLRVISGVLQLGNIVFKKERNtdQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAqtkeqadfa 413
Cdd:cd14905 235 EKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 414 iEALAKATYERMFRWLVLRINKALDKTkrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQ 493
Cdd:cd14905 304 -DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 494 REGIEW-NFIDFGlDLQPCIDLIEKpagppgILALLDEECWFPKATDKSFVEKVMQEQGTHPKF-QKPKQlkdkadFCII 571
Cdd:cd14905 381 TERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------FGIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFV---SELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFR---- 644
Cdd:cd14905 448 HYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrDGVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLScgsn 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 645 --------------------------TVGQLYKeQLAKLMATLRNTNPN--FVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14905 528 npnnvnnpnnnsgggggggnsgggsgSGGSTYT-TYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIKSLC 606
|
650 660
....*....|....*....|....*
gi 12667788 697 VLEGIRICRQGFP----NRVVFQEF 717
Cdd:cd14905 607 LLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
96-764 |
3.03e-68 |
|
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: 243.88 E-value: 3.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 176 SGAGKTENTKKVIQYLAYVAsshksKKDQGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-----DGNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG--AGEHLKtDLLLEPYNKYRFLSNGHVTIPG---------QQDKDMFQETME 324
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSklkyrrddpEGNVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 325 AMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKerNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqgASF-----IGILDIAGFEIFDLNSFEQLCINYTNEKLQQL 479
Cdd:cd14882 313 HTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 480 FNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciDLIEKPAgppGILALLDEECwfPKATDKSFV-EKVMQEQGTHPK 555
Cdd:cd14882 390 YNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYImDRIKEKHSQFVK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 556 fqkpkqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMsetalpga 635
Cdd:cd14882 462 ------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM-------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 636 fKTRKGMFRTVGQlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQ 715
Cdd:cd14882 521 -RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQ 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 12667788 716 EFRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14882 597 EFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
98-722 |
9.34e-67 |
|
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: 242.18 E-value: 9.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 98 LHNLKERYYSGLIYTYSGLFCVVINPYKNLPIY----------SEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRED 167
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 168 QSILCTGESGAGKTENTKKVIQYLAYVASS----HKSKKDQGELE---RQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAgEH---LKTDLLL-EPYNKYRFLSN-----GHVTIP 311
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadplaTNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 312 GQQDKDMfqetMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-------KKERNTDQASMPDNTA------AQ--KVSH 376
Cdd:cd14893 243 ARDYRDL----MSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 377 LLGIN--VTD---FTRGILTpriKVGRDYVQ--KAQTKEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKR--- 442
Cdd:cd14893 319 LLEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKsni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 443 ----QGasfIGILDIAGFEIFD--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQ 509
Cdd:cd14893 396 vinsQG---VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 510 PCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAD------------FCIIHYAGKV 577
Cdd:cd14893 473 KCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 578 DYKADEWLMKNMDPLNDNIATLLHQSSDKfvselwkdVDRIIGLDQVA------GMSETALPGAF--KTRKGMFR----- 644
Cdd:cd14893 551 TYNGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAaassekAAKQTEERGSTssKFRKSASSaresk 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 645 -----TVGQLYKEQLAKLMAtLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 719
Cdd:cd14893 623 nitdsAATDVYNQADALLHA-LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFR 701
|
...
gi 12667788 720 RYE 722
Cdd:cd14893 702 RYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
117-248 |
8.70e-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: 8.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 117 FCVVINPYKNLPIYSEEIV-EMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVA 195
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12667788 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 ... |
96-762 |
1.76e-58 |
|
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: 216.63 E-value: 1.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK-GKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 175 ESGAGKTENTKKVIQYLAYVASSHKS------------------KKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRlptnlndqeednihneenTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 237 KFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 317 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNI-----VFKKE---------------------RNTDQASMPDNTA 370
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 371 AQKV-SHLLGINVTDFTRGILTPRIkVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR--QGASF 447
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 448 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgpPGILAL 527
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPT--EGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 528 LDEECWFPKATDKS-FVEKVMQEQGTHPKFQKPKQLK-DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 605
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 606 KFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQ----LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKA- 680
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 681 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgfmDGKQACVLMIKALELDSNLYRIGQSK 760
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 12667788 761 VF 762
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
933-1830 |
1.48e-33 |
|
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: 142.12 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 933 HLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1012
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEELRE-----ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1013 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARV 1092
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE-------AQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1093 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtlDSTAAQQELRSKREQEvniL 1172
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQQEIEEL---L 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1173 KKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnevkvllqgkgdSEHKRKKVEA 1252
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA------------QLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1253 QLQELQVKFNEGERvrteladKVTKLQVELDNVTGLLSQSDSKSSKLTKdfsALESQLQDT-QELLQEENRQKLSLSTKL 1331
Cdd:TIGR02168 496 RLQENLEGFSEGVK-------ALLKNQSGLSGILGVLSELISVDEGYEA---AIEAALGGRlQAVVVENLNAAKKAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1332 KQVEDEKNSFREQLEEEEeakhnlekqiATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLE--------------GL 1397
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKG----------TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldnAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1398 SQRHEEK-----VAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR 1472
Cdd:TIGR02168 636 ELAKKLRpgyriVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1473 EKETKALSLARALEEAMEQKAELERlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATE 1552
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEA-------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1553 DAKLRLEVNLQAMKAQFeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKN 1632
Cdd:TIGR02168 789 AQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1633 RDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN 1712
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1713 ssgKGALALEEKRRLEARIAqleeeleeeqGNTELINDRLKKANLQIDQINTdlnlershaqKNENARQQLERQNKELKV 1792
Cdd:TIGR02168 948 ---EYSLTLEEAEALENKIE----------DDEEEARRRLKRLENKIKELGP----------VNLAAIEEYEELKERYDF 1004
|
890 900 910
....*....|....*....|....*....|....*...
gi 12667788 1793 KLQEMEGTVKSKYKasitaLEAKIaqleEQLDNETKER 1830
Cdd:TIGR02168 1005 LTAQKEDLTEAKET-----LEEAI----EEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1616 |
2.84e-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: 137.88 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 870 EMETLQSQLMA---EKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQ 946
Cdd:TIGR02168 240 ELEELQEELKEaeeELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 947 ELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHE 1026
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1027 AMITDLEERLRREEKQRQELEKTRRKLEGDSTDLsdQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKI 1106
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1107 RELESQISELQEDLESERASRNKAEKQKRDLGEELEAlKTELEDTLDSTAAQQELRSKREQEVNI-----LKKTLEEEAK 1181
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLSGILGVLSELISVDEGYEAAIEAalggrLQAVVVENLN 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1182 THEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKV-----EAQLQE 1256
Cdd:TIGR02168 557 AAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddLDNALE 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1257 LQVKFNEGERVRTELADKVTK-----------------LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQE 1319
Cdd:TIGR02168 637 LAKKLRPGYRIVTLDGDLVRPggvitggsaktnssileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1320 ENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQ 1399
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1400 RHEEKVAAYDKLEKTKTRLQQELDDLLVDldhQRQSACNLEKKQKKFDQLLAEEKTISakyaEERDRAEAEAREKETKAL 1479
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIE 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1480 SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDaKLRLE 1559
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-RLSEE 948
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12667788 1560 VNLQAMKA-QFERDLQGRDEQSEEKKKQLVRQVREM---------EAELEDER-----KQRSMAVAARKKLE 1616
Cdd:TIGR02168 949 YSLTLEEAeALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieEYEELKERydfltAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1035-1879 |
4.92e-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: 133.64 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1035 RLRREEKQRQeLEKTRRKLEgdstDLSDQIAELQAQIAELKMQlAKKEEELQAAlaRVEEEAAQKNMALKKIRELESQIS 1114
Cdd:TIGR02168 171 KERRKETERK-LERTRENLD----RLEDILNELERQLKSLERQ-AEKAERYKEL--KAELRELELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1115 ELQEDLESERASRNKAEKQKRDLGEELEALKTEL-EDTLDSTAAQQELrskreQEVNILKKTLEEEAKTHEAQIQEMRQK 1193
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKEL-----YALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1194 hsqaVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVkvllqgkgdsehkrkkveaqlQELQVKFNEGERVRTELAD 1273
Cdd:TIGR02168 318 ----LEELEAQLEELESKLDELAEELAELEEKLEELKEEL---------------------ESLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1274 KVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLkqVEDEKNSFREQLEEEEEAKH 1353
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1354 NLEKQIATLHAQvadmkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQR 1433
Cdd:TIGR02168 451 ELQEELERLEEA--------------LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1434 QSACNLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKA---ELERLNKQF--RTEMED 1508
Cdd:TIGR02168 517 GLSGILGVLS---ELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTEiqGNDREI 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1509 LMSSKDDVGkSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAK-LRLEVNLQAMK--------------AQFERDL 1573
Cdd:TIGR02168 594 LKNIEGFLG-VAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKkLRPGYRIVTLDgdlvrpggvitggsAKTNSSI 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1574 QGRD---EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDC 1650
Cdd:TIGR02168 673 LERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1651 MRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR 1730
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1731 IAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKAsIT 1810
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK-RS 911
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1811 ALEAKIAQLEEQLdNETKERQAACKQVRRT--EKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1879
Cdd:TIGR02168 912 ELRRELEELREKL-AQLELRLEGLEVRIDNlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
991-1851 |
4.02e-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: 130.96 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 991 AKEKKLLEDRIA---EFttnlteEEEKSKSLAKLK------NKHEAMITDLEERLRREEKQRQELEK----TRRKLEGDS 1057
Cdd:TIGR02169 152 PVERRKIIDEIAgvaEF------DRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1058 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQED-----------LESERAS 1126
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekigeLEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1127 RNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKhsqaVEELAEQLE 1206
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE----LEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1207 QTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELdnvt 1286
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL---- 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1287 gllsqsdsksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQV 1366
Cdd:TIGR02169 458 ----------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1367 ADMKKKMEDSVGCLETAeeVKRKLQK---DLEGLSQR-----HEEKVAAYDKLEKTKTRlQQELDDLLVDLDHQRQSACN 1438
Cdd:TIGR02169 528 AQLGSVGERYATAIEVA--AGNRLNNvvvEDDAVAKEaiellKRRKAGRATFLPLNKMR-DERRDLSILSEDGVIGFAVD 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1439 LEKKQKKF---------DQLLAE----------------------------------EKTISAKYAEERDRAEAEAREKE 1475
Cdd:TIGR02169 605 LVEFDPKYepafkyvfgDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1476 tkalSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAK 1555
Cdd:TIGR02169 685 ----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1556 LRLEVNLQAMKAQFErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDE 1635
Cdd:TIGR02169 761 KELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1636 AIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIanssg 1715
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI----- 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1716 kgalaleekRRLEARIAQLEEELEEEQGNTELInDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKElkvKLQ 1795
Cdd:TIGR02169 913 ---------EKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNML---AIQ 979
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1796 EMEGTVKskykasitaleaKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQV 1851
Cdd:TIGR02169 980 EYEEVLK------------RLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
970-1554 |
3.96e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 127.36 E-value: 3.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 970 EAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1050 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNK 1129
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1130 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvnilkktlEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK 1209
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1210 RVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKfnEGERVRTELADKVTKLQVELDNVTGLL 1289
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR--GLAGAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1290 SQ----SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQ 1365
Cdd:COG1196 548 LQnivvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1366 VADmkkKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAcnlekkQKK 1445
Cdd:COG1196 628 VAA---RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL------EEA 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1446 FDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskDDVGKSVHELEK 1525
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL----EELERELERLER 774
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 12667788 1526 SKRAL--------------EQQVEEMKTQLEELEDELQATEDA 1554
Cdd:COG1196 775 EIEALgpvnllaieeyeelEERYDFLSEQREDLEEARETLEEA 817
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
959-1710 |
1.22e-27 |
|
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: 122.87 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 959 RQKLQLEKVTTEaKLKKLEEEQIILEDQncKLAKEKKLLEDRIAEFTTNLTEEEEkskSLAKLknkhEAMITDLEERL-R 1037
Cdd:TIGR02169 200 LERLRREREKAE-RYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEE---ELEKL----TEEISELEKRLeE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1038 REEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQknmalkkIRELESQISELQ 1117
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1118 EDLESERasrnkaeKQKRDLGEELEALKTELEDtldstaaqqelrskreqevniLKKTLEEEAKTHeaqiQEMRQKHSQA 1197
Cdd:TIGR02169 343 REIEEER-------KRRDKLTEEYAELKEELED---------------------LRAELEEVDKEF----AETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1198 VEELAEqleqtkrvkanlekakqtLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1277
Cdd:TIGR02169 391 REKLEK------------------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1278 LQVELdnvtgllsqsdsksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEK 1357
Cdd:TIGR02169 453 QEWKL--------------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1358 QIATLHAQVADMKKKMEDSVGCLETAeeVKRKLQK---DLEGLSQR-----HEEKVAAYDKLEKTKTRlQQELDDLLVDL 1429
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERYATAIEVA--AGNRLNNvvvEDDAVAKEaiellKRRKAGRATFLPLNKMR-DERRDLSILSE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1430 DHQRQSACNLEKKQKKF---------DQLLAE----------------------------------EKTISAKYAEERDR 1466
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYepafkyvfgDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1467 AEAEAREKEtkalSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELED 1546
Cdd:TIGR02169 676 LQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1547 ELQATEDAKLRLEVNLQAMKAQFErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHI 1626
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1627 DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL 1706
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
....
gi 12667788 1707 ADEI 1710
Cdd:TIGR02169 909 EAQI 912
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
101-705 |
2.32e-25 |
|
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: 114.84 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 101 LKERYYSGLIYTYSGLFCV-VINPYKNL------PIYSEEIVEMYKGKKRHE--MPPHIYAI------------------ 153
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 154 --TDTAYRSMMQDReDQSILCTGESGAGKTENTKKVIQYLAYVA---------------------------SSHKS---- 200
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftSSTKStiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 201 ---------------------------------------------------------KKDQGELERQL------------ 211
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeKLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 212 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVNGY---IVGANIETYLLEKSRAIRQA------KEERTFHI 276
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 277 FYYLLSGAGEH-----LKTDLLLEPYN--KYRFLSNGHVTIPG--------QQDKDMFQETMEAMRIMGIPEEEQMGLLR 341
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 342 VISGVLQLGNIVFKKERNTDQASMPDN---TAAQKVSHLLGI-NVTDFTRGILTPRIKV--GRDYVQKAQTKEQADFAIE 415
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 416 ALAKATYERMFRWLVLRINKAL-------DKTKRQ---------GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLqql 479
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 480 fnhtmfileqeeYQREGiewNFIDFGLDLQPCI-------DLIEKPAGPPGILALLDEECWFPKAT----------DKSF 542
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRPHLtardsekDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLF 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 543 VEKVMQEQGThpKFQKPKQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL 611
Cdd:cd14894 628 VRNIYDRNSS--RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRM 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 612 WKDVDRiIGLD-----QVAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMatlrntnPNFVRCIIPNHEKKAGKLDPH 686
Cdd:cd14894 706 LNESSQ-LGWSpntnrSMLGSAESRLSGT-KSFVGQFRSHVNVLTSQDDKNM-------PFYFHCIRPNAKKQPSLVNND 776
|
810
....*....|....*....
gi 12667788 687 LVLDQLRCNGVLEGIRICR 705
Cdd:cd14894 777 LVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1699 |
3.41e-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: 114.78 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 856 KVREKQLAAENRLTEMETLqsqlMAEKLQLQEQLQAETElcaEAEELRArLTAKKQELE--EICHDLEARVEEEEERCQH 933
Cdd:TIGR02169 174 KALEELEEVEENIERLDLI----IDEKRQQLERLRRERE---KAERYQA-LLKEKREYEgyELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 934 LQAEKKKMQQNIQELEEQLEEEESARQKLQlekvTTEAKLKKL-EEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1012
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLE----ELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1013 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARV 1092
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1093 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNIL 1172
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1173 KKTLEE-----EAKTHEAQIQEMRQKHSQAVEELAE--------QLEQTKRVKANLEKAkqtLENERGELANEVKVllqg 1239
Cdd:TIGR02169 482 EKELSKlqrelAEAEAQARASEERVRGGRAVEEVLKasiqgvhgTVAQLGSVGERYATA---IEVAAGNRLNNVVV---- 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1240 KGDSEHKR-----KKVEA------QLQELQVKFNEGERVRTELADKVTKLQVELDNV-----------TGLLSQSDSKSS 1297
Cdd:TIGR02169 555 EDDAVAKEaiellKRRKAgratflPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARR 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1298 KLTK-DFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEeeeakhnLEKQIATLHAQVADMKKKMEDS 1376
Cdd:TIGR02169 635 LMGKyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1377 VGCLETAEEVKRKLQKDLEGLSQRHEekvAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTI 1456
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEE---KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1457 SAKYAEER--------DRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKR 1528
Cdd:TIGR02169 785 EARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1529 ALEQQVEEMKTQLEELEDELQatedaklrlevnlqamkaqferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMA 1608
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1609 VAARKKLEMDLKDLEAHIdSANKNRDEAIKQLRKLQAQMKDCMRELDD-----TRASR--EEILAQAKENEKKLKSMEAE 1681
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnMLAIQeyEEVLKRLDELKEKRAKLEEE 1001
|
890
....*....|....*...
gi 12667788 1682 MIQLQEELAAAERAKRQA 1699
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1202-1923 |
9.51e-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: 113.23 E-value: 9.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1202 AEQLEQTKRVKANLEKAKQTLE-NERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQV 1280
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1281 ELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEeeeeakhNLEKQIA 1360
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------SLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1361 TLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSACNLE 1440
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1441 KKqkKFDQLLAEEKTISAKYAEERDRAEAEareKETKALSLARALEEAMEQKAELERLNKQFRTeMEDLMSSKDDVGKSV 1520
Cdd:TIGR02168 435 LK--ELQAELEELEEELEELQEELERLEEA---LEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1521 HELEKSKRALEQQVEEMKTQLE-----ELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRD------EQSEEKKKQLVR 1589
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISvdegyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1590 QVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANkNRDEAIKQLRKLQAQMKdcMRELDDTRASREEILAQA- 1668
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1669 --------------KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQL 1734
Cdd:TIGR02168 666 aktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1735 EEELeeeqgntELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKyKASITALEA 1814
Cdd:TIGR02168 746 EERI-------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1815 KIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRR 1894
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
730 740
....*....|....*....|....*....
gi 12667788 1895 KLQRELedatetadamnREVSSLKNKLRR 1923
Cdd:TIGR02168 898 ELSEEL-----------RELESKRSELRR 915
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1082-1910 |
3.45e-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: 111.31 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1082 EEELQAALARVEEeaaqknmALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeleALKTELEDTlDSTAAQQEL 1161
Cdd:TIGR02169 169 DRKKEKALEELEE-------VEENIERLDLIIDEKRQQLERLRREREKAERYQ--------ALLKEKREY-EGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1162 RSKREQEVNILKK--TLEEEAKTHEAQIQEMRQKHSQAVEELAEQleqTKRVKANLEKAKQTLENERGELANEVKVLLQG 1239
Cdd:TIGR02169 233 EALERQKEAIERQlaSLEEELEKLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRVKEKIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1240 KGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdSKSSKLTKDFSALESQLQDTQELLQE 1319
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT-------EEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1320 ENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK-------MEDSVGCLETAEEVKRKLQK 1392
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeeKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1393 DLEGLSQRHEEKVAAYDKLEKTKTRLQQElddllvdldhqrqsacnlekkqkkfdqLLAEEKTISAKYAEERDRAEAEar 1472
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRE---------------------------LAEAEAQARASEERVRGGRAVE-- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1473 eketkaLSLARALEEAMEQKAELERLNKQFRTEMEDLMSSK--------DDVGKSVHELEKSK---RALEQQVEEMKTQL 1541
Cdd:TIGR02169 514 ------EVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRlnnvvvedDAVAKEAIELLKRRkagRATFLPLNKMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1542 EELEdelQATEDAKLRLEVNLQAMKAQFERDLQG--RDE---QSEEKKKQLVRQVR--EMEAELED-----------ERK 1603
Cdd:TIGR02169 588 RDLS---ILSEDGVIGFAVDLVEFDPKYEPAFKYvfGDTlvvEDIEAARRLMGKYRmvTLEGELFEksgamtggsraPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1604 QRSMAVAARKKLEM---DLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1680
Cdd:TIGR02169 665 GILFSRSEPAELQRlreRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1681 EMIQLQEELAAAErakrqaqQERDELADEIANSSGKGALALEEKRRLEARIAQleEELEEEQGNTELINDRLKKANLQID 1760
Cdd:TIGR02169 745 DLSSLEQEIENVK-------SELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLR 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1761 QINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTV------KSKYKASITALEAKIAQLEEQLDNETKERQAAC 1834
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1835 KQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQrANASRRKLQRELEDATETADAM 1910
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1302-1925 |
2.86e-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: 108.34 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1302 DFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLE 1381
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1382 TAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELddllvdldhqrqsaCNLEKKQKKFDQLLAEEKTISAKYA 1461
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEK--------------VTTEAKIKKLEEDILLLEDQNSKLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1462 EERDRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1541
Cdd:pfam01576 152 KERKLLEERISEFTSN-------LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1542 EELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLK- 1620
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEa 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1621 ---DLEAHIDSANKNRDEAIKQLRKLqAQMKDCMREldDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKR 1697
Cdd:pfam01576 304 lktELEDTLDTTAAQQELRSKREQEV-TELKKALEE--ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1698 QAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNE 1777
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1778 NARQQLERQNKELKVKLQEmEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRN 1857
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1858 AEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGD 1925
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFD 607
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1380-1923 |
1.15e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1380 LETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAK 1459
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1460 YAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1539
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1540 QLEELEDELQATEDAKLRLEVNLQAmkaqferdLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDL 1619
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEE--------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1620 KDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKL--KSMEAEMIQLQEELAAAERAKR 1697
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVliGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1698 QAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGN-TELINDRLKKANLQIDQINTDLNLERSHAQKN 1776
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAaVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1777 ENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQldnetKERQAACKQVRRTEKKLKDVLLQVDDERR 1856
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE-----AELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1857 NAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET----ADAMNREVSSLKNKLRR 1923
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEA 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1037-1612 |
1.19e-21 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 102.81 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1037 RREEKQRQELEKTRRKLEG-DSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEA---AQKNMALKKIRELESQ 1112
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1113 ISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTaaqqELRSKREQEVNILKKTLEEEakthEAQIQEMRQ 1192
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDR----DEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1193 KHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA 1272
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1273 DKVTKLQVELDNVTGllsqsdsKSSKLTKDFSALESQLQDTQELLQE----ENRQKLSLSTKLKQVEDEknsfREQLEEe 1348
Cdd:PRK02224 412 DFLEELREERDELRE-------REAELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVETIEED----RERVEE- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1349 eeakhnLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKdLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVD 1428
Cdd:PRK02224 480 ------LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER-REDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1429 LDHQRQSAcnlEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKAL--SLARALEEAMEQKAELERLNKQFRTEM 1506
Cdd:PRK02224 553 AEEKREAA---AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiaDAEDEIERLREKREALAELNDERRERL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1507 EDLMSSKDDVGKSVHEleKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER--DLQGRDEQSEEKK 1584
Cdd:PRK02224 630 AEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEleELRERREALENRV 707
|
570 580 590
....*....|....*....|....*....|....
gi 12667788 1585 KQL------VRQVREMEAELEDERKQRSMAVAAR 1612
Cdd:PRK02224 708 EALealydeAEELESMYGDLRAELRQRNVETLER 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1198-1798 |
1.77e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1198 VEELAEQLEQTKRVKAnLEKAKQTLENErgELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1277
Cdd:COG1196 202 LEPLERQAEKAERYRE-LKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1278 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEK 1357
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1358 QIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAC 1437
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1438 NLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELErlnkqfrtEMEDLMSSKDDVG 1517
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL--------EAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1518 KSVHELEKSKRaLEQQVEEMKTQLEELEDELQATEDAKLRLEVNlqamkaqfERDLQGRDEQSEEKKKQLVRQVREMEAE 1597
Cdd:COG1196 511 KAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1598 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKS 1677
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1678 MEAEmiQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANL 1757
Cdd:COG1196 662 LTGG--SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 12667788 1758 QIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEME 1798
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1717 |
2.78e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.14 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 859 EKQLAAENRLTEMETlqsqlmAEKLQLQEQLQAETELCAEAEELRARLTAKKQEleeichdlEARVEEEEERCQHLQAEK 938
Cdd:PTZ00121 1096 AFGKAEEAKKTETGK------AEEARKAEEAKKKAEDARKAEEARKAEDARKAE--------EARKAEDAKRVEIARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 939 KKMQQNIQELEEQLEEEESARQKLQLEKVTteaKLKKLEEEQIILEDQncKLAKEKKLLEDRIAEfttnlteEEEKSKSL 1018
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAE---ELRKAEDARKAEAAR--KAEEERKAEEARKAE-------DAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1019 AKLKnkheamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIaelKMQLAKKEEELQAALARVEEEAAQ 1098
Cdd:PTZ00121 1230 KKAE----------EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKAEEKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1099 KNMALKKIRELESQISELQEDLESER----------ASRNKAEKQKRD---LGEELEALKTELEDTLDSTAAQQELRSKR 1165
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKkaeeakkkadAAKKKAEEAKKAaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1166 EQEVNILKKTLEEEAKTHEAqiqemrQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGelANEVKVLLQGKGDSEH 1245
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEA------KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1246 KRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDfsalESQLQDTQELLQEENRQKl 1325
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA----AEAKKKADEAKKAEEAKK- 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1326 slSTKLKQVEDEKNSFR----EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRH 1401
Cdd:PTZ00121 1524 --ADEAKKAEEAKKADEakkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1402 EE----KVAAYDKLEKTKTRlQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKE-- 1475
Cdd:PTZ00121 1602 EEekkmKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEea 1680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1476 TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKS-------VHELEKSKRALEQQVEEMKTQLEELEDEL 1548
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1549 QATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKklEMDLKDLEAHIDS 1628
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADS 1838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1629 ANKNRDEAikqlrklqaqmkdcmrelDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELAD 1708
Cdd:PTZ00121 1839 KNMQLEEA------------------DAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER 1900
|
....*....
gi 12667788 1709 EIANSSGKG 1717
Cdd:PTZ00121 1901 EIPNNNMAG 1909
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
856-1420 |
4.90e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 856 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQ 935
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 936 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKS 1015
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1016 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1095
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1096 AAQKNMALKKIRELESQISELQEDLESERASRN---------KAEKQKRDLGEELEALKTEL--EDTLDSTAAQQELRSK 1164
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligVEAAYEAALEAALAAALQNIvvEDDEVAAAAIEYLKAA 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1165 REQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSE 1244
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1245 HKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDfsALESQLQDTQELLQEENRQK 1324
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER--ELAEAEEERLEEELEEEALE 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1325 LSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDsvgcLET----AEEvkrklqkDLEGLSQR 1400
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA----LGPvnllAIE-------EYEELEER 796
|
570 580
....*....|....*....|
gi 12667788 1401 HEEKVAAYDKLEKTKTRLQQ 1420
Cdd:COG1196 797 YDFLSEQREDLEEARETLEE 816
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1591 |
1.07e-19 |
|
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: 96.68 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 856 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQ 935
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 936 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKS 1015
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1016 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA---ELKMQLAKKEEELQAALarv 1092
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGSVGERYATAI--- 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1093 eeEAAQKNMALKKIRELESQISELQEDLESERASR------NKAEKQKRDLGEELE-------------------ALKTE 1147
Cdd:TIGR02169 542 --EVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRatflplNKMRDERRDLSILSEdgvigfavdlvefdpkyepAFKYV 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1148 LEDTLdstaAQQELRSKREQEVNILKKTLEEEAKTHEAQI----QEMRQKHSQAVEELAEQLEQTKRVKAnLEKAKQTLE 1223
Cdd:TIGR02169 620 FGDTL----VVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggsRAPRGGILFSRSEPAELQRLRERLEG-LKRELSSLQ 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1224 NERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDF 1303
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1304 SALESQLQDTQELLQEEnrqklslstKLKQVEDEKNSfreqleeeeeakhnLEKQIATLHAQVADMKKKMEDSVGCLETA 1383
Cdd:TIGR02169 775 HKLEEALNDLEARLSHS---------RIPEIQAELSK--------------LEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1384 EEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKtisakyaEE 1463
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE-------RK 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1464 RDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkDDVGKSVHELEKSKRALE-------QQVEE 1536
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEpvnmlaiQEYEE 983
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1537 MKTQLEELEDELqatedAKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLVRQV 1591
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 ... |
974-1866 |
2.94e-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: 95.42 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 974 KKLEEEQIILEDQNCKLAKEKKLLE--DRIAEFTTNLTEEEEKSKSLAKLKNKheamitdleERLRREEKQRQELEKTRR 1051
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEetENLAELIIDLEELKLQELKLKEQAKK---------ALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1052 KLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAE 1131
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1132 KQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvnilKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRV 1211
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE----LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1212 KANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQ 1291
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1292 SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKK 1371
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1372 KMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLA 1451
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1452 EEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDvgKSVHELEKSKRALE 1531
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAE--SELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1532 QQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAA 1611
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1612 RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQ-----MKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQ 1686
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAElleeeQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1687 EELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDL 1766
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1767 NLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKD 1846
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
890 900
....*....|....*....|
gi 12667788 1847 VLLQVDDERRNAEQYKDQAD 1866
Cdd:pfam02463 1021 EFLELFVSINKGWNKVFFYL 1040
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1080-1710 |
5.84e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 93.98 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1080 KKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtLDSTAAQQ 1159
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1160 ELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKAnLEKAKQTLENERGELANEVKVLLQG 1239
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKE----IEELEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1240 KGDSEHKRKKVEAQLQELQVKFNEGErvrtELADKVTKLQVELDNVtgllsqsdSKSSKLTKDFSALESQLQDTQELLQE 1319
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEEL--------EERHELYEEAKAKKEELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1320 ENRQKLSlsTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGC-----LETAEEVKRKLQKDL 1394
Cdd:PRK03918 384 LTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCgreltEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1395 EGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVdldhqrqsacnLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREK 1474
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESE-----------LIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1475 ETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDA 1554
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1555 KLRLEVNLQAMKaqferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARK-----KLEMDLKDLEAHIDSA 1629
Cdd:PRK03918 611 EKELEREEKELK-----KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEEL 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1630 NKNRDEAIKQLRKLQaqmkdcmRELDDTRASREEIlaqakeneKKLKSMEAEMIQLQEELAAAE-RAKRQAQQERDELAD 1708
Cdd:PRK03918 686 EKRREEIKKTLEKLK-------EELEEREKAKKEL--------EKLEKALERVEELREKVKKYKaLLKERALSKVGEIAS 750
|
..
gi 12667788 1709 EI 1710
Cdd:PRK03918 751 EI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
997-1576 |
6.98e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.57 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 997 LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST---DLSDQIAELQAQIAE 1073
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1074 LkmqlakkEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQ--------------KRDLGE 1139
Cdd:PRK02224 291 L-------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeslredaddleerAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1140 ELEALKTELEDtldstaAQQELRSKREQevnilkktleeeaktheaqiqemrqkhsqaVEELAEQLEQtkrvkanLEKAK 1219
Cdd:PRK02224 364 EAAELESELEE------AREAVEDRREE------------------------------IEELEEEIEE-------LRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1220 QTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKL 1299
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1300 TKDFSALESQlqdtqellQEENRQKLSLSTKLKQVEDEKNSFREQleeeeeaKHNLEKQIATLHAQVADMKKKME---DS 1376
Cdd:PRK02224 481 EAELEDLEEE--------VEEVEERLERAEDLVEAEDRIERLEER-------REDLEELIAERRETIEEKRERAEelrER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1377 VGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYD-KLEKTKTRLQQELDDllvdldhqRQSACNLEKKQKKFDQLLAEEKT 1455
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNsKLAELKERIESLERI--------RTLLAAIADAEDEIERLREKREA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1456 ISAKYAEERDR-AEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDvgksvheLEKSKRALEQQV 1534
Cdd:PRK02224 618 LAELNDERRERlAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQAEIGAVENEL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 12667788 1535 EEmktqLEELEDELQATEDAKLRLEV------NLQAMKAQFERDLQGR 1576
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 ... |
856-1717 |
1.84e-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: 92.73 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 856 KVREKQLAAENRLTEMETLQSQLMAEKLQ-LQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 934
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQaKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 935 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1014
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1015 SKSLAKLKNKHEAmitDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1094
Cdd:pfam02463 337 IEELEKELKELEI---KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1095 EAAQKNMALKKIRELESQISELQEDLESERA-----------------SRNKAEKQKRDLGEELEALKTELEDTLDSTAA 1157
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQGklteekeelekqelkllKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1158 QQELRSKREQEVNILKKTLEEEAKTHEA-QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1236
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGgRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1237 LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQEL 1316
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1317 LQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDsvgcletaEEVKRKLQKDLEG 1396
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL--------KKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1397 LSQRHEEKVAAYDKLEKTKTRLQQELDDllvdldhqrqsacNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKET 1476
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEE-------------KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1477 KALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKL 1556
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1557 RLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVaaRKKLEMDLKDLEAHIDSANKNRDEA 1636
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE--EAEILLKYEEEPEELLLEEADEKEK 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1637 IKQLRKLQAQMKDCM-RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSG 1715
Cdd:pfam02463 951 EENNKEEEEERNKRLlLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
..
gi 12667788 1716 KG 1717
Cdd:pfam02463 1031 KG 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
858-1223 |
3.15e-18 |
|
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: 92.04 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 858 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEIC---HDLEARVEEEEERCQHL 934
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 935 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1014
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1015 SKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1094
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1095 EAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEEL-EALKTELEDTLDSTAAQQELRSKREQEVNILK 1173
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 12667788 1174 KTLEEEAKTHEAQIQEMrqkhsqavEELAEQLEQTKRVKANLEKAKQTLE 1223
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEY--------EELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1589-1889 |
4.86e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1589 RQVREMEAELEdeRKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAqmkdcmrELDDTRASREEILAQA 1668
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1669 KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELI 1748
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1749 NDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTvKSKYKASITALEAKIAQLEEQLDNETK 1828
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1829 ERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRA 1889
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1106-1921 |
2.15e-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: 89.02 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1106 IRELESQISELQEDLESeraSRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA 1185
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1186 QiqemRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN--ERGELANEVKVLLQGKGDSEHKRK---KVEAQLQEL--Q 1258
Cdd:pfam15921 157 A----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilVDFEEASGKKIYEHDSMSTMHFRSlgsAISKILRELdtE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1259 VKFNEG---------ERVRTELADKVTKL-QVELDNVTGLLSQSDSKSSKLTKDFSALESQ---LQDTQELLQEENRQKL 1325
Cdd:pfam15921 233 ISYLKGrifpvedqlEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1326 SLStkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVAdmkkkmedsvgcLETAEEVKRKLQKDleglsQRHEEKV 1405
Cdd:pfam15921 313 SMY--MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV------------LANSELTEARTERD-----QFSQESG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1406 AAYDKLEKTKTRLqqelddllvdldHQRQSACNLEKKQKK--FDQLLAEEKTISAKYAEERDRaEAEAREKETKALSLAR 1483
Cdd:pfam15921 374 NLDDQLQKLLADL------------HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDR-NMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1484 ALEEAMEQK-AELERLNKQFR---TEMEDLMSSKDDVGKSVHELEKSKRALE---QQVEEMKTQLEELEDELQAT--EDA 1554
Cdd:pfam15921 441 ECQGQMERQmAAIQGKNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1555 KLRLEVNLQAmkaqfeRDLQGRDEQSEekkkqlvrQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRD 1634
Cdd:pfam15921 521 KLRSRVDLKL------QELQHLKNEGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1635 EAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSS 1714
Cdd:pfam15921 587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1715 GKGALALEEKRRLEARIaqleeeleeeQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENArqqlerQNKELKVKL 1794
Cdd:pfam15921 667 NELNSLSEDYEVLKRNF----------RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS------DGHAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1795 QeMEGTVKSKyKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVD-----------DERRNAEQYKD 1863
Cdd:pfam15921 731 G-MQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNkmagelevlrsQERRLKEKVAN 808
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1864 QA---DKASTRLKQLKRQLeeaeeEAQRANASRRKLQRELeDATETADAMNREVSSLKNKL 1921
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 ... |
964-1569 |
5.48e-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: 87.38 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 964 LEKVTTEAKLKKleEEQIILEDQNCKLAKEKKLLEDRIAEFttnLTEEEEKSKSLAKLKNKHeamitdleerlrreekqr 1043
Cdd:TIGR04523 105 LSKINSEIKNDK--EQKNKLEVELNKLEKQKKENKKNIDKF---LTEIKKKEKELEKLNNKY------------------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1044 QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEeeaaqknmalkKIRELESQISELQEDLESE 1123
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ-----------KNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1124 RASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV---NILKKTLEEEAKTHEAQIQEMRQKHSQavee 1200
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQ---- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1201 laeqlEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKkveaqlqELQVKFNEGERVRTELADKVTKLQV 1280
Cdd:TIGR04523 307 -----DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-------ELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1281 eldnvtgLLSQSDSKSS---KLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEK 1357
Cdd:TIGR04523 375 -------LKKENQSYKQeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1358 QIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELD--DLLVDLDHQRQS 1435
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKdlTKKISSLKEKIE 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1436 ACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSKDD 1515
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKE-------IEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1516 VGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQF 1569
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1534-1909 |
5.54e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 5.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1534 VEEMKTQLEELEDELQATEDAKlrlevNLQAMKAQFERDLQG-RDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAAR 1612
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYR-----ELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1613 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1692
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1693 ERAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQLEEELEEEQgntELINDRLKKANLQIDQINTDLNLERSH 1772
Cdd:COG1196 350 EEELEEAEAELAEAE--------------EALLEAEAELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1773 AQKNENARQQLERQNKELKVKLQEMEGTvkskyKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVD 1852
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1853 DERRNAEQYKDQADKASTRLKQ-LKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1909
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
857-1548 |
9.84e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 857 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHD---LEARVEEEEERCQH 933
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 934 LQAEKKKMQQniqeleeqleeEESARQKLQLEKVTTEAKLKKLEEEqiiledqncklakeKKLLEDRIAEFTTNLTEEEE 1013
Cdd:PRK03918 226 LEKEVKELEE-----------LKEEIEELEKELESLEGSKRKLEEK--------------IRELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1014 KSKSLAKLKNKHEAMITdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVE 1093
Cdd:PRK03918 281 KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1094 EEAAQKNMALKKIRELEsqiselqedleserasrnkaEKQKRDLGEELEALKTELEdtldstaaqqelrskreqEVNILK 1173
Cdd:PRK03918 359 ERHELYEEAKAKKEELE--------------------RLKKRLTGLTPEKLEKELE------------------ELEKAK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1174 KTLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKANLEKAKQTL-ENERGELANEVKVLLqgkgdsehkrKKVEA 1252
Cdd:PRK03918 401 EEIEEEISKITARIGELKKE----IKELKKAIEELKKAKGKCPVCGRELtEEHRKELLEEYTAEL----------KRIEK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1253 QLQELQVKFNEGERVRTELaDKVTKLQVELDNVTGLLSQSDSKSSKLTK-DFSALESQLQDTQELLQEENRQKLSLSTKL 1331
Cdd:PRK03918 467 ELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1332 KQVEdEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKkkmedsvgcLETAEEVKRKLqKDLEGLSQRHEEKVAAYDKL 1411
Cdd:PRK03918 546 KELE-KLEELKKKLAELEKKLDELEEELAELLKELEELG---------FESVEELEERL-KELEPFYNEYLELKDAEKEL 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1412 EKTKTRLQQELDDLLVDLDhqrqsacNLEKKQKKFDQLLAEEKTISAKYAEErdraeaEAREKETKALSLARALEEAMEQ 1491
Cdd:PRK03918 615 EREEKELKKLEEELDKAFE-------ELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELAGLRAE 681
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1492 KAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEqQVEEMKTQLEELEDEL 1548
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1015-1706 |
1.30e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.51 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1015 SKSLAKLKNKHEAMITDLE--ERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE-----EELQA 1087
Cdd:COG4913 231 VEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLA----ELEYLRAALRLWFAQRRLELLEAEleelrAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1088 ALARVEEEAAQKNMALKKIRELESQIS--------ELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQ 1159
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1160 ELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKV---L 1236
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFvgeL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1237 LQGKGDSEHKRKKVEAQL----------QELQVKFNE-------GERVRTEladKVTKLQVELDNVTgllSQSDSKSSKL 1299
Cdd:COG4913 467 IEVRPEEERWRGAIERVLggfaltllvpPEHYAAALRwvnrlhlRGRLVYE---RVRTGLPDPERPR---LDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1300 TKDFSALESQLQdtQELLQEENRQKlslstklkqVEDEknsfrEQLeeeeeakHNLEKQIaTLHAQVadmkkKMEDSVGC 1379
Cdd:COG4913 541 DFKPHPFRAWLE--AELGRRFDYVC---------VDSP-----EEL-------RRHPRAI-TRAGQV-----KGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1380 LETAEEVKRKLQkdlegLSQRHEEKVAAydkLEKTKTRLQQElddllvdldhqrqsacnLEKKQKKFDQLLAEEKTISAK 1459
Cdd:COG4913 592 KDDRRRIRSRYV-----LGFDNRAKLAA---LEAELAELEEE-----------------LAEAEERLEALEAELDALQER 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1460 YAEERDRAEAEAREKETKalSLARALEEAMEQKAELERLNKQFRT---EMEDLMSSKDDVGKSVHELEKSKRALEQQVEE 1536
Cdd:COG4913 647 REALQRLAEYSWDEIDVA--SAEREIAELEAELERLDASSDDLAAleeQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1537 MKTQLEELEDELQ-ATEDAKLRLEVNLQAMKAQferdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQ-RSMAVAARKK 1614
Cdd:COG4913 725 AEEELDELQDRLEaAEDLARLELRALLEERFAA-----ALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNRE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1615 LEMDLKDLEAHIDSAnknrDEAIKQLRKLqaqmkdcmrelddtrasREEILAQAKENEKKL--KSMEAEMIQLQEELaaa 1692
Cdd:COG4913 800 WPAETADLDADLESL----PEYLALLDRL-----------------EEDGLPEYEERFKELlnENSIEFVADLLSKL--- 855
|
730
....*....|....
gi 12667788 1693 ERAKRQAQQERDEL 1706
Cdd:COG4913 856 RRAIREIKERIDPL 869
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
881-1623 |
2.77e-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: 85.41 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 881 EKLQLQEQLQAET-----ELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNiQELEEQLEEE 955
Cdd:TIGR00618 173 FPLDQYTQLALMEfakkkSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS-HAYLTQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 956 ESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLedRIAEfttnlteeeeKSKSLAKLKNKHEAMITDLEER 1035
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAA----------HIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1036 LRREEKQRQElektRRKLEGDSTDLSDQIAELQaqiaelkmQLAKKEEELqaalARVEEEAAQKNMALKKIRELESQISE 1115
Cdd:TIGR00618 320 MRSRAKLLMK----RAAHVKQQSSIEEQRRLLQ--------TLHSQEIHI----RDAHEVATSIREISCQQHTLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1116 LQEDLESERASRNKAEKQKRDLGEEleALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKH- 1194
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQRE--QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHl 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1195 ---SQAVEELaEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGErvrtel 1271
Cdd:TIGR00618 462 qesAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE------ 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1272 aDKVTKLQVELDNVTGllsQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEA 1351
Cdd:TIGR00618 535 -QTYAQLETSEEDVYH---QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1352 KHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDH 1431
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1432 QRQSAC-NLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAEL--ERLNKQFRTEMED 1508
Cdd:TIGR00618 691 QLTYWKeMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1509 LMS--SKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdeqseEKKKQ 1586
Cdd:TIGR00618 771 TAAlqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKSA 842
|
730 740 750
....*....|....*....|....*....|....*..
gi 12667788 1587 LVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLE 1623
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
887-1442 |
6.09e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 887 EQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERcqhlQAEKKKMQQNIQELEEQLEEEESARQKLQLEK 966
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK----KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 967 VTTEAKlKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNL-----TEEEEKSKSLAKLKNKHEAMITDLEERLRREEK 1041
Cdd:PTZ00121 1484 KADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdeakkAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1042 QRQELEKTRrklEGDSTDLSDQIAELQAQIAELK----MQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQ 1117
Cdd:PTZ00121 1563 KKKAEEAKK---AEEDKNMALRKAEEAKKAEEARieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1118 EDLESErasRNKAEKQKRDlgEELEALKTELEdtldstaAQQELRSKREQEVniLKKTLEEEAKTHEAQIQEMRQKhsQA 1197
Cdd:PTZ00121 1640 KKEAEE---KKKAEELKKA--EEENKIKAAEE-------AKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEA--KK 1703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1198 VEELAEQLEQTKRVKANLEKAkqtlENERGELANEVKvllqgKGDSEHKRKKVEAQLQE------LQVKFNEGERVRTEL 1271
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKA----EEENKIKAEEAK-----KEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIR 1774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1272 ADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQeeNRQKLSLSTKLKQVEDEKNSFREQ---LEEE 1348
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI--NDSKEMEDSAIKEVADSKNMQLEEadaFEKH 1852
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1349 EEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDkleKTKTRLQQELDDLLVD 1428
Cdd:PTZ00121 1853 KFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNND---IIDDKLDKDEYIKRDA 1929
|
570
....*....|....
gi 12667788 1429 LDhQRQSACNLEKK 1442
Cdd:PTZ00121 1930 EE-TREEIIKISKK 1942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1029-1795 |
8.52e-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: 84.01 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1029 ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQ----IAELQA--------------QIAELKMQLAKKE---EELQA 1087
Cdd:pfam15921 112 VIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQlqntVHELEAakclkedmledsntQIEQLRKMMLSHEgvlQEIRS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1088 ALARVEEEAAQK-----NMALKKIRELESQISELQEDLESERASrnkAEKQKRDLGEELEALKTELEDTLDSTAAQQELR 1162
Cdd:pfam15921 192 ILVDFEEASGKKiyehdSMSTMHFRSLGSAISKILRELDTEISY---LKGRIFPVEDQLEALKSESQNKIELLLQQHQDR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1163 SKR---EQEVNIlkKTLEEEAKTHEAQ----------IQEM-RQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGE 1228
Cdd:pfam15921 269 IEQlisEHEVEI--TGLTEKASSARSQansiqsqleiIQEQaRNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1229 LANEVKVllqgkgdsehkrkkVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALES 1308
Cdd:pfam15921 347 LEKQLVL--------------ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1309 QLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKR 1388
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1389 KLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQkkfdqllaeektisakyaeerdrae 1468
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ------------------------- 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1469 aeareKETKALSLaraleeameQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEdEL 1548
Cdd:pfam15921 548 -----TECEALKL---------QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK-IL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1549 QATEDAKLrlevnlqamkaqfeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDS 1628
Cdd:pfam15921 613 KDKKDAKI--------------RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1629 ANKN----RDEAIKQLRKLQAQMKDCMRELDDTRASreeilaqakenekkLKSMEAE-------MIQLQEELaAAERAKR 1697
Cdd:pfam15921 679 LKRNfrnkSEEMETTTNKLKMQLKSAQSELEQTRNT--------------LKSMEGSdghamkvAMGMQKQI-TAKRGQI 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1698 QAQQERDELADE-IANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIndRLKKANLQIDQINTDLNLERSHAQKN 1776
Cdd:pfam15921 744 DALQSKIQFLEEaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL--RSQERRLKEKVANMEVALDKASLQFA 821
|
810 820
....*....|....*....|
gi 12667788 1777 EnARQQLERQNKE-LKVKLQ 1795
Cdd:pfam15921 822 E-CQDIIQRQEQEsVRLKLQ 840
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
990-1668 |
2.14e-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: 82.47 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 990 LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelektrRKLegdsTDLSDQIAELQA 1069
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM------RQL----SDLESTVSQLRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1070 QIAELKMQLAKKEEELQAAL----ARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQK-----RDLGEE 1140
Cdd:pfam15921 332 ELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1141 --LEALKTELEDtldstaaqqelRSKREQEVNILKKTLEEEAKTH-EAQIQEMRQKHS--QAVEELAEQLEQTKRV---- 1211
Cdd:pfam15921 412 itIDHLRRELDD-----------RNMEVQRLEALLKAMKSECQGQmERQMAAIQGKNEslEKVSSLTAQLESTKEMlrkv 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1212 -------KANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRteladkvtKLQVELDN 1284
Cdd:pfam15921 481 veeltakKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR--------NVQTECEA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1285 VTGLLSQSDsksskltKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1364
Cdd:pfam15921 553 LKLQMAEKD-------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1365 QVADMKKKMEDSVGC----LETAEEVKRKLQK----------DLEGLSQRHEEKVAAY----DKLEKTKTRLQQELDDLL 1426
Cdd:pfam15921 626 RVSDLELEKVKLVNAgserLRAVKDIKQERDQllnevktsrnELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQ 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1427 VDLDHQRQSACNLEKKQKKFDQL-LAEEKTISAKyaeerdRAEAEARekETKALSLARALEEAMEQKAELERLNKQFRTE 1505
Cdd:pfam15921 706 SELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK------RGQIDAL--QSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1506 MEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERD---LQGRDEQSEE 1582
Cdd:pfam15921 778 LSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDvkeLQGPGYTSNS 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1583 KKKQLVRQVREMEAELEDERKQRSMAvaarkklemdlKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRE 1662
Cdd:pfam15921 858 SMKPRLLQPASFTRTHSNVPSSQSTA-----------SFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKA 926
|
....*.
gi 12667788 1663 EILAQA 1668
Cdd:pfam15921 927 EDKGRA 932
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
971-1851 |
2.71e-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: 82.40 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 971 AKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEeeksksLAKLKNKHEAMITDLEERLRREEKQRQELEKTR 1050
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1051 RKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAalarveeeaaqknmalkkiRELESQISELQEDLESERASRNKA 1130
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS-------------------LATRLELDGFERGPFSERQIKNFH 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1131 EKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ------AVEELAEQ 1204
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSSDRILEL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1205 LEQTKRVKANLEKAKQTLENErgELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDN 1284
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTE--TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1285 VtgllSQSDSKSSKLTKDFSAlESQLQDTQEllqeenrqklSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1364
Cdd:TIGR00606 555 K----SRHSDELTSLLGYFPN-KKQLEDWLH----------SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1365 QVADMKKKMEDSVGC------LETAEEVKRKLQKDL--------------EGLSQRHEEKVAAYDKLEKTKTRLQQELDD 1424
Cdd:TIGR00606 620 QLSSYEDKLFDVCGSqdeesdLERLKEEIEKSSKQRamlagatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1425 LLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARaleEAMEQKAELERLNKQFRT 1504
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR---DIQRLKNDIEEQETLLGT 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1505 EMEDLMSSKD---DVGksvhelekSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERD-----LQGR 1576
Cdd:TIGR00606 777 IMPEEESAKVcltDVT--------IMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskIELN 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1577 DEQSEEKKKQlVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMreldd 1656
Cdd:TIGR00606 849 RKLIQDQQEQ-IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ----- 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1657 traSREEILAQAKENEKKLKSMEAEMI--QLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIaQL 1734
Cdd:TIGR00606 923 ---QEKEELISSKETSNKKAQDKVNDIkeKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI-NE 998
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1735 EEELEEEQGNTELINDRLKKANLQIDQINTDLN-LERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALE 1813
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKeVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQK 1078
|
890 900 910
....*....|....*....|....*....|....*...
gi 12667788 1814 akiaQLEEQLDNETKERQAacKQVRRTEKKLKDVLLQV 1851
Cdd:TIGR00606 1079 ----GYEKEIKHFKKELRE--PQFRDAEEKYREMMIVM 1110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1198-1922 |
3.88e-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: 81.65 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1198 VEELAEQLEQTKRVKANLEKAkQTLENERGELanEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1277
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERY-QALLKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1278 LQVELDNVTGLLSQ-SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLE 1356
Cdd:TIGR02169 270 IEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1357 KQIATLHAQVADMKKKMEDSVgclETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKT---RLQQELDDLLVDLDHQR 1433
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLR---AELEEVDKEFAETRDELKDYREKLEKLKREINELKReldRLQEELQRLSEELADLN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1434 QSACNLEKKQKKFDqllaeektisakyaEERDRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSK 1513
Cdd:TIGR02169 427 AAIAGIEAKINELE--------------EEKEDKALEIKKQEWK-------LEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1514 DDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGR-------DEQSEEKKKQ 1586
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRlnnvvveDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1587 LVRQVREMEAELEDERKQRSMAVAARKKLE-------MDLKDLEAHIDSANKN--RD----EAIKQLRKL--QAQMKDCM 1651
Cdd:TIGR02169 566 LLKRRKAGRATFLPLNKMRDERRDLSILSEdgvigfaVDLVEFDPKYEPAFKYvfGDtlvvEDIEAARRLmgKYRMVTLE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1652 RELDD--------TRASREEILAQAKENEKkLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEE 1723
Cdd:TIGR02169 646 GELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS-------RK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1724 KRRLEARIaqleeeleeeqgntELINDRLKKANLQIDQINTDLnleRSHAQKNENARQQLERQNKELkvklQEMEgTVKS 1803
Cdd:TIGR02169 718 IGEIEKEI--------------EQLEQEEEKLKERLEELEEDL---SSLEQEIENVKSELKELEARI----EELE-EDLH 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1804 KYKASITALEAKIA-----QLEEQLDNETKERQAACKQVRRTEKKLKDVLL---QVDDERRNAEQY----KDQADKASTR 1871
Cdd:TIGR02169 776 KLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQELQEQridlKEQIKSIEKE 855
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1872 LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLR 1922
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1307-1923 |
4.06e-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: 81.64 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1307 ESQLQDTQE-------LLQEENRQKLSLSTKLKQVEDEKNsFREQLEEEEEA-----KHNLEKQIATLHAQVADMKKKME 1374
Cdd:TIGR02168 178 ERKLERTREnldrledILNELERQLKSLERQAEKAERYKE-LKAELRELELAllvlrLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1375 DsvgcletAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 1454
Cdd:TIGR02168 257 E-------LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkddvgksVHELEKSKRALEQQV 1534
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-------VAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1535 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKK 1614
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELK---ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1615 LEMDLKDLEAHIDSAnKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQ--LQEELAAA 1692
Cdd:TIGR02168 480 AERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQavVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1693 ERAkrqaqqerdelADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQI------------- 1759
Cdd:TIGR02168 559 KKA-----------IAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlv 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1760 -DQINTDLNLERSHAQKNENARQQLERQNKE-LKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQV 1837
Cdd:TIGR02168 628 vDDLDNALELAKKLRPGYRIVTLDGDLVRPGgVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1838 RRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSL 1917
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
....*.
gi 12667788 1918 KNKLRR 1923
Cdd:TIGR02168 788 EAQIEQ 793
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
839-1144 |
1.26e-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: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 839 QVSRQEEEMMAKEEELVKVREKQLAAEN-------RLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQ 911
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 912 ELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLA 991
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 992 KEKK-------LLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQI 1064
Cdd:TIGR02168 845 EQIEelsedieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1065 AELQAQIAELKMQLAKKEEELqAALARVEEEAAQKNMALK---------KIRELESQISEL-------QEDLESERASRN 1128
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERL-SEEYSLTLEEAEALENKIeddeeearrRLKRLENKIKELgpvnlaaIEEYEELKERYD 1003
|
330
....*....|....*.
gi 12667788 1129 KAEKQKRDLGEELEAL 1144
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETL 1019
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
857-1682 |
1.34e-14 |
|
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: 80.09 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 857 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELrarLTAKKQELEEICHDLEARVEEEEERCQHLQA 936
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKV---FQGTDEQLNDLYHNHQRTVREKERELVDCQR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 937 EKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEE--EEK 1014
Cdd:TIGR00606 327 ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIErqEDE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1015 SKSLAKLKNkheamitDLEERLRREEKQRQELEKTR----RKLEGDSTDLSDQIAELQAQIAELKM------QLAKKEEE 1084
Cdd:TIGR00606 407 AKTAAQLCA-------DLQSKERLKQEQADEIRDEKkglgRTIELKKEILEKKQEELKFVIKELQQlegssdRILELDQE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1085 LQAALARVEEEAAQKNMALKKIRELESQiselQEDLESERASRNKAEKQKrDLGEELEALKTELEDTLDSTAAQQELRSK 1164
Cdd:TIGR00606 480 LRKAERELSKAEKNSLTETLKKEVKSLQ----NEKADLDRKLRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1165 REQEVNIL---------KKTLEEEAKTHEAQIQEMRQKHSQAVEELAeQLEQTKRVKANLEKAKQTLENERGELANEVKV 1235
Cdd:TIGR00606 555 KSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA-SLEQNKNHINNELESKEEQLSSYEDKLFDVCG 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1236 LLQGKGDSEHKRKKVE---AQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQD 1312
Cdd:TIGR00606 634 SQDEESDLERLKEEIEkssKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKS 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1313 TQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEE------V 1386
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtI 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1387 KRKLQKDLEGLSQRHEEKVAAYD--KLEKTKTRLQQELDDLLVDLDHQRQSACNLEK----KQKKFDQL------LAEEK 1454
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKliqdQQEQIQHLksktneLKSEK 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVH-ELEKSKRALEQQ 1533
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1534 VEEMKTQLEELEDelqATEDAKLRLEVNLQAMKAQFerdlqgrdEQSEEKKKQLVRQVREMEAELEDERKQRSMAV--AA 1611
Cdd:TIGR00606 954 HGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL--------EECEKHQEKINEDMRLMRQDIDTQKIQERWLQdnLT 1022
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1612 RKKLEMDLKDLEAHIDSANKNRDEaiKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1682
Cdd:TIGR00606 1023 LRKRENELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1006-1730 |
1.57e-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: 79.88 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1006 TNLTEEEEKSKSL-AKLKNKHEAmITDLEERLRREEKQRQELEKTRR-KLEGDSTDLSDQIAELQAQIAELKMQLAKKEE 1083
Cdd:pfam12128 244 TKLQQEFNTLESAeLRLSHLHFG-YKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1084 ELQAA--------LARVEEEAAQKNMALKKIRELESQ-------------ISELQEDLESERASRNKAE----KQKRD-L 1137
Cdd:pfam12128 323 ELEALedqhgaflDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdVTAKYNRRRSKIKEQNNRDiagiKDKLAkI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1138 GEELEALKTELEDTLDstAAQQELRSKREQEVNILKktleEEAKTHEAQIQEM--RQKHSQAVEELAEQLEQTKrvkANL 1215
Cdd:pfam12128 403 REARDRQLAVAEDDLQ--ALESELREQLEAGKLEFN----EEEYRLKSRLGELklRLNQATATPELLLQLENFD---ERI 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1216 EKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSK 1295
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGK 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1296 --SSKLTK----DFSALESQLQDTQEL----LQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQ 1365
Cdd:pfam12128 554 viSPELLHrtdlDPEVWDGSVGGELNLygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1366 VADMKKKMEDSVGCLETAEEVKRKLqkdleglsqrHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSacnLEKKQKK 1445
Cdd:pfam12128 634 LEKASREETFARTALKNARLDLRRL----------FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1446 FDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMedlmsskddvgksvheleK 1525
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS-GAKAELKALETWYKRDL------------------A 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1526 SKRALEQQVEEMKTQLEELEDELQatedaklRLEVNLQAMkAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDerkqr 1605
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIE-------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISE----- 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1606 smavaarkkLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDtRASREEILAQAKENEKKLKSMEAEMIQL 1685
Cdd:pfam12128 826 ---------LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC-EMSKLATLKEDANSEQAQGSIGERLAQL 895
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 12667788 1686 QEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR 1730
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDH 940
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
821-1393 |
2.05e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 821 KLRNWQWWRLFTKVKPLLQVSRQEEEMMAKE---EELVKVREKQLAAENRLTEMETLQSQLmaeKLQLQEQLQAEtELCA 897
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEArkaDELKKAEEKKKADEAKKAEEKKKADEA---KKKAEEAKKAD-EAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 898 EAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLE 977
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 978 EEQIILEDQNCKLAKEKKLLEdriaefttnLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelEKTRRKLEgds 1057
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADE---------AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA--EEAKKKAE--- 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1058 tdlsdqiAELQAQIAELKMQLAKKEEELQaalaRVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRdl 1137
Cdd:PTZ00121 1468 -------EAKKADEAKKKAEEAKKADEAK----KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK-- 1534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1138 gEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKA---- 1213
Cdd:PTZ00121 1535 -KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeak 1613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1214 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADK-----VTKLQVELDNVTGL 1288
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeAKKAEEDEKKAAEA 1693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1289 LSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSfREQLEEEEEAKHNLEKQIATLHAQVAD 1368
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK-AEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
570 580
....*....|....*....|....*
gi 12667788 1369 MKKKMEDSVGCLETAEEVKRKLQKD 1393
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1413 |
3.79e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 854 LVKVREKQLAA-ENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQ 932
Cdd:PRK03918 194 LIKEKEKELEEvLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK----LEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 933 HLQAEKKKMQQNIQELEEQLEEEESARqKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1012
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1013 EKSKSLAKLKNKHEA--MITDLEERLRREEKQR-----QELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEEL 1085
Cdd:PRK03918 349 ELEKRLEELEERHELyeEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELK----KEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1086 QAALARVE-------------EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKteLEDTL 1152
Cdd:PRK03918 425 KKAIEELKkakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1153 DstaaqqELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ--AVEELAEQLEQTKRVKANLEKAKQTLENERGELA 1230
Cdd:PRK03918 503 E------QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1231 NEVKVLlqGKGDSEHKRKKVEaQLQELQVKFNEGERVRTELADKVTKLQVELDNvtglLSQSDSKSSKLTKDFSALESQL 1310
Cdd:PRK03918 577 KELEEL--GFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEELRKEL 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1311 QDTQELLQEENRQKlsLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKmedsvgcletAEEVKrKL 1390
Cdd:PRK03918 650 EELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA----------KKELE-KL 716
|
570 580
....*....|....*....|...
gi 12667788 1391 QKDLEGLsQRHEEKVAAYDKLEK 1413
Cdd:PRK03918 717 EKALERV-EELREKVKKYKALLK 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
860-1593 |
4.41e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 860 KQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAE----AEELRARLTAKKQELEEICHDLEARVEeeeercqhlq 935
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkkAEEKKKADEAKKAEEKKKADEAKKKAE---------- 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 936 aEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILE--DQNCKLAKEKKLLEDRIAEFTTNLTEEEE 1013
Cdd:PTZ00121 1313 -EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1014 KSKslaKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlAKKEEELQAALARVE 1093
Cdd:PTZ00121 1392 KAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK---KKAEEAKKAEEAKKK 1465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1094 EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILK 1173
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1174 KTLEEEAKTHEAQIQEMRQKHSQAVEElAEQLEQTKRVKANLEKAKQTLENERGELANEVKvllqgKGDSEHKRKKVEAQ 1253
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK-----KMKAEEAKKAEEAK 1619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1254 LQELQVKFNEGERVRTELADKVTKLQVEldnvtgllsqsdsKSSKLTKDFSalESQLQDTQELLQEENRQKlsLSTKLKQ 1333
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKK-------------KAEELKKAEE--ENKIKAAEEAKKAEEDKK--KAEEAKK 1682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1334 VEDEKNSFREQLEEEEEAKHNLEKqiatLHAQVADMKKKMEDsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEK 1413
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEE----LKKKEAEEKKKAEE----LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1414 TKTRLQQElddllvdldhQRQSACNLEKKQKKFDQLLAEEktisAKYAEERDRAEAEAREKETKAlSLARALEEAMEQKA 1493
Cdd:PTZ00121 1755 EKKKIAHL----------KKEEEKKAEEIRKEKEAVIEEE----LDEEDEKRRMEVDKKIKDIFD-NFANIIEGGKEGNL 1819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1494 ELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEE-------MKTQLEELEDELQATEDAKLRLEVNLQAMK 1566
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEdgnkeadFNKEKDLKEDDEEEIEEADEIEKIDKDDIE 1899
|
730 740 750
....*....|....*....|....*....|....*
gi 12667788 1567 AQF-ERDLQGRDEQS-------EEKKKQLVRQVRE 1593
Cdd:PTZ00121 1900 REIpNNNMAGKNNDIiddkldkDEYIKRDAEETRE 1934
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1034-1862 |
5.65e-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: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1034 ERLRREEKQRQELEKTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKnmalKKIRELE 1110
Cdd:COG3096 282 ELSERALELRRELFGARRQL----AEEQYRLVEMARELEELSARESDLEQDYQAAsdhLNLVQTALRQQ----EKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1111 SQISELQEDLESERASRNKAEKQKRDLGEELEA-------LKTELED---TLDS--TAA---QQELRSKRE-QEVNILKK 1174
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVqqTRAiqyQQAVQALEKaRALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1175 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN-----ERGELANEVKVLLQGKGDSEH---K 1246
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYRSQQAlaqR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1247 RKKVEAQLQELQVKFNEGERVRTELADkvtklqveldnvtglLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEE---------------FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1327 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVadmkkkmedsvGC-LETAEEVKRKLQKDLEGLSQRHEEKv 1405
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS-----------GEaLADSQEVTAAMQQLLEREREATVER- 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1406 aayDKLEKTKTRLQQELDDLlvdldHQRQSACNLEKKQKKfDQ----LLAE---EKTISakyaeerDRAEAEAREKETKA 1478
Cdd:COG3096 647 ---DELAARKQALESQIERL-----SQPGGAEDPRLLALA-ERlggvLLSEiydDVTLE-------DAPYFSALYGPARH 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1479 LSLARALEEAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEK------SKRAL---------------- 1530
Cdd:COG3096 711 AIVVPDLSAVKEQLAGLEDC-------PEDLYliegdpDSFDDSVFDAEELEDavvvklSDRQWrysrfpevplfgraar 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1531 EQQVEEMKTQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED---- 1600
Cdd:COG3096 784 EKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEAELAALRQRRSELERELAQhraq 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1601 ERKQRSMAVAARKKLEMdlkdLEAHIDSANKNRDEAikqlrkLQAQMKDCMRELDDTRASREEI------LAQAKENEKK 1674
Cdd:COG3096 859 EQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELDAAQEAQAFIqqhgkaLAQLEPLVAV 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1675 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN----SSGKGALALEEKR----RLEARIAQLEEELEEEqgnte 1746
Cdd:COG3096 929 LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRrphfSYEDAVGLLGENSdlneKLRARLEQAEEARREA----- 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1747 liNDRLKKANLQIDQINTDL-NLERSHAQKNENArQQLERQNKELKVKL-QEMEGTV---KSKYKASITALEAKIAQLEE 1821
Cdd:COG3096 1004 --REQLRQAQAQYSQYNQVLaSLKSSRDAKQQTL-QELEQELEELGVQAdAEAEERArirRDELHEELSQNRSRRSQLEK 1080
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 12667788 1822 QLDNETKERQAACKQVRRTEKKLKdvllqvdDERRNAEQYK 1862
Cdd:COG3096 1081 QLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAK 1114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1108-1920 |
1.88e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1108 ELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA-- 1185
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDar 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1186 QIQEMRQKHSQAVEELAEQLEQTKRVKANlEKAKQTLENERGELANEVKVLLQGKgDSEHKRKKVEAQLQELQVKFNEGE 1265
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARKAEDARKAEEA-RKAEDAKKAEAARKAEEVRKAEELR-KAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1266 RVRTEL-ADKVTKLQ-VELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKlslSTKLKQVEdEKNSFRE 1343
Cdd:PTZ00121 1219 KAEDAKkAEAVKKAEeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAE-EKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1344 QLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVgclETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELD 1423
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK---KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1424 DLLVDLDHQRQSACNLEKKQKkfdqllAEEktisAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFR 1503
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKK------ADE----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1504 TEME-DLMSSKDDVGKSVHELEKsKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEE 1582
Cdd:PTZ00121 1442 EAKKaDEAKKKAEEAKKAEEAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1583 KKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQmkdcmrELDDTRASRE 1662
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE------EAKKAEEARI 1594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1663 EILAQAKENEKKLKSmeaemiqlqEELAAAERAKRQAQQERDELADEIANSSGKGALAlEEKRRLEariaqleeeleeeq 1742
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKA---------EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA-EEKKKAE-------------- 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1743 gntelindRLKKANlqidqintdlnlERSHAQKNENARQQLERQNKELKVKLQEMEgtvkSKYKASITALEAKIAQLEEQ 1822
Cdd:PTZ00121 1651 --------ELKKAE------------EENKIKAAEEAKKAEEDKKKAEEAKKAEED----EKKAAEALKKEAEEAKKAEE 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1823 LDNETKERQAACKQVRRTEKKLKdvlLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELED 1902
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
810
....*....|....*...
gi 12667788 1903 ATETADAMNREVSSLKNK 1920
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1161-1730 |
2.51e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1161 LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnEVKVLlqgk 1240
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETL---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1241 gdsehkrkkvEAQLQELQVKFNEGERVRTELADKVTKLQVEL----DNVTGLLSQSDsksskltkdfsaLESQLQDTQEL 1316
Cdd:PRK02224 257 ----------EAEIEDLRETIAETEREREELAEEVRDLRERLeeleEERDDLLAEAG------------LDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1317 LQEE-NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLE 1395
Cdd:PRK02224 315 RREElEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1396 GLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAkyaeerdraeaearEKE 1475
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEC--------------GQP 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1476 TKALSLARALEEAMEQKAELERLNKQFRTEMEDLmSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDak 1555
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE-- 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1556 lRLEvNLQAMKAQFERDLQGRDEQSEEKKKQlVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDE 1635
Cdd:PRK02224 538 -RAE-ELRERAAELEAEAEEKREAAAEAEEE-AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1636 aikqlRKLQAQMKDCMRELDDTRASREEILAqAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSG 1715
Cdd:PRK02224 615 -----REALAELNDERRERLAEKRERKRELE-AEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
570
....*....|....*
gi 12667788 1716 KgalaLEEKRRLEAR 1730
Cdd:PRK02224 689 E----LEELEELRER 699
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
999-1240 |
4.42e-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: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 999 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1078
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1079 AKKEEELQAALArveeeAAQKNMALKKIRELESQiselQEDLESERASR--NKAEKQKRDLGEELEALKTELEDTLDSTA 1156
Cdd:COG4942 100 EAQKEELAELLR-----ALYRLGRQPPLALLLSP----EDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1157 AQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1236
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....
gi 12667788 1237 LQGK 1240
Cdd:COG4942 251 LKGK 254
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
960-1709 |
4.83e-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: 74.76 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 960 QKLQLEKVTTEAKLK----KLEEEQIILEDQNcKLAKEKKLLEDRIaefTTNLTEEEEKSKSLAKLKNKHEAMITDLEER 1035
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1036 LRREEKQRQELEKTRRKLEGDSTDLSDQIAelqaqiaelKMQLAKKEEELQAALARVEEEAaqknmalkKIRELESQISE 1115
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIE---------KMILAFEELRVQAENARLEMHF--------KLKEDHEKIQH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1116 LQEDLESERasrNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQevnilkktLEEEAKTHEAQIQEMRQKHS 1195
Cdd:pfam05483 227 LEEEYKKEI---NDKEKQVSLLLIQITEKENKMKDL---TFLLEESRDKANQ--------LEEKTKLQDENLKELIEKKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1196 QAVEELAEqleqtkrVKANLEKAKQTLENERGELANEVKVLLQgkgdsehKRKKVEAQLQELQVKFNEGERVRTELADKV 1275
Cdd:pfam05483 293 HLTKELED-------IKMSLQRSMSTQKALEEDLQIATKTICQ-------LTEEKEAQMEELNKAKAAHSFVVTEFEATT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1276 TKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVE---DEKNSFREQLEEEEEAK 1352
Cdd:pfam05483 359 CSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEkllDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1353 HNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQ 1432
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1433 RQSACNLEKKQKKfdqLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS 1512
Cdd:pfam05483 519 QEDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1513 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1592
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLE 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1593 EMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENE 1672
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
730 740 750
....*....|....*....|....*....|....*..
gi 12667788 1673 KKLKSmeaemiQLQEELAAAERAKRQAQQERDELADE 1709
Cdd:pfam05483 756 LSLKK------QLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1380-1923 |
7.33e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1380 LETAEEvKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACN---------LEKKQKKFDQLL 1450
Cdd:COG4913 244 LEDARE-QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRaelarleaeLERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1451 AEEKTISAKYAE-----------ERDRAEAEAREKETKALSLARALEeAMEQKAELERlnKQFRTEMEDLMSSKDDVGKS 1519
Cdd:COG4913 323 EELDELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLA-ALGLPLPASA--EEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1520 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ-----------SEEKKKQ-- 1586
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelievrPEEERWRga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1587 ------------LV-----RQVRE------MEAELEDERKQRSMAVAARKKLE-------MDLKD------LEAHIdsaN 1630
Cdd:COG4913 480 iervlggfaltlLVppehyAAALRwvnrlhLRGRLVYERVRTGLPDPERPRLDpdslagkLDFKPhpfrawLEAEL---G 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1631 KNRD----EAIKQLRK------LQAQMKD--CMRELDDTRASREE-ILAQakENEKKLKSMEAEMIQLQEELAAAERAKR 1697
Cdd:COG4913 557 RRFDyvcvDSPEELRRhpraitRAGQVKGngTRHEKDDRRRIRSRyVLGF--DNRAKLAALEAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1698 QAQQERDeladeianssgkgalALEEKRRLEARIAQleeeleeeqgntelindrlkkanLQIDQINTDLnLERSHAQKnE 1777
Cdd:COG4913 635 ALEAELD---------------ALQERREALQRLAE-----------------------YSWDEIDVAS-AEREIAEL-E 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1778 NARQQLERQNKELkvklqemegtvkskykasitaleakiAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRN 1857
Cdd:COG4913 675 AELERLDASSDDL--------------------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1858 AEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETAdamNREVSSLKNKLRR 1923
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL---RARLNRAEEELER 791
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1383-1960 |
1.41e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1383 AEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAE 1462
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1463 ERDRAEAEAREKETKALSLARALEEAmeQKAELERLNKQFR-TEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1541
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAA--RKAEEERKAEEARkAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKF 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1542 EELEDELQATEDAKLRLEvnlQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERK----------QRSMAVAA 1611
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAE---EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadeakkkaeeAKKKADAA 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1612 RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMK---------DCMRELDDTRASREEILAQAKENEKK---LKSME 1679
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeeakkkaDAAKKKAEEKKKADEAKKKAEEDKKKadeLKKAA 1414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1680 A------EMIQLQEELAAAERAKRQAQQERDelADEIANSSGKGALALEEKRRLE-ARIAQLEEELEEEQGNTELINDRL 1752
Cdd:PTZ00121 1415 AakkkadEAKKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEeAKKADEAKKKAEEAKKADEAKKKA 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1753 KKANLQIDQINTDLNLERS--HAQKNENARQQLERQNKELKVKLQEMEGTVKSKykasiTALEAKIAQLEEQLDNETKER 1830
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-----KADELKKAEELKKAEEKKKAE 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1831 QAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQleeaeeEAQRANASRRKLQRELEDATETADAM 1910
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA------EEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1911 NREVSSLKNKLRRGDLPFVVPR-RMARKGAGDGSDEEVDGKADGAEAKPAE 1960
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAaEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
859-1319 |
1.45e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 859 EKQLAAENRLTEMETLQSQlmAEKLQLQEQLQAE----TELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 934
Cdd:PRK02224 228 QREQARETRDEADEVLEEH--EERREELETLEAEiedlRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 935 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1014
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1015 SKSLaklknkhEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1094
Cdd:PRK02224 386 IEEL-------EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECG 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1095 EAAQKNMALKKIRELESQISELQEDLESERASRNKAEKqKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKK 1174
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1175 TLEEEAKTHEAQIQEMRQKHSQAvEELAEQLEQTKRVKANLEKAKQTLENERGELAN--EVKVLLQGKGDSEHKRKKVEA 1252
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAA-AEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKRE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1253 QLQELQVKFNE-----GERVRtELADKVTKLQVE------------LDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQE 1315
Cdd:PRK02224 617 ALAELNDERRErlaekRERKR-ELEAEFDEARIEearedkeraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
....
gi 12667788 1316 LLQE 1319
Cdd:PRK02224 696 LRER 699
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1041-1868 |
2.50e-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: 72.31 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDL 1120
Cdd:TIGR00618 124 KKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1121 ESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQevnilkktleeeaKTHEAQIQEMRQKHSQAVEE 1200
Cdd:TIGR00618 204 QLLTLCTPCMPDTYHERKQVLEKELKHLRE------ALQQTQQSHAY-------------LTQKREAQEEQLKKQQLLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1201 LAEQLEQTKRVKANLEKAkqtleNERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRteladkvtklqv 1280
Cdd:TIGR00618 265 LRARIEELRAQEAVLEET-----QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL------------ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1281 eldnvtgllsqsdSKSSKLTKDFSALESQLQDTQELLQEENRqklslstkLKQVEDEKNSFREQLEEeeeaKHNLEKQIA 1360
Cdd:TIGR00618 328 -------------MKRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQ----QHTLTQHIH 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1361 TLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLE 1440
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1441 KKQKKFDQLLAEEKtisakyaeerDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMEDLMSSKDDVGK-- 1518
Cdd:TIGR00618 463 ESAQSLKEREQQLQ----------TKEQIHLQETRKKAVVLARLLELQ-EEPCPLCGSCIHPNPARQDIDNPGPLTRRmq 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1519 ----SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQgrdeqseekkkQLVRQVREM 1594
Cdd:TIGR00618 532 rgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN-----------ITVRLQDLT 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1595 EAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCM-RELDDTRASREEILAQAKENEK 1673
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQeRVREHALSIRVLPKELLASRQL 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1674 KLKSMEAEMIQL---QEELAAAERAKRQAQQ---ERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNtEL 1747
Cdd:TIGR00618 681 ALQKMQSEKEQLtywKEMLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK-AR 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1748 INDRLKKANLQIDQINTDLNLERShAQKNENARQQLERQNKELKVKLQEMEGTVKSkYKASITALEAKIAQLEEQLDNET 1827
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHL-AAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFLSRL 837
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 12667788 1828 KERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKA 1868
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1012-1498 |
3.58e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.72 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1012 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR 1091
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1092 VEEEAAQKNMAL--KKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV 1169
Cdd:COG4717 132 QELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1170 NILKKTLEEEAKTHEAQIQEMRQKhsQAVEELAEQLEQTKR----------VKANLEKAKQTLENERGELANEVKVLLQG 1239
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENE--LEAAALEERLKEARLllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1240 KGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQlqdTQELLQE 1319
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL---EEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1320 ENRQKLSLSTKLKQVEDEKnSFREQLeEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGcletaeevkrklQKDLEGLSQ 1399
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEE-ELRAAL-EQAEEYQELKEELEELEEQLEELLGELEELLE------------ALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1400 RHEEKVAAYDKLEKTKTRLQQElddllvdldhqrQSACNLEKKQKKFDQLLAEektisAKYAEERDRAEAEAREKETKAL 1479
Cdd:COG4717 433 ELEELEEELEELEEELEELREE------------LAELEAELEQLEEDGELAE-----LLQELEELKAELRELAEEWAAL 495
|
490
....*....|....*....
gi 12667788 1480 SLARALEEAMEQKAELERL 1498
Cdd:COG4717 496 KLALELLEEAREEYREERL 514
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1031-1205 |
4.52e-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: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1031 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMAlKKIRELE 1110
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1111 SqiseLQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldstaaqQELRSKREQEVNILKKTLEEEAKTHEAQIQEM 1190
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 12667788 1191 RQKHSQAVEELAEQL 1205
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1477-1712 |
4.59e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1477 KALSL-ARALeeAMEQkaeLERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAlEQQVEEMKTQ---LEELEDELQATE 1552
Cdd:COG4913 192 KALRLlHKTQ--SFKP---IGDLDDFVREYMLEEPDTFEAADALVEHFDDLERA-HEALEDAREQielLEPIRELAERYA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1553 DAKLRLEVN------LQAMKAQFERDL-QGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMD-LKDLEA 1624
Cdd:COG4913 266 AARERLAELeylraaLRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1625 HIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEmiqLQEELAAAERAKRQAQQERD 1704
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELR 422
|
....*...
gi 12667788 1705 ELADEIAN 1712
Cdd:COG4913 423 ELEAEIAS 430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1066-1796 |
5.69e-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: 71.20 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1066 ELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERasrNKAEKQKRDLGEELEALK 1145
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK---DKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1146 TEledtldstaaqQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQTLENE 1225
Cdd:TIGR04523 114 ND-----------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1226 RGELANEVKvllqgkgDSEHKRKKVEAQLQELQVKFNEgervRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSA 1305
Cdd:TIGR04523 182 KLNIQKNID-------KIKNKLLKLELLLSNLKKKIQK----NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1306 LESQLQDTQELLQEENRQklsLSTKLKQVEDEKNSFReqleeeeeakhNLEKQIATLHAQVADMKKKMEDSV-----GCL 1380
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQ---LSEKQKELEQNNKKIK-----------ELEKQLNQLKSEISDLNNQKEQDWnkelkSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1381 ETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEK-KQKKFDQLLAEEKTISAk 1459
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQIND- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1460 yaeerdrAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1539
Cdd:TIGR04523 396 -------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1540 QLEELEDELQATEdaklrlevnlqamkaqferdlqgrdEQSEEKKKQLVRQVREMEaELEDERKQrsmavaarkkLEMDL 1619
Cdd:TIGR04523 469 QLKVLSRSINKIK-------------------------QNLEQKQKELKSKEKELK-KLNEEKKE----------LEEKV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1620 KDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMREL--DDTRASREEILAQAKENEKKLKsmeaemiQLQEELAAAERAKR 1697
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIE-------ELKQTQKSLKKKQE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1698 QAQQERDELADEIANSSGKgalaLEEKrrlEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNE 1777
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKE----IEEK---EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
730
....*....|....*....
gi 12667788 1778 NARQQLERQNKELKVKLQE 1796
Cdd:TIGR04523 659 NKWPEIIKKIKESKTKIDD 677
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1615 |
7.96e-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: 70.85 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 854 LVKVREKQLAAE-----NRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEE 928
Cdd:TIGR00606 346 LVEQGRLQLQADrhqehIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 929 ERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKL--EEEQIILEDQNCKLAKEKKLLEDRIAEFTT 1006
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIleLDQELRKAERELSKAEKNSLTETLKKEVKS 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1007 NLTEEEEKSKSLAKL------KNKHEAMITDLE----------ERLRREEKQ--------------RQELEKTRRKLEGD 1056
Cdd:TIGR00606 506 LQNEKADLDRKLRKLdqemeqLNHHTTTRTQMEmltkdkmdkdEQIRKIKSRhsdeltsllgyfpnKKQLEDWLHSKSKE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1057 STDLSDQIAELQAQIAEL---KMQLAKKEEELQAALARVEEeaaqKNMALKKIRELESQISELQEDLESERASRN----- 1128
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLeqnKNHINNELESKEEQLSSYED----KLFDVCGSQDEESDLERLKEEIEKSSKQRAmlaga 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1129 --------------------------KAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1182
Cdd:TIGR00606 662 tavysqfitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1183 HEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERgELANEVKVLLQGKGDSEHKRKKVEAQLQELQVkfN 1262
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERFQMELKDVERKIAQQAAKLQG--S 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1263 EGERVRTELADKVTKLQVELDNVTgllsqsdsksskltkdfsaleSQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1342
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVV---------------------SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIG 877
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1343 EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKtrlqqel 1422
Cdd:TIGR00606 878 TNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD---SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK------- 947
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1423 ddllvdldhqrqsacnlekkqKKFDQLLAEEKTISAKYAEERDRaeaEAREKETKALSLARALEEAMEQKaelERLNKQF 1502
Cdd:TIGR00606 948 ---------------------EKVKNIHGYMKDIENKIQDGKDD---YLKQKETELNTVNAQLEECEKHQ---EKINEDM 1000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1503 RTEMEDLMSSK--DDVGKSVHELEKSKRALEQQVEEMKTQLEEL-EDELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQ 1579
Cdd:TIGR00606 1001 RLMRQDIDTQKiqERWLQDNLTLRKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRN-HVLALGRQKG 1079
|
810 820 830
....*....|....*....|....*....|....*.
gi 12667788 1580 SEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKL 1615
Cdd:TIGR00606 1080 YEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTEL 1115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1042-1298 |
8.51e-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: 8.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1042 QRQELEKTRRKLEgdstDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEEAAQKNmalKKIRELESQISELQEDLe 1121
Cdd:COG4942 18 QADAAAEAEAELE----QLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALA---RRIRALEQELAALEAEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1122 serasrNKAEKQKRDLGEELEALKTELEDTLDstAAQQelRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEEL 1201
Cdd:COG4942 86 ------AELEKEIAELRAELEAQKEELAELLR--ALYR--LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1202 AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVE 1281
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*..
gi 12667788 1282 LDNVTGLLSQSDSKSSK 1298
Cdd:COG4942 236 AAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1326-1921 |
1.12e-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: 70.05 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1326 SLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKV 1405
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1406 AAYDKLEKTK--------------TRLQQELDDLLVDLDHQRQSACNLEKKQKKF-DQLLAEEKTIsakyaeerDRAEAE 1470
Cdd:TIGR04523 124 VELNKLEKQKkenkknidkflteiKKKEKELEKLNNKYNDLKKQKEELENELNLLeKEKLNIQKNI--------DKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1471 AREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQ---QVEEMKTQLEELEDE 1547
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQlkdEQNKIKKQLSEKQKE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1548 LQATEDAKLRLEVNLQAMKAQFErDLqgRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHID 1627
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEIS-DL--NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1628 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELaaaerakRQAQQERDELA 1707
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI-------KKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1708 DEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1787
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1788 KELKVKLQEMEGTVKSkYKASITALEAKIAQLEEQLDNetKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADK 1867
Cdd:TIGR04523 506 KELEEKVKDLTKKISS-LKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1868 ASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1478-1721 |
1.17e-11 |
|
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: 68.64 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1478 ALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLR 1557
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1558 LEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAvAARKKLEMDLKDLEAHIDSANKNRDEAI 1637
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1638 KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1717
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
....
gi 12667788 1718 ALAL 1721
Cdd:COG4942 254 KLPW 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1535-1923 |
1.26e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1535 EEMKTQLEELEDELQATEDAKLRLEVN-LQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELEDERKQRsmavAARK 1613
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNgLESELAELDEEI----ERYEEQREQARETRDEADEVLEEHEERR----EELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1614 KLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE 1693
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1694 RAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHA 1773
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1774 QKNENARQQLERQNKELKVKLQEMEGTVK---------------------------SKYKASITALEAKIAQLEEQLDnE 1826
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVE-E 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1827 TKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET 1906
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
410
....*....|....*..
gi 12667788 1907 ADAMNREVSSLKNKLRR 1923
Cdd:PRK02224 574 VAELNSKLAELKERIES 590
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
870-1468 |
1.43e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.94 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 870 EMETLQSQLMA-EKL-QLQEQLQAETELCAEAEELRARLTA-----KKQELEEICHDLEARVEEEEERCQHLQAEKKKMQ 942
Cdd:COG4913 243 ALEDAREQIELlEPIrELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 943 QNIQELEEQLEEEESAR-QKLQLEKVTTEAKLKKLEEEQIILEDQ----NCKLAKEKKLLEDRIAEFTTNLTEEEEKSKS 1017
Cdd:COG4913 323 EELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAE-LQAQIAELK-----MQLAKKEEELQAALAR 1091
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPfvgelIEVRPEEERWRGAIER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1092 ----------VEEEAAQKnmALKKIRELesqisELQEDLESERASRNKAEKQKRDLGEelEALKTELEdtLDSTAAQQEL 1161
Cdd:COG4913 483 vlggfaltllVPPEHYAA--ALRWVNRL-----HLRGRLVYERVRTGLPDPERPRLDP--DSLAGKLD--FKPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1162 RSKREQEVNILKKTLEEEAKTHEAQIQEMRQ-KHSQAVEELAEQleqtKRVKANL------EKAKQTLENERGELANEVK 1234
Cdd:COG4913 552 EAELGRRFDYVCVDSPEELRRHPRAITRAGQvKGNGTRHEKDDR----RRIRSRYvlgfdnRAKLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1235 VLLQGKGDSEHKRKKVEAQLQELQ--VKFNEGERVRTELADKVTKLQVELDNvtglLSQSDSksskltkDFSALESQLQD 1312
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELER----LDASSD-------DLAALEEQLEE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1313 TQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADmkkKMEDSVGCLETAEEVKRKLQK 1392
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVERELRENLEE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1393 DLEGLSQRHEEkvaAYDKLEKTKTRLQQELDDLLV------------DLDHQRQSACNLEKKQKKFDQLLAEEKT----- 1455
Cdd:COG4913 774 RIDALRARLNR---AEEELERAMRAFNREWPAETAdldadleslpeyLALLDRLEEDGLPEYEERFKELLNENSIefvad 850
|
650
....*....|...
gi 12667788 1456 ISAKYAEERDRAE 1468
Cdd:COG4913 851 LLSKLRRAIREIK 863
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1439-1924 |
3.54e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1439 LEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskdDVGK 1518
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1519 SVHELEKSKRALEQQVEEMKTQLEELED---ELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREME 1595
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1596 AELEDERKQRSMAVAARKKLEMDLKDLEA-HIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN--- 1671
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENeLEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1672 ----EKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQgNTEL 1747
Cdd:COG4717 286 lallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1748 INDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKA-SITALEAKIAQLEEQLDNE 1826
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1827 TKERQAACKQVRRTEKKLKDVLLQvdderrnaeqykDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET 1906
Cdd:COG4717 445 EEELEELREELAELEAELEQLEED------------GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
490
....*....|....*....
gi 12667788 1907 -ADAMNREVSSLKNKLRRG 1924
Cdd:COG4717 513 rLPPVLERASEYFSRLTDG 531
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1107-1915 |
4.90e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1107 RELESQISELQEDLESERASRNKAEK--QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAkthE 1184
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE---L 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1185 AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER-GELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNE 1263
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1264 GERVRTELADkvtklqveldNVTGLLSQSDSKSSKLTKDFSALESQLQDTQEllqeenrqklslstKLKQVEDEKNSfre 1343
Cdd:COG4913 378 SAEEFAALRA----------EAAALLEALEEELEALEEALAEAEAALRDLRR--------------ELRELEAEIAS--- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1344 qleeeeeakhnLEKQIATLHAQVADMKKKMEDSVGCLET-----AE--EVK---RKLQKDLEGL----------SQRHEE 1403
Cdd:COG4913 431 -----------LERRKSNIPARLLALRDALAEALGLDEAelpfvGEliEVRpeeERWRGAIERVlggfaltllvPPEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1404 KVAAYDKLEKTKTRLQqelddllvdldhqrqsacnlekkqkkfdqllaeektisakYAEERDRAEAEAREKETKAlSLAR 1483
Cdd:COG4913 500 AALRWVNRLHLRGRLV----------------------------------------YERVRTGLPDPERPRLDPD-SLAG 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1484 aleeameqkaELERLNKQFRTEMEDLMSSKDDVGK--SVHELEKSKRALeqqveemktqleeledelqaTEDAKLRLEvn 1561
Cdd:COG4913 539 ----------KLDFKPHPFRAWLEAELGRRFDYVCvdSPEELRRHPRAI--------------------TRAGQVKGN-- 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1562 lqamKAQFERDLQGRDEQ-------SEEKKKQLVRQVREMEAELEDerkqrsmAVAARKKLEMDLKDLEAhidsanknRD 1634
Cdd:COG4913 587 ----GTRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAE-------AEERLEALEAELDALQE--------RR 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1635 EAIKQLRKLQAQMKDcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANss 1714
Cdd:COG4913 648 EALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-- 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1715 gkgalALEEKRRLEARIAQLEEELEEEQgnTELINDRLKKANLQidqintdlNLERSHAQKNENARQQLERQNKELKVKL 1794
Cdd:COG4913 725 -----AEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGD--------AVERELRENLEERIDALRARLNRAEEEL 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1795 QEMEGTVKSKYKASITALEAKIAQLEE------QLDNE---TKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQykdqa 1865
Cdd:COG4913 790 ERAMRAFNREWPAETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREIKE----- 864
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 12667788 1866 dkastRLKQLKRQLEEAE---------EEAQRANASRRKLQRELEDATETADAMNREVS 1915
Cdd:COG4913 865 -----RIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1213-1699 |
5.95e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1213 ANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQS 1292
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1293 DsksskLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEdeknsfreqleeeeeakhNLEKQIATLHAQVADMKKK 1372
Cdd:COG4717 129 P-----LYQELEALEAELAELPERLEELEERLEELRELEEELE------------------ELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1373 MEdsvgcLETAEEVKRkLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQrqsacNLEKKQKKFDQLLAE 1452
Cdd:COG4717 186 LS-----LATEEELQD-LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-----ALEERLKEARLLLLI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1453 EKTISAKYAEERDRAEAEAREKETKALSLA----------RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE 1522
Cdd:COG4717 255 AAALLALLGLGGSLLSLILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1523 LEKSKRALEQQVEEMKTQLEELEDELQ--ATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKkQLVRQVREMEAELED 1600
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1601 ERK--QRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCM--RELDDTRASREEILAQAKENEKKLK 1676
Cdd:COG4717 414 LLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWA 493
|
490 500
....*....|....*....|...
gi 12667788 1677 SMEAEMIQLQEELAAAERAKRQA 1699
Cdd:COG4717 494 ALKLALELLEEAREEYREERLPP 516
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1270-1913 |
6.01e-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: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1270 ELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNsfreqlEEEE 1349
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN------GELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1350 EAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQ---ELDDLL 1426
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSkikEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1427 VDLDHQRQSAcnleKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEA--------------MEQK 1492
Cdd:pfam12128 392 IAGIKDKLAK----IREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1493 AELERLNK------QFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQA---TEDAKLRLEVNL- 1562
Cdd:pfam12128 468 NFDERIERareeqeAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagTLLHFLRKEAPDw 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1563 -QAMKAQFERDLQGR-DEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQL 1640
Cdd:pfam12128 548 eQSIGKVISPELLHRtDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1641 RKLQAQMKDCMRELDDTRASreeiLAQAKENEKKLKS-MEAEMIQLQEelaAAERAKRQAQQERDELADEIANSSGKGAL 1719
Cdd:pfam12128 628 VQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1720 ALEEKRR--LEARIAQLEEELeeeqgntELINDRlkkaNLQIDQINTDLNLERSHAQKNENArqqLERQNK-ELKVKlqE 1796
Cdd:pfam12128 701 WLEEQKEqkREARTEKQAYWQ-------VVEGAL----DAQLALLKAAIAARRSGAKAELKA---LETWYKrDLASL--G 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1797 MEGTVKSKYKASITALEAKIAQLE---------EQLDNET--KERQAACKQVRRTEKKLKDvlLQVDDERRNAEqykdqa 1865
Cdd:pfam12128 765 VDPDVIAKLKREIRTLERKIERIAvrrqevlryFDWYQETwlQRRPRLATQLSNIERAISE--LQQQLARLIAD------ 836
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 12667788 1866 dkASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNRE 1913
Cdd:pfam12128 837 --TKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSE 882
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1450-1923 |
7.76e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1450 LAEEKTISAKYAEERDRAEA----------EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKS 1519
Cdd:PRK02224 215 LAELDEEIERYEEQREQAREtrdeadevleEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1520 VHEL-------EKSKRALEQQVEEMKTQLEELEDELqatEDAKLRLevnlQAMKAQFERdLQGRDEQSEEKKKQLVRQVR 1592
Cdd:PRK02224 295 RDDLlaeagldDADAEAVEARREELEDRDEELRDRL---EECRVAA----QAHNEEAES-LREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1593 EMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENE 1672
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1673 KKLKSMEA-EMIQLQEELAAAERAKrQAQQERDELADEIANssgkgalALEEKRRLEARIAQLEEELEEEQGnTELINDR 1751
Cdd:PRK02224 447 ALLEAGKCpECGQPVEGSPHVETIE-EDRERVEELEAELED-------LEEEVEEVEERLERAEDLVEAEDR-IERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1752 LKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKAsITALEAKIAQLEEQLDNETK--- 1828
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE-VAELNSKLAELKERIESLERirt 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1829 ---ERQAACKQVRRTEKKLKDvLLQVDDERRnaeqykDQADKASTRLKQLKRQ-----LEEAEEEAQRANASRRKLQREL 1900
Cdd:PRK02224 597 llaAIADAEDEIERLREKREA-LAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKL 669
|
490 500
....*....|....*....|...
gi 12667788 1901 EDATETADAMNREVSSLKNKLRR 1923
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEE 692
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1443-1846 |
1.01e-10 |
|
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: 66.46 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1443 QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE 1522
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1523 LEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKaqferdlqgrdeqseEKKKQLVRQVREMEAELEDER 1602
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1603 KQRSMAVAARKKLEMDLKDLEAHIDsankNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1682
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1683 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGA---LALEEKRrleariAQLEEELEEEQGNTELINDRLKKANLQI 1759
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAdasLALREGR------ARWAQERETLQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1760 DQINTDLNLERSHAQK-----------NENARQQLERQNKELKVKLQEMEGTvKSKYKASITALEAKIAQLEEQLDNET- 1827
Cdd:pfam07888 328 QRLEERLQEERMEREKlevelgrekdcNRVQLSESRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVAd 406
|
410 420
....*....|....*....|
gi 12667788 1828 -KERQAACKQVRRTEKKLKD 1846
Cdd:pfam07888 407 aKWSEAALTSTERPDSPLSD 426
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
959-1511 |
1.20e-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: 66.58 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 959 RQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKL------------LEDRIAEF---TTNLTEE-EEKSKSLAKLK 1022
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknksLESQISELkkqNNQLKDNiEKKQQEINEKT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1023 ---NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlaKKEEELQAALARVEEEAAQK 1099
Cdd:TIGR04523 246 teiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1100 NMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTL--- 1176
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqnq 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1177 EEEAKTHEAQIQEMRQKH---SQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1253
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1254 LQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKlslstKLKQ 1333
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL-----KKEN 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1334 VEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEK 1413
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1414 TKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKA 1493
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEK 718
|
570
....*....|....*...
gi 12667788 1494 ELERLnKQFRTEMEDLMS 1511
Cdd:TIGR04523 719 ELKKL-DEFSKELENIIK 735
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1016-1851 |
1.59e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1016 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDL--SDQIAELQAQIAELKMQLAKKEEELQAALARVE 1093
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqQEKIERYQADLEELEERLEEQNEVVEEADEQQE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1094 EEAAQKNMALKKIRELESQISELQE--DLESERASRNKAEKQkrdLGEELEALKTELEDTLDSTAA-QQELRSKREQEVN 1170
Cdd:PRK04863 380 ENEARAEAAEEEVDELKSQLADYQQalDVQQTRAIQYQQAVQ---ALERAKQLCGLPDLTADNAEDwLEEFQAKEQEATE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1171 ILkktLEEEAKTHEAqiQEMRQKHSQAVEELAEQLEQTKRVKANlEKAKQTLenerGELANEVKVLLQGKGdsehkrkkV 1250
Cdd:PRK04863 457 EL---LSLEQKLSVA--QAAHSQFEQAYQLVRKIAGEVSRSEAW-DVARELL----RRLREQRHLAEQLQQ--------L 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1251 EAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdsksskltkDFSALESQLQDTQELLQEENRQKLSLSTK 1330
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDED---------------ELEQLQEELEARLESLSESVSEARERRMA 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1331 LKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKvaayDK 1410
Cdd:PRK04863 584 LRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEE----------FEDSQDVTEYMQQLLERERELTVER----DE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1411 LEKTKTRLQQElddllVDLDHQRQSAcNLEKKQKKFDQ----LLAEektISAKYAEErDRAEAEAREKETKALSLARALE 1486
Cdd:PRK04863 650 LAARKQALDEE-----IERLSQPGGS-EDPRLNALAERfggvLLSE---IYDDVSLE-DAPYFSALYGPARHAIVVPDLS 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1487 EAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEKS----------------------KRALEQQVEEMK 1538
Cdd:PRK04863 720 DAAEQLAGLEDC-------PEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLR 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1539 TQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED----ERKQRSMA 1608
Cdd:PRK04863 793 AEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqEQQQRSQL 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1609 VAARKKLEMdlkdLEAHIDSANKNRDEA-IKQLRKLQAQMKDCmreLDDTR--ASREEILAQAKENEKKLKSMEAEMIQL 1685
Cdd:PRK04863 868 EQAKEGLSA----LNRLLPRLNLLADETlADRVEEIREQLDEA---EEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQL 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1686 QEELAAAERAKRQAQQERDELADEIANssgKGALALEEKRRLEAriaqleeeleEEQGNTELINDRLKKANLQIDQINTD 1765
Cdd:PRK04863 941 KQDYQQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMLA----------KNSDLNEKLRQRLEQAEQERTRAREQ 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1766 LNLERS-HAQKNE------NARQQLERQNKELKVKLQEM-----EG------TVKSKYKASITALEAKIAQLEEQLDNET 1827
Cdd:PRK04863 1008 LRQAQAqLAQYNQvlaslkSSYDAKRQMLQELKQELQDLgvpadSGaeerarARRDELHARLSANRSRRNQLEKQLTFCE 1087
|
890 900
....*....|....*....|....
gi 12667788 1828 KERQAACKQVRRTEKKLKDVLLQV 1851
Cdd:PRK04863 1088 AEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1330-1926 |
2.15e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1330 KLKQVEDEKNSFREQLEEEEEAKHNLEKQIATlhaqvadMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEkvaayd 1409
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKE-------KEKELEEVLREINEISSELPELREELEKLEKEVKE------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1410 kLEKTKTRLqqelddllvdldhqrqsacnlEKKQKKFDQLLAEEKTISAKYAEERDRAEaEAREKETKALSLARALEEAM 1489
Cdd:PRK03918 233 -LEELKEEI---------------------EELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1490 EQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQV---EEMKTQLEELEDELQATEDAKLRLEVNLQAmk 1566
Cdd:PRK03918 290 EKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL-- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1567 aqFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsmavaARKKLEMDLKDLEAHI---DSANKNRDEAIKQLRKL 1643
Cdd:PRK03918 364 --YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-------AKEEIEEEISKITARIgelKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1644 QAQMKDCMRELDDTRasREEILAqakENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERD---------ELADEIANSS 1714
Cdd:PRK03918 435 KGKCPVCGRELTEEH--RKELLE---EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliklkELAEQLKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1715 GK-GALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN----KE 1789
Cdd:PRK03918 510 EKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEE 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1790 LKVKLQEMEGTVK-----SKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDE---------- 1854
Cdd:PRK03918 590 LEERLKELEPFYNeylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeyeelreeyl 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1855 ---------RRNAEQYKDQADKASTRLKQLKRQLeeaeeeaqranASRRKLQRELED---ATETADAMNREVSSLKNKLR 1922
Cdd:PRK03918 670 elsrelaglRAELEELEKRREEIKKTLEKLKEEL-----------EEREKAKKELEKlekALERVEELREKVKKYKALLK 738
|
....
gi 12667788 1923 RGDL 1926
Cdd:PRK03918 739 ERAL 742
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1036-1905 |
2.56e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.13 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1036 LRREEKQRQELEKTRRKLEGDSTDLSdqiaELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKN---MALKKIREL 1109
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLV----EMARELAELNEAESDLEQDYQAAsdhLNLVQTALRQQEkieRYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1110 ESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE---------EEA 1180
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglpdltaDNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1181 KTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL-----ENERGELANEVKVLLQgkgdsEHKRKKVEA-QL 1254
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVrkiagEVSRSEAWDVARELLR-----RLREQRHLAeQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1255 QELQVKFNEGERvRTELADKVTKLQVELDNVTGLLSQSDSksskltkDFSALESQLQDTQELLQEENRQKLSLSTKLKQV 1334
Cdd:PRK04863 516 QQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1335 EDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKvaayDKLEKT 1414
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLAAQDALARLREQSGEE----------FEDSQDVTEYMQQLLERERELTVER----DELAAR 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1415 KTRLQQELDDLlvdldHQRQSAcNLEKKQKKFDQ----LLAEektISAKYAEErDRAEAEAREKETKALSLARALEEAME 1490
Cdd:PRK04863 654 KQALDEEIERL-----SQPGGS-EDPRLNALAERfggvLLSE---IYDDVSLE-DAPYFSALYGPARHAIVVPDLSDAAE 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1491 QKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEKS----------------------KRALEQQVEEMKTQLE 1542
Cdd:PRK04863 724 QLAGLEDC-------PEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAERE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1543 ELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED----ERKQRSMAVAAR 1612
Cdd:PRK04863 797 ELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqEQQQRSQLEQAK 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1613 KKLEMdlkdLEAHIDSANKNRDEA-IKQLRKLQAQMKDCmreLDDTR--ASREEILAQAKENEKKLKSMEAEMIQLQEEL 1689
Cdd:PRK04863 872 EGLSA----LNRLLPRLNLLADETlADRVEEIREQLDEA---EEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDY 944
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1690 AAAERAKRQAQQERDELADEIANssgKGALALEEKRRLEAriaqleeeleEEQGNTELINDRLKKANLQIDQintdlnle 1769
Cdd:PRK04863 945 QQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMLA----------KNSDLNEKLRQRLEQAEQERTR-------- 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1770 rshaqknenARQQLERQNKELKVKLQemegtVKSKYKASITALEAKIAQLEEQLDNET-KERQAACKQVRRTEKKLKDVL 1848
Cdd:PRK04863 1004 ---------AREQLRQAQAQLAQYNQ-----VLASLKSSYDAKRQMLQELKQELQDLGvPADSGAEERARARRDELHARL 1069
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1849 LQvDDERRNaeqykdqadkastrlkQLKRQLEEAEEEAQRANASRRKLQRELEDATE 1905
Cdd:PRK04863 1070 SA-NRSRRN----------------QLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1686-1931 |
4.12e-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: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1686 QEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTD 1765
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1766 LNLERSHAQKNENARQQLERQNK-ELKVKLQEMEGTVKSK--YKASITALEAKIAQLEEQLDNETKERQaackQVRRTEK 1842
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRA----ELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1843 KLKDVLLQVDDERRNAEQYKDQADKAstrLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLR 1922
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
....*....
gi 12667788 1923 RGDLPFVVP 1931
Cdd:COG4942 252 KGKLPWPVS 260
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1248-1920 |
4.91e-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: 64.66 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1248 KKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDtqellqeENRQKLSL 1327
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN-------DKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1328 STKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAA 1407
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1408 YDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLaralEE 1487
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL----EQ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1488 AMEQKAELERLNKQFRTEMEDLMSSKD-DVGKSVHElekskraleqQVEEMKTQLEELEDELQATEDAKLRLEVNLqamk 1566
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEqDWNKELKS----------ELKNQEKKLEEIQNQISQNNKIISQLNEQI---- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1567 AQFERDLQGRDEQSEEKKKQLvrqvREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSA---NKNRDEAIKQL--- 1640
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQREL----EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklNQQKDEQIKKLqqe 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1641 -RKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGAL 1719
Cdd:TIGR04523 421 kELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1720 ALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNlERSHAQKNENARQQLERQNKELkvklqemeg 1799
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN-KDDFELKKENLEKEIDEKNKEI--------- 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1800 tvkSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKdvllqvdderrnaeqykdqadkastrlkQLKRQL 1879
Cdd:TIGR04523 571 ---EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS----------------------------SLEKEL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 12667788 1880 EEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1920
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
854-1370 |
5.97e-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: 64.36 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 854 LVKVREKqlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTakkQELEEICHDLEARVEEEEERCQH 933
Cdd:pfam05483 246 LIQITEK----ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEED 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 934 LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeqiILEDQNCKLAKEkkllEDRIAEFTTNLTEEEE 1013
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKN----EDQLKIITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1014 KSKSLAKLKNKHEAMITDLEERLRREEK---QRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL----------AK 1080
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseehyLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1081 KEEELQAALARVE----EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALK---TELEDTLD 1153
Cdd:pfam05483 472 EVEDLKTELEKEKlkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekeMNLRDELE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1154 STaaQQELRSKREQEVNILKKTlEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEV 1233
Cdd:pfam05483 552 SV--REEFIQKGDEVKCKLDKS-EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1234 KVLlqgkGDSEHKRKKVEAQLQELQVKFNE---------------GERVRTEL------ADKVTKLQVELD-----NVTG 1287
Cdd:pfam05483 629 KQL----NAYEIKVNKLELELASAKQKFEEiidnyqkeiedkkisEEKLLEEVekakaiADEAVKLQKEIDkrcqhKIAE 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1288 LLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVA 1367
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
...
gi 12667788 1368 DMK 1370
Cdd:pfam05483 785 DKK 787
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
27-72 |
7.23e-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: 55.90 E-value: 7.23e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 12667788 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 ... |
1214-1868 |
1.18e-09 |
|
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: 63.50 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1214 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSD 1293
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1294 SKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK- 1372
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1373 --MEDSVGCLETAEEVKRKLQKDLEGL----SQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKF 1446
Cdd:TIGR04523 197 lkLELLLSNLKKKIQKNKSLESQISELkkqnNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1447 DQllAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVG---KSVHEL 1523
Cdd:TIGR04523 277 EQ--NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkKELTNS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1524 EKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFE------RDLQGRDEQSEEKKKQLVRQVREMEAE 1597
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQnqeklnQQKDEQIKKLQQEKELLEKEIERLKET 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1598 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKS 1677
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1678 MEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalaleekrrleariaqleeeleeeqgntelINDRLKKANL 1757
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNK-----------------------------------DDFELKKENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1758 QIDQINTDLNLERSHAQKNEnarqqLERQNKELKVKLQEmegtvkskYKASITALEAKIAQLEEQLDNETKERQAACKQV 1837
Cdd:TIGR04523 560 EKEIDEKNKEIEELKQTQKS-----LKKKQEEKQELIDQ--------KEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
650 660 670
....*....|....*....|....*....|.
gi 12667788 1838 RRTEKKLKDVLLQVDDERRNAEQYKDQADKA 1868
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
859-1454 |
1.37e-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: 63.20 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 859 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEK 938
Cdd:pfam05483 201 ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 939 KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKlledriaeftTNLTEEEEKSKSL 1018
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE----------AQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1019 AKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSDQIAELQaQIAELKMQLAKKEEELQAALARVEEEAAQ 1098
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSELE-EMTKFKNNKEVELEELKKILAEDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1099 KNMALKKIRELESQISELQEDLESErasrnkaEKQKRDLGEELEALKTELEDTLDS-----TAAQQELRSKREQEVNILK 1173
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELIFLLQAR-------EKEIHDLEIQLTAIKTSEEHYLKEvedlkTELEKEKLKNIELTAHCDK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1174 KTLEEEAKTHEAQIQEMRQKHSQavEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1253
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQ--EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1254 LQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQ------DTQELLQEENRQKLS- 1326
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayeikvNKLELELASAKQKFEe 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1327 -LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKL----QKDLEGLSQRH 1401
Cdd:pfam05483 655 iIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIieerDSELGLYKNKE 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 12667788 1402 EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 1454
Cdd:pfam05483 735 QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
932-1260 |
1.56e-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: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 932 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKleEEQIILEDQNCKLAKEKKLleDRIaefttnltEE 1011
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMEREREL--ERI--------RQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1012 EEKSKSLAKLKNKHEAM----ITDLE----ERLRREEKQRQELEKTRRKlegdSTDLSDQIAELQAQIAELKMQLAKKEE 1083
Cdd:pfam17380 356 EERKRELERIRQEEIAMeisrMRELErlqmERQQKNERVRQELEAARKV----KILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1084 ELQAALARVEEEAAQKnmaLKKIRELE----SQISELQEDLESERASRNKAEKQKRD--LGEEL--EALKTELEDTLDST 1155
Cdd:pfam17380 432 ARQREVRRLEEERARE---MERVRLEEqerqQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQrrKILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1156 AAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEkakqTLENERgELANEVKv 1235
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE----AMERER-EMMRQIV- 582
|
330 340
....*....|....*....|....*
gi 12667788 1236 llqgkgDSEHKRKKVEAQLQELQVK 1260
Cdd:pfam17380 583 ------ESEKARAEYEATTPITTIK 601
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1063-1223 |
3.14e-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: 59.55 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1063 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeELE 1142
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1143 ALKTELEdtldSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL 1222
Cdd:COG1579 93 ALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
.
gi 12667788 1223 E 1223
Cdd:COG1579 169 A 169
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1018-1631 |
3.60e-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: 61.68 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAA 1097
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1098 QKNMALKKIRELESQISELQEDLES--ERASRNKAEKQKRDLgeELEALKTELEDTLDstaaQQELRSKREQEVNILKKT 1175
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISClkNELSELRRQIQRAEL--ELQSTNSELEELQE----RLDLLKAKASEAEQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1176 LE---EEAKTHEAQIQEMRQKHSQAVEELAEqleqTKRVKANLEKAKqTLENERGELANEVKVLLQGKGDSEhkrkKVEA 1252
Cdd:pfam05557 158 LEkqqSSLAEAEQRIKELEFEIQSQEQDSEI----VKNSKSELARIP-ELEKELERLREHNKHLNENIENKL----LLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1253 QLQELQVKFNEGERVRTELADkvtkLQVELdnvtgllsqsdsksSKLTKDFSALESQLQDTQELLqeenRQKLSLSTKLK 1332
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAAT----LELEK--------------EKLEQELQSWVKLAQDTGLNL----RSPEDLSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1333 QVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHE---EKVAAYD 1409
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyrAILESYD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1410 K-LEKTKTRLQqelddllvdldhqrqsacnLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALeEA 1488
Cdd:pfam05557 367 KeLTMSNYSPQ-------------------LLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL-QA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1489 MEQKAELErlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELedELQATEDAK----LRLEVNLQA 1564
Cdd:pfam05557 427 LRQQESLA--------DPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR--CLQGDYDPKktkvLHLSMNPAA 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1565 MKAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDerkQRSMAVAARKKLEMDLKDLEAHIDSANK 1631
Cdd:pfam05557 497 EAYQQRKNQL---EKLQAEIERLKRLLKKLEDDLEQ---VLRLPETTSTMNFKEVLDLRKELESAEL 557
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
859-1226 |
3.65e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 859 EKQLAAENRLTEMETLQSQLMAEKLQ---LQEQLQAETELCAEAEELRARLTAKKQELEEICHDL----EARVEEEEERC 931
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 932 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTtEAKLKKLEEEQIILEDQN--CKLAKEKKLLEDRIAEFTTNLT 1009
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLLLLIAAalLALLGLGGSLLSLILTIAGVLF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1010 EEEE----KSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST-------DLSDQIAELQAQIAEL---- 1074
Cdd:COG4717 281 LVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlspeellELLDRIEELQELLREAeele 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1075 -KMQLAKKEEELQAALARV----EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDlgEELEALKTELE 1149
Cdd:COG4717 361 eELQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1150 DTLDSTAAQQELRSKREQEVNILKKTLEEEAktheaQIQEMRQKHSQAVEELAEQLEQTKRVK---ANLEKAKQTLENER 1226
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDG-----ELAELLQELEELKAELRELAEEWAALKlalELLEEAREEYREER 513
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1060-1698 |
3.96e-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: 61.76 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1060 LSDQIAELQAQIAELKMQLAKKEEELQAALARVE---EEAAQKNMALKKirELESQISELQEdleserasrnkaekQKRD 1136
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKtfwSPELKKERALRK--EEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1137 LGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAvEELAEQLEQTKR----VK 1212
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEH-ERQAKELFLLRKtleeME 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1213 ANLEKAKQTLeNERGELANEVKVLLQGKG--------DSEHKRKKVEAQLQ------ELQVKFNEGERVRTELADKvTKL 1278
Cdd:pfam10174 144 LRIETQKQTL-GARDESIKKLLEMLQSKGlpkksgeeDWERTRRIAEAEMQlghlevLLDQKEKENIHLREELHRR-NQL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1279 QVELDNVTGL---LSQSDSKSSKLTKDFSALESQLQ--DTQELLQEENRQKlslstKLKQVEDEKNSFR------EQLEE 1347
Cdd:pfam10174 222 QPDPAKTKALqtvIEMKDTKISSLERNIRDLEDEVQmlKTNGLLHTEDREE-----EIKQMEVYKSHSKfmknkiDQLKQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1348 EEEAKHN----LEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELD 1423
Cdd:pfam10174 297 ELSKKESellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1424 DLLVDLDHQRQSACNLEKK----QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLArALEEAMEQKAE-LERL 1498
Cdd:pfam10174 377 TLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1499 NKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ------ATEDAKLR-LEVNLQAMKAQFER 1571
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1572 dLQGRD------EQSEEKKKQLVRQVREMEAELEDERKQRSMAVA-------ARKKLEMDLKDLEAHIDSANKNRDEAIK 1638
Cdd:pfam10174 536 -LENQLkkahnaEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAeverllgILREVENEKNDKDKKIAELESLTLRQMK 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1639 QLRKLQAQMKDCMRELddtRASREEILAQAKENEKKLKSMEAEmIQLQEELAAAERAKRQ 1698
Cdd:pfam10174 615 EQNKKVANIKHGQQEM---KKKGAQLLEEARRREDNLADNSQQ-LQLEELMGALEKTRQE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
895-1125 |
4.79e-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: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 895 LCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLK 974
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 975 KLEEEQIILEDQnckLAKEKKLLEDRIAEFTTNLTEEE-------EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELE 1047
Cdd:COG4942 87 ELEKEIAELRAE---LEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1048 KTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERA 1125
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1531-1733 |
5.40e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1531 EQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVA 1610
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1611 ARKKLEMDLKDLEAHIDSanKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1690
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 12667788 1691 AAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1733
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1053-1281 |
7.44e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.80 E-value: 7.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1053 LEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR--VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKA 1130
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1131 EKQkrdLGEELEALKTELEDTLDSTAAQQelRSKREQEVNILKKTLEEE---AKTHEAQIQEMRQKHSQAVEELAEQLEQ 1207
Cdd:COG3206 246 RAQ---LGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1208 TKRVkanLEKAKQTLENERGELANEVKVLlqgkgdsehkrKKVEAQLQELQVKFNEGERVRTELADKVTKLQVE 1281
Cdd:COG3206 321 ELEA---LQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1459-1933 |
8.71e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 8.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1459 KYAEERDRAEAEAREKET--KALSLARALEEAMEQKAELERLNKQfrtemedlmsskddvgksVHELEKSKRALEQQVEE 1536
Cdd:COG4913 259 ELAERYAAARERLAELEYlrAALRLWFAQRRLELLEAELEELRAE------------------LARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1537 MKTQLEELEDELQateDAKLRLEVNLQAMKAQFERDLQGRdeqsEEKKKQLVRQVREMEAELEDERKQrsmAVAARKKLE 1616
Cdd:COG4913 321 LREELDELEAQIR---GNGGDRLEQLEREIERLERELEER----ERRRARLEALLAALGLPLPASAEE---FAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1617 MDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRAS-----------REEILAQAKENEKKLKSMeAEMIQL 1685
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRksniparllalRDALAEALGLDEAELPFV-GELIEV 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1686 QEELA----AAERAKRQAQQ-----ERDELAdeianssgkgALALEEKRRLEARIaqleeeleeeqgNTELINDRLKKAN 1756
Cdd:COG4913 470 RPEEErwrgAIERVLGGFALtllvpPEHYAA----------ALRWVNRLHLRGRL------------VYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1757 ---LQIDQINTDLNLERSHAQknENARQQLERQNKELKVK-LQEM---------EGTVKSKY------------------ 1805
Cdd:COG4913 528 rprLDPDSLAGKLDFKPHPFR--AWLEAELGRRFDYVCVDsPEELrrhpraitrAGQVKGNGtrhekddrrrirsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1806 ---KASITALEAKIAQLEEQLdNETKERQAACKQVRRTEKKLKDVLLQVDD-------------ERRNAEQYKDQADKAS 1869
Cdd:COG4913 606 fdnRAKLAALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEyswdeidvasaerEIAELEAELERLDASS 684
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1870 TRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGDLPFVVPRR 1933
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1628-1871 |
8.87e-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: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1628 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1707
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1708 DEIANSSGKGALALeekRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1787
Cdd:COG4942 97 AELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1788 KELKVKLQEMEgtvksKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADK 1867
Cdd:COG4942 174 AELEALLAELE-----EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 12667788 1868 ASTR 1871
Cdd:COG4942 249 AALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1129-1846 |
9.59e-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: 60.51 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1129 KAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQE---MRQKHSQAVEELAEQL 1205
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnaTRHLCNLLKETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1206 EQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGER-VRTELADKVTKlqveldn 1284
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEeYKKEINDKEKQ------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1285 VTGLLSQSDSKSSKLtKDFSalesqlqdtqeLLQEENRQKLSlstklkQVEDEKNSFREQLEEEEEAKHNLEKQIAtlha 1364
Cdd:pfam05483 242 VSLLLIQITEKENKM-KDLT-----------FLLEESRDKAN------QLEEKTKLQDENLKELIEKKDHLTKELE---- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1365 qvaDMKKKMEDSVGCLETAEEvkrKLQKDLEGLSQRHEEKVAAYDKLEKTKTrlqqeldDLLVDLDHQRQSACNLEK--- 1441
Cdd:pfam05483 300 ---DIKMSLQRSMSTQKALEE---DLQIATKTICQLTEEKEAQMEELNKAKA-------AHSFVVTEFEATTCSLEEllr 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1442 -KQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARaLEEAMEQKAELERLNKQFRTEMEDLMSSKDDV---- 1516
Cdd:pfam05483 367 tEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE-LKKILAEDEKLLDEKKQFEKIAEELKGKEQELifll 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1517 ---GKSVHELE-------KSKRALEQQVEEMKTQLEELE---DELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEK 1583
Cdd:pfam05483 446 qarEKEIHDLEiqltaikTSEEHYLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1584 KKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREE 1663
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1664 ILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEEleeeqg 1743
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEK------ 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1744 nTELINDRLKKANLQID-----QINTDLNLERSHAQKNENARQQLERQNKELKVKLQEmEGTVKSKYKASITALEAKIAQ 1818
Cdd:pfam05483 680 -AKAIADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE-QSSAKAALEIELSNIKAELLS 757
|
730 740
....*....|....*....|....*...
gi 12667788 1819 LEEQLDNETKERQAACKQVRRTEKKLKD 1846
Cdd:pfam05483 758 LKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1062-1253 |
1.06e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1062 DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLEserASRNKAEKQKRDLGEEL 1141
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1142 EALK---------------TELEDTLDSTAAQQELRSKREQEVNILKKtLEEEAKTHEAQIQEMRQKHSQAVEELAEQLE 1206
Cdd:COG3883 93 RALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 12667788 1207 QTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1253
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1018-1176 |
1.09e-08 |
|
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: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL--AKKEEELQAALARVEEE 1095
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1096 AAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtldstAAQQELRSKREQEVNILKKT 1175
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE------AELEELEAEREELAAKIPPE 175
|
.
gi 12667788 1176 L 1176
Cdd:COG1579 176 L 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1470-1917 |
1.19e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1470 EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ 1549
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1550 ATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKdLEAHID 1627
Cdd:PRK03918 225 KLEKEVKELEelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1628 SANKNRDEAIKQLRKLQAQMKDCMRELDDtrasREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK----------- 1696
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKakkeelerlkk 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1697 RQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTElindRLKKANLQIDQINTDLNLERSHAQKN 1776
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKCPVCGRELTEEHRKELLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1777 EnARQQLERQNKELKvKLQEMEgtvkSKYKASITALEAKIAQLEEQLdnetKERQAAcKQVRRTEKKLKDVLLQ-VDDER 1855
Cdd:PRK03918 456 E-YTAELKRIEKELK-EIEEKE----RKLRKELRELEKVLKKESELI----KLKELA-EQLKELEEKLKKYNLEeLEKKA 524
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12667788 1856 RNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRanasRRKLQRELEDATETADAMNREVSSL 1917
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEEL 582
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1083-1550 |
1.51e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1083 EELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKR--DLGEELEALKTELEDT---LDSTAA 1157
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1158 QQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLl 1237
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1238 qgkgDSEHKRKKVEAQLQELQVKFNeGERVRTELADKVTKLQVELDNVTGLLSQSDS----KSSKLTKDFSALESQLQDT 1313
Cdd:COG4717 233 ----ENELEAAALEERLKEARLLLL-IAAALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1314 QELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAkhnlEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKD 1393
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDR----IEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1394 LEGLSQRHEEKvAAYDKLEKTKTRLQQelddllvdldhqrqsacnlekkqkkfdQLLAEEKTISAKYA-EERDRAEAEAR 1472
Cdd:COG4717 384 EEELRAALEQA-EEYQELKEELEELEE---------------------------QLEELLGELEELLEaLDEEELEEELE 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1473 EKETKALSLARALEEAMEQKAELErlnkqfrTEMEDLMSSkddvgksvHELEKskraLEQQVEEMKTQLEELEDELQA 1550
Cdd:COG4717 436 ELEEELEELEEELEELREELAELE-------AELEQLEED--------GELAE----LLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1305-1557 |
2.21e-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: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1305 ALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEeeeeakhNLEKQIATLHAQVADMKKKMEDSVGCLETAE 1384
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-------ALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1385 EVKRKLQKDLEGLSQRHEEKVAAydklektktrLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEER 1464
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRA----------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1465 DRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 1544
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 12667788 1545 EDELQATEDAKLR 1557
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1392-1789 |
2.24e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1392 KDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDqLLAEEKTISAKYAEERDRAEA-E 1470
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1471 AREKETKAL--SLARALEEAMEQKAELERLNKQF----RTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 1544
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1545 EDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQ-------------LVRQVREMEAELEDERKQRSMAVAA 1611
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1612 RKKLE-MDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASReEILAQAKENEKKLKSMEAEMIQLQEELA 1690
Cdd:COG4717 313 LEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1691 AAERAKRQAQQERDELADEIANSSG--KGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNL 1768
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|.
gi 12667788 1769 ERSHAQKnENARQQLERQNKE 1789
Cdd:COG4717 472 AELLQEL-EELKAELRELAEE 491
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1026-1230 |
2.51e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1106 IRELESQISELQEDLESE-------RASR-NKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE 1177
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldRLSAlSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 12667788 1178 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA 1230
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
957-1223 |
2.60e-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: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 957 SARQKLQLEKVTTEAKLK-------KLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMI 1029
Cdd:pfam19220 41 RELPQAKSRLLELEALLAqeraaygKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1030 TDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:pfam19220 121 EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1110 ESQ-------ISELQEDLESERASRNKAEKQkrdLGEELEALKTELE------DTLDSTAA--QQELRSKREQEVNILKK 1174
Cdd:pfam19220 201 ETQldatrarLRALEGQLAAEQAERERAEAQ---LEEAVEAHRAERAslrmklEALTARAAatEQLLAEARNQLRDRDEA 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 12667788 1175 TLEEEAKTHEAQIqEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQTLE 1223
Cdd:pfam19220 278 IRAAERRLKEASI-ERDTLERR-LAGLEADLERRTQQFQEMQRARAELE 324
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1443-1905 |
2.99e-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: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1443 QKKFDQLLAEEKTISAkyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERlnKQFRTEMEDLMSSKDDVGKSVHE 1522
Cdd:TIGR00606 172 KQKFDEIFSATRYIKA---LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR--DQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1523 LEKSKRALeQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDER 1602
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1603 KQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLK--SMEA 1680
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVieRQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1681 EMIQLQEELAAAERAKRQAQQERDELADEIansSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKanlqiD 1760
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEK---KGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL-----D 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1761 QINTDLNLERSHAQKNENARQQLERqnkELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRT 1840
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKE---VKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1841 EKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATE 1905
Cdd:TIGR00606 555 KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
884-1100 |
3.12e-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: 57.85 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 884 QLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEES--ARQK 961
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAelEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 962 LQLEKVTTEA-KLKKLEEEQIILEDQNCK--------LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDL 1032
Cdd:COG4942 104 EELAELLRALyRLGRQPPLALLLSPEDFLdavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1033 EERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKN 1100
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
856-1122 |
3.66e-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: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 856 KVREKQLAAE-NRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEarvEEEEERCQHL 934
Cdd:pfam17380 364 RIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRL 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 935 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNcklakeKKLLEDRIAEFTTNLTEEEEK 1014
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR------RKILEKELEERKQAMIEEERK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1015 SKSLAKLKNKHEAMITDLEERLRREEKQRQELE-KTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQaalaRVE 1093
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKA----RAE 590
|
250 260 270
....*....|....*....|....*....|
gi 12667788 1094 EEAAQKNMALKKIreLESQISELQ-EDLES 1122
Cdd:pfam17380 591 YEATTPITTIKPI--YRPRISEYQpPDVES 618
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
858-1525 |
4.53e-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: 58.29 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 858 REKQLAAENRlTEMETLQSQLMA---EKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 934
Cdd:pfam10174 43 KERALRKEEA-ARISVLKEQYRVtqeENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 935 QAEKKK--------------MQQNIQELEEQLEEEESARQKLqLEKVTTEAKLKKLEEE------------------QII 982
Cdd:pfam10174 122 QSEHERqakelfllrktleeMELRIETQKQTLGARDESIKKL-LEMLQSKGLPKKSGEEdwertrriaeaemqlghlEVL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 983 LEDQNCKLAKEKKLLEDRiaeftTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSD 1062
Cdd:pfam10174 201 LDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1063 QIAELQA----------QIAELKMQLAKKEEELQAALARVEE------------EAAQKNMALKKIRE--LESQISELQE 1118
Cdd:pfam10174 273 EIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETltnqnsdckqhiEVLKESLTAKEQRAaiLQTEVDALRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1119 DLESERASRNKAEKQKRDLGEELEALKTELEDTLDstaaqqeLRSKREQEVNILKKTLE---EEAKTHEAQIQEMRqkhs 1195
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKD-------MLDVKERKINVLQKKIEnlqEQLRDKDKQLAGLK---- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1196 QAVEELAEQLEQTKRVKANLEKA----KQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTEL 1271
Cdd:pfam10174 422 ERVKSLQTDSSNTDTALTTLEEAlsekERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1272 ADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQElLQEENRQKLSLSTKLKQVEDEKNSFREQ------- 1344
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQEVARYKEEsgkaqae 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1345 -------LEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKlqKDLEGLSQRHEEKVAAYDKlektktR 1417
Cdd:pfam10174 581 verllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK--KGAQLLEEARRREDNLADN------S 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1418 LQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALsLArALEEAMEQKAELER 1497
Cdd:pfam10174 653 QQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL-LA-AISEKDANIALLEL 730
|
730 740
....*....|....*....|....*...
gi 12667788 1498 LNKQFRTEMEDLMSSKDDVGKSVHELEK 1525
Cdd:pfam10174 731 SSSKKKKTQEEVMALKREKDRLVHQLKQ 758
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1522-1923 |
5.04e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALE----QQVEEMKTQLEELEDELQATEDAKLRLevnlqamkaqfeRDLQGRDEQSEEKKKQLVRQVREMEAE 1597
Cdd:COG4717 50 RLEKEADELFkpqgRKPELNLKELKELEEELKEAEEKEEEY------------AELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1598 LE--DERKQRSMAVAARKKLEMDLKDLEAHIDSAnknrDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAK-ENEKK 1674
Cdd:COG4717 118 LEklEKLLQLLPLYQELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1675 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR-----IAQLEEELEEEQGNTELIN 1749
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1750 DRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKY------KASITALEAKIAQLEEQL 1823
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlppdlsPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1824 DNETKERQAACKQVRRTEKK--LKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQR--ANASRRKLQRE 1899
Cdd:COG4717 354 REAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEE 433
|
410 420
....*....|....*....|....
gi 12667788 1900 LEDATETADAMNREVSSLKNKLRR 1923
Cdd:COG4717 434 LEELEEELEELEEELEELREELAE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1185-1407 |
5.19e-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: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1185 AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFneg 1264
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1265 ERVRTELADKVTKLQV--ELDNVTGLLSQSDSksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1342
Cdd:COG4942 100 EAQKEELAELLRALYRlgRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1343 EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAA 1407
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
862-1512 |
8.84e-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: 57.54 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 862 LAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICH------DLEARVEEEEERCQHLQ 935
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHlhfgykSDETLIASRQEERQETS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 936 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTT-EAKLKKLEEEQIILEDQNCKLAK-----------EKKLLEDRIAE 1003
Cdd:pfam12128 286 AELNQLLRTLDDQWKEKRDELNGELSAADAAVAKdRSELEALEDQHGAFLDADIETAAadqeqlpswqsELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1004 FTTN---LTEEEEKSKSLAKLKNKHEamITDLEERL--RREEKQRQELEKT----------RRKLEGDSTDLSDQ----- 1063
Cdd:pfam12128 366 LTGKhqdVTAKYNRRRSKIKEQNNRD--IAGIKDKLakIREARDRQLAVAEddlqaleselREQLEAGKLEFNEEeyrlk 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1064 --IAELQAQIA------ELKMQLAKKEEELQAA-----LARVEEEAAQKNMALKKIR----------------ELESQIS 1114
Cdd:pfam12128 444 srLGELKLRLNqatatpELLLQLENFDERIERAreeqeAANAEVERLQSELRQARKRrdqasealrqasrrleERQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1115 ELQEDLESERAS-----RNKAEKQKRDLGEELEA---LKTELEDTLDSTAAQQE-------LRSKREQ--EVNILKKTLE 1177
Cdd:pfam12128 524 ELELQLFPQAGTllhflRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGElnlygvkLDLKRIDvpEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1178 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER---GELANEVKVLLQGKGDS--EHKRKKVEa 1252
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARldlRRLFDEKQSEKDKKNKAlaERKDSANE- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1253 QLQEL--QVKFNEG------ERVRTELADKVTKLQVELDNVTGLLsqsDSKSSKLTKDFSALESQLQDTQELLQEENRQK 1324
Cdd:pfam12128 683 RLNSLeaQLKQLDKkhqawlEEQKEQKREARTEKQAYWQVVEGAL---DAQLALLKAAIAARRSGAKAELKALETWYKRD 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1325 LslstKLKQVEDEKNSfreqleeeeeakhNLEKQIATLHAQVADMKKKMEDS----VGCLETAEEVKRKLQKDLEGLSQR 1400
Cdd:pfam12128 760 L----ASLGVDPDVIA-------------KLKREIRTLERKIERIAVRRQEVlryfDWYQETWLQRRPRLATQLSNIERA 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1401 HEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSacnLEKKQKKFDQLLAEEKTISAKYAEER-----DRAEAEAREKE 1475
Cdd:pfam12128 823 ISE-------LQQQLARLIADTKLRRAKLEMERKA---SEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERL 892
|
730 740 750
....*....|....*....|....*....|....*..
gi 12667788 1476 TKALSLARALEEAMEQkaeLERLNKQFRTEMEDLMSS 1512
Cdd:pfam12128 893 AQLEDLKLKRDYLSES---VKKYVEHFKNVIADHSGS 926
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
873-1703 |
1.20e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 873 TLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLeARVEEEEErcqhlQAEK-KKMQQNIQELEEQ 951
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL-NLVQTALR-----QQEKiERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 952 LEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQnckLAKEKKLLE--DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMI 1029
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQ---LADYQQALDvqQTRAIQYQQAVQALERAKQLCGLPDLTADNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1030 TDLEERLRREEKQR-QELEKTRRKLegdstDLSDQIAELQAQIAELKMQLAKKEEELQA------ALARVEEE---AAQK 1099
Cdd:PRK04863 441 EDWLEEFQAKEQEAtEELLSLEQKL-----SVAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvareLLRRLREQrhlAEQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1100 NMALKKIRELEsQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDStaAQQELRSKREQevnilKKTLEEE 1179
Cdd:PRK04863 516 QQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES--LSESVSEARER-----RMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1180 AKTHEAQIQEMRQKHSQ------AVEELAEQLEQTKRVKANLEKA-KQTLENERGelanevkvLLQGKGDSEHKRKKVEA 1252
Cdd:PRK04863 588 LEQLQARIQRLAARAPAwlaaqdALARLREQSGEEFEDSQDVTEYmQQLLERERE--------LTVERDELAARKQALDE 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1253 QLQEL-QVKFNEGERVRTeLADKVTKLQVEL--DNVT--------GLLSQsdSKSSKLTKDFSALESQLQDTQELLQEen 1321
Cdd:PRK04863 660 EIERLsQPGGSEDPRLNA-LAERFGGVLLSEiyDDVSledapyfsALYGP--ARHAIVVPDLSDAAEQLAGLEDCPED-- 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1322 rqklslstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATlhaqvADMKKKMEDSVGCLETAEEVKRklqkdLEGLSQRH 1401
Cdd:PRK04863 735 ---------LYLIEGDPDSFDDSVFSVEELEKAVVVKIAD-----RQWRYSRFPEVPLFGRAAREKR-----IEQLRAER 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1402 EEKVAAYDKLEKTKTRLQQelddllvdlDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSL 1481
Cdd:PRK04863 796 EELAERYATLSFDVQKLQR---------LHQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQ 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1482 ARALEEAMEQKAEL---------ERLNKQFRTEMEDLMSSKDDV------GKSVHELEKSKRAL---EQQVEEMKTQLEE 1543
Cdd:PRK04863 867 LEQAKEGLSALNRLlprlnlladETLADRVEEIREQLDEAEEAKrfvqqhGNALAQLEPIVSVLqsdPEQFEQLKQDYQQ 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1544 LEDELQATeDAKLRLEVNLQAMKAQFE-RDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDL 1622
Cdd:PRK04863 947 AQQTQRDA-KQQAFALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASL 1025
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1623 EAHIDSANKNRDEAIKQLRKLQAQMKDCMRELddTRASREEILAQAKEN-------EKKLKSMEAEMIQLQEELAAAERA 1695
Cdd:PRK04863 1026 KSSYDAKRQMLQELKQELQDLGVPADSGAEER--ARARRDELHARLSANrsrrnqlEKQLTFCEAEMDNLTKKLRKLERD 1103
|
....*...
gi 12667788 1696 KRQAQQER 1703
Cdd:PRK04863 1104 YHEMREQV 1111
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1666-1879 |
1.49e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1666 AQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDeladeIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNT 1745
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1746 ELINDRLKKANLQIDQINTDLNLershaqknenarQQLERQNKELKVKLQEMEGTVKSKYKAsITALEAKIAQLEEQLDN 1825
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVI------------QQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQ 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1826 ETKERQAAckqvrrTEKKLKDVLLQVDDERRNAEQYKDQAD---KASTRLKQLKRQL 1879
Cdd:COG3206 310 EAQRILAS------LEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREV 360
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1085-1310 |
1.64e-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: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1085 LQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSK 1164
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1165 REQEVNILKKTLEEEAKTHE-----------------AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERG 1227
Cdd:COG4942 95 LRAELEAQKEELAELLRALYrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1228 ELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSklTKDFSALE 1307
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP--AAGFAALK 252
|
...
gi 12667788 1308 SQL 1310
Cdd:COG4942 253 GKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1578-1804 |
1.74e-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: 55.54 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDT 1657
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1658 RASREEILAQAkenEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEE 1737
Cdd:COG4942 103 KEELAELLRAL---YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1738 LEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSK 1804
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
968-1219 |
2.00e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 968 TTEAKLKKLEEEQIILEDQncklAKEKKLLEDRIAEFTTNLTE-EEEKSKSLAKLKNKHEAMITDLEERLRREEK----- 1041
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEERLKELEPfyney 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1042 -----QRQELEKTRRKLEGDSTDLSDQIAELqaqiAELKMQLAKKEEELQAALARVEEEAAQKnmALKKIRELESQISEL 1116
Cdd:PRK03918 605 lelkdAEKELEREEKELKKLEEELDKAFEEL----AETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGL 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1117 QEDLESERASRNKAEKQKRDLGEELEAL---KTELEDTLDSTAAQQELRskreqevnilKKTLEEEAKTHEAQIQEMRQK 1193
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEERekaKKELEKLEKALERVEELR----------EKVKKYKALLKERALSKVGEI 748
|
250 260
....*....|....*....|....*.
gi 12667788 1194 HSQAVEELAEQLEQTKRVKANLEKAK 1219
Cdd:PRK03918 749 ASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
887-1344 |
2.07e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 887 EQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEeeesaRQKLQLEK 966
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQLLPLYQE-----LEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 967 VTTEAKLKKLEEEQIILEDqnckLAKEKKLLEDRIAEFTTNLTEEEE-----KSKSLAKLKNKHEAMITDLEERLRREEK 1041
Cdd:COG4717 142 AELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEqlslaTEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1042 QRQELEKTRRKLEGDSTDLsdQIAELQAQIAELKMQL-----------------AKKEEELQAALARVEEEAAQKNMALK 1104
Cdd:COG4717 218 AQEELEELEEELEQLENEL--EAAALEERLKEARLLLliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1105 KIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQevnilkktLEEEAKTHE 1184
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--------LEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1185 AQIQE---MRQKHSQAVEELAEQLEQTKRVKaNLEKAKQTLENERGELANEVKVLLQGKGDSEhkrkkVEAQLQELQVKF 1261
Cdd:COG4717 368 LEQEIaalLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1262 NEGERVRTELADKVTKLQVELDNVTGllsqsdskssklTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF 1341
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEE------------DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
...
gi 12667788 1342 REQ 1344
Cdd:COG4717 510 REE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1522-1720 |
2.24e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQ---FERDLQGRDEQSEEKKKQLVRQVREME--- 1595
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREELGERARALYrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1596 ---------------AELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRAS 1660
Cdd:COG3883 100 gsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1661 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1720
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1012-1134 |
2.49e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.99 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1012 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakkEEELQAALAR 1091
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 12667788 1092 VEEEAAQknmALKKIRELESQISELQ--EDLESERASRNKAEKQK 1134
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYASVkaHELIEARKRLNKANEKK 623
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
899-1287 |
2.68e-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: 55.29 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 899 AEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQqniqeleEQLEEEESARQKLQLEKVTTEAKLKKLEE 978
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE-------RQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 979 EQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST 1058
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1059 DLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKqkrdLG 1138
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG----LG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1139 EELEALKTELEDTldstaaQQELRSKREQ--EVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEqtkRVKANLE 1216
Cdd:pfam07888 258 EELSSMAAQRDRT------QAELHQARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIE---KLSAELQ 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1217 KAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQE----LQVKFNEGERVRT---ELADKVTKLQVELDNVTG 1287
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQElkasLRVAQKEKEQLQAekqELLEYIRQLEQRLETVAD 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
958-1170 |
3.20e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 958 ARQKLQlekvTTEAKLKKLEEEQIILEdqnckLAKEKKLLEDRIAEFTTNLT-------EEEEKSKSLAKLKNKHEAMIT 1030
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAearaelaEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1031 DLEE--RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAkkeEELQAALARVEEEAAQknmALKKIRE 1108
Cdd:COG3206 258 ELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12667788 1109 LESQISELQEDLESErasrNKAEKQKRDLGEELEALKTELEDTLdstAAQQELRSKREQEVN 1170
Cdd:COG3206 332 LQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVG 386
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1141-1602 |
3.26e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1141 LEALKTELEDTLDstAAQQELRSKREQEVNILKKTLEEEakthEAQIQEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQ 1220
Cdd:COG4717 40 LAFIRAMLLERLE--KEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEE-YAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1221 TLENERGELANEVKV--LLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA---DKVTKLQVELDNVTGLLSQSDSK 1295
Cdd:COG4717 113 ELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEeleAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1296 S-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKnsFREQLEEEEEAKHNLEKQIATLHAQVADMKKKME 1374
Cdd:COG4717 193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1375 DSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 1454
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1455 TISAKYAEERDRAEAEAREKETKAL-------------SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKsvH 1521
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALlaeagvedeeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--E 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEE-KKKQLVRQV-REMEAE 1597
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEwAALKLALELlEEAREE 508
|
....*
gi 12667788 1598 LEDER 1602
Cdd:COG4717 509 YREER 513
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1652-1876 |
3.39e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1652 RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEE--LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA 1729
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1730 RIAQLEEELEEEQGNTELINDRLkkanlQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASI 1809
Cdd:COG3206 248 QLGSGPDALPELLQSPVIQQLRA-----QLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1810 TALEAKIAQLEEQLDNETKERQaackQVRRTEKKLKDvlLQvdderRNAEQYKDQADKASTRLKQLK 1876
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLA----ELPELEAELRR--LE-----REVEVARELYESLLQRLEEAR 378
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
963-1345 |
4.19e-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: 54.96 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 963 QLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQ 1042
Cdd:COG5185 225 AKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1043 RQELEKTRRKLEgdstdlsdqiaelQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkiRELESQISELQEDLES 1122
Cdd:COG5185 305 IDIKKATESLEE-------------QLAAAEAEQELEESKRETETGIQNLTAEIEQGQ------ESLTENLEAIKEEIEN 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1123 ERASRNKAEKQkrdlgEELEALKTELEDTLDSTaaQQELRSKREQEVNILkKTLEEEAKTHEAQIQEMRQKHSQAVEELA 1202
Cdd:COG5185 366 IVGEVELSKSS-----EELDSFKDTIESTKESL--DEIPQNQRGYAQEIL-ATLEDTLKAADRQIEELQRQIEQATSSNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1203 EQleqtkrvkanlEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKveaqlQELQVKFNEGERVRTELADKV----TKL 1278
Cdd:COG5185 438 EV-----------SKLLNELISELNKVMREADEESQSRLEEAYDEIN-----RSVRSKKEDLNEELTQIESRVstlkATL 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12667788 1279 QVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLK-----QVEDEKNSFREQL 1345
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNaktdgQAANLRTAVIDEL 573
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1323-1888 |
4.28e-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: 55.13 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1323 QKLSLSTKLKQVEDEKN----SFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAE-------EVKRKLQ 1391
Cdd:pfam05557 3 ELIESKARLSQLQNEKKqmelEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEealreqaELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1392 KDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERD------ 1465
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQnlekqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1466 --RAEAEAREKE--------TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQvE 1535
Cdd:pfam05557 163 ssLAEAEQRIKElefeiqsqEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-E 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1536 EMKTQLEELEDELQATEdAKLRLEVNLQAMKAQFER---DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRsmavaar 1612
Cdd:pfam05557 242 KYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1613 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSME--AEMIQLQE 1687
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1688 ELAAAERAkrqaqqeRDELADEIANSSGKGALALEekRRLEARIAQLEEELeeeQGNTELINDRLKKANlqidqinTDLN 1767
Cdd:pfam05557 394 AHNEEMEA-------QLSVAEEELGGYKQQAQTLE--RELQALRQQESLAD---PSYSKEEVDSLRRKL-------ETLE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1768 LERshaqknenarQQLERQNKELKVKL--QEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLK 1845
Cdd:pfam05557 455 LER----------QRLREQKNELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE 524
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 12667788 1846 DVLLQVDderRNAEQYKDQADKastRLKQLKRQLEEAEEEAQR 1888
Cdd:pfam05557 525 DDLEQVL---RLPETTSTMNFK---EVLDLRKELESAELKNQR 561
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1628-1845 |
4.84e-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: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1628 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1707
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1708 DEIANSSGKGAL--ALEEKRRLEARIAQLEEELEEEQGNTELINDrLKKANLQIDQINTDLnlershaqknENARQQLER 1785
Cdd:COG3883 93 RALYRSGGSVSYldVLLGSESFSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAEL----------EAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1786 QNKELKVKLQEMEgTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLK 1845
Cdd:COG3883 162 LKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
932-1130 |
5.24e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 932 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEqiiLEDQNCKLAKEKKLLEDRIAEF------- 1004
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGERARALyrsggsv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1005 --------TTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKM 1076
Cdd:COG3883 103 syldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1077 QLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKA 1130
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1026-1160 |
5.31e-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: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1026 EAMITDLEERLRRE--EKQRQELEKTRRKLEGDSTDLSD------------QIAELQAQIAELKMQLAKKEEELQAALAR 1091
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12667788 1092 VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQkrdlgEELEALKTEL---EDTLDSTAAQQE 1160
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1107-1918 |
6.02e-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: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1107 RELESQISELQEDLESERASRNKAEKQKRDLGEELEALkteledtldsTAAQQELrskrEQEVNILKKTLeeeAKTHEA- 1185
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEEL----------SARESDL----EQDYQAASDHL---NLVQTAl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1186 QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGD-----SEHKRKKVEAQlQELQVK 1260
Cdd:COG3096 344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqalDVQQTRAIQYQ-QAVQAL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1261 fnEGERVRTELADkvtklqVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELlQEENRQKLSLSTKLK-QVEDEK- 1338
Cdd:COG3096 423 --EKARALCGLPD------LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAA-RRQFEKAYELVCKIAgEVERSQa 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1339 -NSFREQLEEEEEAKHNLEkQIATLHAQVADmkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTR 1417
Cdd:COG3096 494 wQTARELLRRYRSQQALAQ-RLQQLRAQLAE-----------LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1418 LQQELDDLLVDLDHQRQSACNLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLA--RALEEAMEQKAEL 1495
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQL---EQLRARIKELAARAPAWLAAQDALERLREQSGEALAdsQEVTAAMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1496 ERLNKQfrtemedlmsSKDdvgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQATEDAKLRLEVNLQ----- 1563
Cdd:COG3096 639 EREATV----------ERD-------ELAARKQALESQIERLSqpggaedPRLLALAERLGGVLLSEIYDDVTLEdapyf 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1564 ------AMKAQFERDLQGrdeqseekkkqlvrqVREMEAELEDerkqrsmavaarkkLEMDLKDLEAHIDSANKNRDEAI 1637
Cdd:COG3096 702 salygpARHAIVVPDLSA---------------VKEQLAGLED--------------CPEDLYLIEGDPDSFDDSVFDAE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1638 KQLRKLQAQMKDcmRELDDTRASREEILAQAKEnEKKLKSMEAEMIQLQEELA--AAERAK--RQAQQERDELADEIA-- 1711
Cdd:COG3096 753 ELEDAVVVKLSD--RQWRYSRFPEVPLFGRAAR-EKRLEELRAERDELAEQYAkaSFDVQKlqRLHQAFSQFVGGHLAva 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1712 -NSSGKGALAL--EEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINtdLNLERSHAQKNENARQQLErqnk 1788
Cdd:COG3096 830 fAPDPEAELAAlrQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN--LLADETLADRLEELREELD---- 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1789 elkvKLQEMEGTVKSKYKAsITALEAKIAQL------EEQLDNETKERQAACKQVRRTEKKLKDVLlqvddERRNAEQYK 1862
Cdd:COG3096 904 ----AAQEAQAFIQQHGKA-LAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRRLKQQIFALSEVV-----QRRPHFSYE 973
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 12667788 1863 D---QADKASTRLKQLKRQLEeaeeeaqRANASRRKLQRELEDATETADAMNREVSSLK 1918
Cdd:COG3096 974 DavgLLGENSDLNEKLRARLE-------QAEEARREAREQLRQAQAQYSQYNQVLASLK 1025
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1406-1918 |
6.24e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.91 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1406 AAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTIsakyAEERDRAEAEAREKETKALSLARAL 1485
Cdd:PRK01156 166 RNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSIT----LKEIERLSIEYNNAMDDYNNLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1486 EEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKR-----------------ALEQQVEEMKTQLEELEDEL 1548
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1549 QATEDAKLRLEVnLQAMKAQFERDLQGRDE---------QSEEKKKQLVRQVREMEAELEDERKQR-------------- 1605
Cdd:PRK01156 322 NKYHAIIKKLSV-LQKDYNDYIKKKSRYDDlnnqileleGYEMDYNSYLKSIESLKKKIEEYSKNIermsafiseilkiq 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1606 ----SMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMK----DCMRELDDTRASREEILAQAKENEKKLKS 1677
Cdd:PRK01156 401 eidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngQSVCPVCGTTLGEEKSNHIINHYNEKKSR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1678 MEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANL 1757
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1758 QI-DQINTDLNleRSHAQKN----ENARQQLERQNKELK---VKLQEMEGT---VKSKYKASITALEAKIAQLEEQLdNE 1826
Cdd:PRK01156 561 EDlDSKRTSWL--NALAVISlidiETNRSRSNEIKKQLNdleSRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY-NE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1827 TKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET 1906
Cdd:PRK01156 638 IQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDR 717
|
570
....*....|..
gi 12667788 1907 ADAMNREVSSLK 1918
Cdd:PRK01156 718 INDINETLESMK 729
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
874-1610 |
6.39e-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: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 874 LQSQLMAEKLQLQEQLQAETELCAE-AEELRARLTAKKQELEEICHDLEARVEEEEE-RCQHLQAekKKMQQNIQELEEQ 951
Cdd:COG3096 413 IQYQQAVQALEKARALCGLPDLTPEnAEDYLAAFRAKEQQATEEVLELEQKLSVADAaRRQFEKA--YELVCKIAGEVER 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 952 LEEEESAR--------QKLQLEKVTT-EAKLKKLEEEqiiLEDQNcklaKEKKLLEDRIAEFTTNLTEEEEksksLAKLK 1022
Cdd:COG3096 491 SQAWQTARellrryrsQQALAQRLQQlRAQLAELEQR---LRQQQ----NAERLLEEFCQRIGQQLDAAEE----LEELL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1023 NKHEAMITDLEERLRREEKQRQELektRRKLEgdstdlsdqiaELQAQIAELKmQLAKKEEELQAALARVEEEAAQknmA 1102
Cdd:COG3096 560 AELEAQLEELEEQAAEAVEQRSEL---RQQLE-----------QLRARIKELA-ARAPAWLAAQDALERLREQSGE---A 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1103 LKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALkteledTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1182
Cdd:COG3096 622 LADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL------SQPGGAEDPRLLALAERLGGVLLSEIYDDVTL 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1183 HEAQIQEMR---QKHSQAVEELAeqleqtkRVKANLEKAKQTLEN----ERGELANEVKVLlqgkgDSEHKRKKVEAQLQ 1255
Cdd:COG3096 696 EDAPYFSALygpARHAIVVPDLS-------AVKEQLAGLEDCPEDlyliEGDPDSFDDSVF-----DAEELEDAVVVKLS 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1256 ELQVKFNE-------GERVRTELADkvtKLQVELDNVTGLLSQSD---SKSSKLTKDFSALESQ------LQDTQELLQE 1319
Cdd:COG3096 764 DRQWRYSRfpevplfGRAAREKRLE---ELRAERDELAEQYAKASfdvQKLQRLHQAFSQFVGGhlavafAPDPEAELAA 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1320 ENRQklslstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGclETAEEVKRKLQKDLEGLS- 1398
Cdd:COG3096 841 LRQR-------RSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLA--DRLEELREELDAAQEAQAf 911
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1399 -QRHEEKVAaydKLEKTKTRLQQELDdllvdldhqrqsacNLEKKQKKFDQLLAEEKTISAK---YAEERDRAEAEAREK 1474
Cdd:COG3096 912 iQQHGKALA---QLEPLVAVLQSDPE--------------QFEQLQADYLQAKEQQRRLKQQifaLSEVVQRRPHFSYED 974
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1475 ETKALSLARALEEAMEQK---AELERLnkQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELedELQAT 1551
Cdd:COG3096 975 AVGLLGENSDLNEKLRARleqAEEARR--EAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL--GVQAD 1050
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1552 EDAKLRLEVNLQAMKAQFERDLQGRDE------QSEEKKKQLVRQVREMEAELEDERKQRSMAVA 1610
Cdd:COG3096 1051 AEAEERARIRRDELHEELSQNRSRRSQlekqltRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA 1115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1357-1614 |
7.43e-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: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1357 KQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQElddllvdldhqrqsa 1436
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1437 cnLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDV 1516
Cdd:COG4942 85 --LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1517 GKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAmkaqferdLQGRDEQSEEKKKQLVRQVREMEA 1596
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEALIARLEA 234
|
250
....*....|....*...
gi 12667788 1597 ELEDERKQRSMAVAARKK 1614
Cdd:COG4942 235 EAAAAAERTPAAGFAALK 252
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1025-1277 |
8.37e-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: 52.84 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1025 HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalk 1104
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1105 kirELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ--EVNILKKTLEEEAKT 1182
Cdd:pfam09787 115 ---ELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQltETLIQKQTMLEALST 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1183 heaqiqemrQKHSQAVEelaeqleqtkrvkanLEKAKQTLENERGELANEVKVLLQGKGDSEHKRkkveaqLQELQVKFN 1262
Cdd:pfam09787 192 ---------EKNSLVLQ---------------LERMEQQIKELQGEGSNGTSINMEGISDGEGTR------LRNVPGLFS 241
|
250
....*....|....*
gi 12667788 1263 EGERVRTELADKVTK 1277
Cdd:pfam09787 242 ESDSDRAGMYGKVRK 256
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1026-1867 |
8.76e-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: 54.67 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1026 EAMITDLEERLRREEKQRQELEKTRRKL-----EGDSTDLSDQIAELQAQI-AELKMQLAK-------KEEELQAALARV 1092
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQNMETATVELhlsniENKKNELLDIIVEIKKHIhGEINKDLNKiledfknKEKELSNKINDY 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1093 EEEAAQKNMALKKIRELESQISElQEDLESerasrNKAEKQKRDLGEELEALKTeledtldsTAAQQELRSKREQEVnil 1172
Cdd:TIGR01612 775 AKEKDELNKYKSKISEIKNHYND-QINIDN-----IKDEDAKQNYDKSKEYIKT--------ISIKEDEIFKIINEM--- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1173 kKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQL-EQTKRVKANLEKAKQTLE----NERGELANEVKVLLQGKGDSEHKR 1247
Cdd:TIGR01612 838 -KFMKDDFLNKVDKFINFENNCKEKIDSEHEQFaELTNKIKAEISDDKLNDYekkfNDSKSLINEINKSIEEEYQNINTL 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1248 KKVEaqlQELQVKFNEGERVRtELADKVTKLQVELDNVTGLLSQSDS---------------KSSKLTKDFS--ALESQL 1310
Cdd:TIGR01612 917 KKVD---EYIKICENTKESIE-KFHNKQNILKEILNKNIDTIKESNLieksykdkfdntlidKINELDKAFKdaSLNDYE 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1311 QDTQELLQEENRQKLSLSTklkqveDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVgcLETAEEVKRKL 1390
Cdd:TIGR01612 993 AKNNELIKYFNDLKANLGK------NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI--YNIIDEIEKEI 1064
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1391 QKDLEGLSQRHEEKV-AAYDKLEKTKTRLqqelddllvdldhqrqsacnlekKQKKFDQLLAEEktiSAKYAEERDRAea 1469
Cdd:TIGR01612 1065 GKNIELLNKEILEEAeINITNFNEIKEKL-----------------------KHYNFDDFGKEE---NIKYADEINKI-- 1116
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1470 eareketkalslaraleeameqKAELERLNKQfrtemedlmsskddVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ 1549
Cdd:TIGR01612 1117 ----------------------KDDIKNLDQK--------------IDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1550 AT---EDAKlRLEVNLQAMKAQFERDLQGRDEQseekkKQLVRQVREMEAELEDERKQRSMAVAARKKLEmdlKDLEAHI 1626
Cdd:TIGR01612 1161 KAisnDDPE-EIEKKIENIVTKIDKKKNIYDEI-----KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLG---KLFLEKI 1231
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1627 DSANKNRDEAIKQLRKLqaqmkdcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEelaaaERAKRQAQQERDEL 1706
Cdd:TIGR01612 1232 DEEKKKSEHMIKAMEAY-------IEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD-----DKDHHIISKKHDEN 1299
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1707 ADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKK-AN----LQIDQINTDLNLERSHAQKnenarq 1781
Cdd:TIGR01612 1300 ISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEiANiyniLKLNKIKKIIDEVKEYTKE------ 1373
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1782 qLERQNKELKVKLQEMEGTVKsKYKASITALEAKiAQLEEQLDNetkerqaacKQVRRTEKKLKDVLLQVDDERRNAEQY 1861
Cdd:TIGR01612 1374 -IEENNKNIKDELDKSEKLIK-KIKDDINLEECK-SKIESTLDD---------KDIDECIKKIKELKNHILSEESNIDTY 1441
|
....*.
gi 12667788 1862 KDQADK 1867
Cdd:TIGR01612 1442 FKNADE 1447
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1018-1152 |
9.80e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 53.71 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1018 LAKLKNKHEAmiTDLEERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE---EELQAALARVEE 1094
Cdd:COG2433 382 LEELIEKELP--EEEPEAEREKEHEERELTEEEEEIR----RLEEQVERLEAEVEELEAELEEKDeriERLERELSEARS 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1095 EAAQKNMALKKIRELESQISELQEDLESErasRNKAEKQKRDLGEELEALKTELEDTL 1152
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
791-1249 |
1.07e-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: 54.20 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 791 RGYLARKAFAKRQQQLTAMKVLQRNCAAYLKLRNWQWWRLFT---KVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENR 867
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQ 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 868 LTEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEICHDLEARVEEEeercQHLQAEKKKMQQNIQ 946
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEdVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD----NRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 947 ELEEQLEEEESARQKLQLEKVTTEAKLK-KLEEEQIILEDQNCklAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKh 1025
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQpEQDLQDVRLHLQQC--SQELALKLTALHALQLTLTQERVREHALSIRVLP- 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1026 eamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:TIGR00618 672 -------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQS 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1106 IRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA 1185
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1186 QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEnergELANEVKVLLQGKGDSEHKRKK 1249
Cdd:TIGR00618 825 TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----QLTQEQAKIIQLSDKLNGINQI 884
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
854-1702 |
1.12e-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: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 854 LVKVREKQLAAENRLTEMetlqsqlmAEKLQLQEQLQA--ETELCAEAEELRARLTAKKQ---------ELEEICHDLEA 922
Cdd:COG3096 294 LFGARRQLAEEQYRLVEM--------ARELEELSARESdlEQDYQAASDHLNLVQTALRQqekieryqeDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 923 R---VEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILedQNCKLAKEKklLED 999
Cdd:COG3096 366 QeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALC--GLPDLTPEN--AED 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1000 RIAEFTtnlteeeekskslAKLKNKHEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQiaelkmQLA 1079
Cdd:COG3096 442 YLAAFR-------------AKEQQATEEVL-ELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTAR------ELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1080 KKEEELQAALARVEEEAAQknmalkkIRELEsQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDStaAQQ 1159
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQ-------LAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE--LEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1160 ELRSKREQevnilKKTLEEEAKTHEAQIQEMRQKH------SQAVEELAEQLEQTKRVKANLEKAKQT-LENERGelane 1232
Cdd:COG3096 572 QAAEAVEQ-----RSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEALADSQEVTAAMQQlLERERE----- 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1233 vkvLLQGKGDSEHKRKKVEAQLQEL-QVKFNEGERVRTeLADKV--TKLQVELDNVT--------GLLsqSDSKSSKLTK 1301
Cdd:COG3096 642 ---ATVERDELAARKQALESQIERLsQPGGAEDPRLLA-LAERLggVLLSEIYDDVTledapyfsALY--GPARHAIVVP 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1302 DFSALESQLQDTQE-----LLQEENRQKLSLST-KLKQVEDE---KNSFReQLEEEEEAKHNL------EKQIATLHAQv 1366
Cdd:COG3096 716 DLSAVKEQLAGLEDcpedlYLIEGDPDSFDDSVfDAEELEDAvvvKLSDR-QWRYSRFPEVPLfgraarEKRLEELRAE- 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1367 ADmkkkmEDSVGCLETAEEVkRKLQKDLEGLSQ---RH------EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAC 1437
Cdd:COG3096 794 RD-----ELAEQYAKASFDV-QKLQRLHQAFSQfvgGHlavafaPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLD 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1438 NLEKKQKKFDQLLAEEKTISAKYAEERDRaeaEAREKetkalslaraLEEAMEQKAELERLNKQFRtEMEDLMSSKDDVG 1517
Cdd:COG3096 868 QLKEQLQLLNKLLPQANLLADETLADRLE---ELREE----------LDAAQEAQAFIQQHGKALA-QLEPLVAVLQSDP 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1518 KSVHELEKSKRALEQQVEEMKTQLEELEDELQ-----ATEDAKLRLEVN---LQAMKAQFERDLQGRdEQSEEKKKQLVR 1589
Cdd:COG3096 934 EQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLGENsdlNEKLRARLEQAEEAR-REAREQLRQAQA 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1590 QVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRdeAIKQLRKLQAQmkdcmreLDDTRASREEIlaqak 1669
Cdd:COG3096 1013 QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEER--ARIRRDELHEE-------LSQNRSRRSQL----- 1078
|
890 900 910
....*....|....*....|....*....|...
gi 12667788 1670 enEKKLKSMEAEMIQLQEELAAAERAKRQAQQE 1702
Cdd:COG3096 1079 --EKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1065-1340 |
1.13e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1065 AELQAQIAELKMQlaKKEEELQAALARVEEEAAQknmALKKIRELESQISELQEDLEserasrnKAEKQKRDLGEELEAL 1144
Cdd:PRK11281 39 ADVQAQLDALNKQ--KLLEAEDKLVQQDLEQTLA---LLDKIDRQKEETEQLKQQLA-------QAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1145 KTELEDTLDSTAAQQELRskreqevnilkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN 1224
Cdd:PRK11281 107 KDDNDEETRETLSTLSLR------------QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1225 ERGELANevkVLLQGKGDSEHKRKKVEAQLQ--ELQVKFNegervRTELADKvTKLQvELDNvtgllSQSDSKSSKLTKd 1302
Cdd:PRK11281 175 IRNLLKG---GKVGGKALRPSQRVLLQAEQAllNAQNDLQ-----RKSLEGN-TQLQ-DLLQ-----KQRDYLTARIQR- 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 12667788 1303 fsaLESQLQDTQELLqeeNRQKLSLSTklKQVEDEKNS 1340
Cdd:PRK11281 239 ---LEHQLQLLQEAI---NSKRLTLSE--KTVQEAQSQ 268
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1000-1324 |
1.14e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.75 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1000 RIAEFTTNLTEEEEKSKSLAKLKNkheAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA 1079
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSD---FQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1080 KKEEELQAalarveeeAAQKNMalkKIRELESQISELQEDLESERASRNKAEKQkrdLGEELEALKTE---LEDtlDSTA 1156
Cdd:PLN02939 181 ETDARIKL--------AAQEKI---HVEILEEQLEKLRNELLIRGATEGLCVHS---LSKELDVLKEEnmlLKD--DIQF 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1157 AQQELRSKREQEVNILKktLEEEAKTHEAQIQEMRQKHSQAVEELAEQleQTKRVKANLEKAkQTLENERGELANEVK-- 1234
Cdd:PLN02939 245 LKAELIEVAETEERVFK--LEKERSLLDASLRELESKFIVAQEDVSKL--SPLQYDCWWEKV-ENLQDLLDRATNQVEka 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1235 -VLLQGKGDSEHKRKKVEAQLQELQV-KFNegervrtelADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQD 1312
Cdd:PLN02939 320 aLVLDQNQDLRDKVDKLEASLKEANVsKFS---------SYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
330
....*....|..
gi 12667788 1313 TQELLQEENRQK 1324
Cdd:PLN02939 391 TLSKLKEESKKR 402
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
897-1503 |
1.37e-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: 53.59 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 897 AEAEELRARLTAKKQELE--EICH-----DLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKlQLEkvtt 969
Cdd:pfam05557 2 AELIESKARLSQLQNEKKqmELEHkrariELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALRE-QAE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 970 EAKLKKLEEEQIiledqnCKLAKEKKLLEDRIAEFTTNLTEEeeksksLAKLknKHEAMITDLEERLRREEKQ--RQELE 1047
Cdd:pfam05557 77 LNRLKKKYLEAL------NKKLNEKESQLADAREVISCLKNE------LSEL--RRQIQRAELELQSTNSELEelQERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1048 KTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKEEelqaaLARVEEEAAQKNMALKKIRELESQISELQEDLESERASR 1127
Cdd:pfam05557 143 LLKAKA----SEAEQLRQNLEKQQSSLAEAEQRIKE-----LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1128 NKAEKQKRD---LGEELEALKTELEDTLDSTAAQQELRSKREQevniLKKTLEEEAKTHEAQIQEMRQKhsqavEELAEQ 1204
Cdd:pfam05557 214 KHLNENIENkllLKEEVEDLKRKLEREEKYREEAATLELEKEK----LEQELQSWVKLAQDTGLNLRSP-----EDLSRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1205 LEQTKRVKANLEKAKQTLENERGELANEVKVLlqgkgdsEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDN 1284
Cdd:pfam05557 285 IEQLQQREIVLKEENSSLTSSARQLEKARREL-------EQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1285 VTGLLSQSDSK------SSKLTKDFSALESQLQDTQELLQEenrqklsLSTKLKQVEDEKNSFREQLEEeeeakhnLEKQ 1358
Cdd:pfam05557 358 YRAILESYDKEltmsnySPQLLERIEEAEDMTQKMQAHNEE-------MEAQLSVAEEELGGYKQQAQT-------LERE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1359 IATLHAQVAdmkkkMEDSVGCLETAEEVKRKLQkDLEGLSQRHEEKVAAYDkLEKTKTRLQQELDDLLVDLDHQRQSACN 1438
Cdd:pfam05557 424 LQALRQQES-----LADPSYSKEEVDSLRRKLE-TLELERQRLREQKNELE-MELERRCLQGDYDPKKTKVLHLSMNPAA 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1439 LEKKQKK--FDQLLAEEKTISAKYAEERDRAEAEAREKETkalSLARALEEAMEQKAELERLNKQFR 1503
Cdd:pfam05557 497 EAYQQRKnqLEKLQAEIERLKRLLKKLEDDLEQVLRLPET---TSTMNFKEVLDLRKELESAELKNQ 560
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1268-1497 |
1.40e-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: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1268 RTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEE 1347
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1348 EeeaKHNLEKQIATLHaqvadmKKKMEDSVGCLETAEEVKRkLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLV 1427
Cdd:COG4942 102 Q---KEELAELLRALY------RLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1428 DLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELER 1497
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1522-1743 |
1.42e-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: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQSEEKKKQLVRQVREMEAELEDE 1601
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1602 RKQ-RSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1680
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLLSPEDFL----DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12667788 1681 EMIQLQEELAAAERAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQLEEELEEEQG 1743
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLE--------------KELAELAAELAELQQEAEELEA 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1635-1929 |
1.47e-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: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1635 EAIKQLRKLQAQMKDCMR---ELDDTRASREeILAQAKENEKKLKSMEAEMIQLQEELAAAERAkrQAQQERDELADEIA 1711
Cdd:COG4913 222 DTFEAADALVEHFDDLERaheALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1712 NssgkgalALEEKRRLEARIAQLEeeleeeqgntelinDRLKKANLQIDQintdlnLERSHAQKNENARQQLERQNKELK 1791
Cdd:COG4913 299 E-------LRAELARLEAELERLE--------------ARLDALREELDE------LEAQIRGNGGDRLEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1792 VKLQEMEGTVKskykasitALEAKIAQLEEQLDNETKERQAACKQVRRtekklkdvllQVDDERRNAEQYKDQADKASTR 1871
Cdd:COG4913 352 RELEERERRRA--------RLEALLAALGLPLPASAEEFAALRAEAAA----------LLEALEEELEALEEALAEAEAA 413
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1872 LKQLKRQLEEAEEEAQRANASRRKLQRELEDATetaDAMNREVsslknKLRRGDLPFV 1929
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRKSNIPARLLALR---DALAEAL-----GLDEAELPFV 463
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
802-1413 |
1.55e-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: 53.51 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 802 RQQQLTAMKVLQRNCAAYLKLRNWqwwRLFTKVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEME---TLQSQL 878
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKE---ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknsLTETLK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 879 MAEKLQLQEQLQAETELCAEAEELRAR------------LTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQ 946
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLH 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 947 ELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLakEKKLLE----DRIAEFTTNLTEEEEKSKS----L 1018
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY--EDKLFDvcgsQDEESDLERLKEEIEKSSKqramL 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1019 AKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQ 1098
Cdd:TIGR00606 659 AGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1099 KNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQEVNILKKTLEE 1178
Cdd:TIGR00606 739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV---TIMERFQMELKDVERKIAQQAAKL 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1179 EAKTHEAQIQEMRQKHSQAVEEL---AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQ 1255
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELdtvVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST 895
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1256 ELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQE-ENRQKLSLSTKLKQV 1334
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQK 975
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1335 EDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK---MEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKV----AA 1407
Cdd:TIGR00606 976 ETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQerwLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVlqmkQE 1055
|
....*.
gi 12667788 1408 YDKLEK 1413
Cdd:TIGR00606 1056 HQKLEE 1061
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
993-1218 |
1.62e-06 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 53.40 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 993 EKKLLEDRiaeftTNLTEEEEKSKSLAklknkhEAMITDLEERLRREEKQRQELEKTRR-----------KLEGDSTDLs 1061
Cdd:PLN03188 1046 EKKLEQER-----LRWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRcaeelkeamqmAMEGHARML- 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1062 DQIAELQaqiaELKMQLAKKEEELQAALARVEEEAAQ---KNMALKKIRELESQISELQedleSERasrnkaEKQKRDLG 1138
Cdd:PLN03188 1114 EQYADLE----EKHIQLLARHRRIQEGIDDVKKAAARagvRGAESKFINALAAEISALK----VER------EKERRYLR 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1139 EELEALKTELEDTLDSTAAQQEL--RSKREQEVNIL--KKTLEEEAKTHEA--QIQEMRQKHSQAVEELAEQLEQTKRVK 1212
Cdd:PLN03188 1180 DENKSLQAQLRDTAEAVQAAGELlvRLKEAEEALTVaqKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPK 1259
|
....*.
gi 12667788 1213 ANLEKA 1218
Cdd:PLN03188 1260 EAIRPA 1265
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1381-1910 |
1.75e-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: 53.19 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1381 ETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKY 1460
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1461 AEERDRAEAEAREKETKALSLARALE------EAMEQKAELERLNKQFR--TEMEDLMSSKDDVGKSVHELEKSKRALEQ 1532
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEkmilafEELRVQAENARLEMHFKlkEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1533 QVEEMKTQLEELEDELQATEDAKLRLEvnlqamkaqferdlqGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAAR 1612
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLE---------------EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1613 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE----NEKKLKSMEAEMIQLQEE 1688
Cdd:pfam05483 313 KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1689 LAAAERAKRQAQQERDEL--------------------ADEIANSSGKGALALEEKRR----LEARI-----AQLEEELE 1739
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELkkilaedeklldekkqfekiAEELKGKEQELIFLLQAREKeihdLEIQLtaiktSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1740 EEQGNTELINDRLKKANL------------QIDQINTDLNLE-RSHAQKNENARQQLERQNKELKvKLQEMEGTVKSKYK 1806
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELtahcdklllenkELTQEASDMTLElKKHQEDIINCKKQEERMLKQIE-NLEEKEMNLRDELE 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1807 ASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEA 1886
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
570 580
....*....|....*....|....
gi 12667788 1887 QRANASRRKLQRELEDATETADAM 1910
Cdd:pfam05483 632 NAYEIKVNKLELELASAKQKFEEI 655
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1432-1800 |
1.86e-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: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1432 QRQSACNLEKKQKKFDqllaeektisaKYAEERDRAEAEAREKEtkalslaraleeaMEQKAELERLNKQFRTEMEDlms 1511
Cdd:pfam17380 279 QHQKAVSERQQQEKFE-----------KMEQERLRQEKEEKARE-------------VERRRKLEEAEKARQAEMDR--- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1512 skddvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLrlevnlqAMKAQFERDLQgRDEQSEEKKKQLVRQv 1591
Cdd:pfam17380 332 ------QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEI-------AMEISRMRELE-RLQMERQQKNERVRQ- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1592 remeaELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN 1671
Cdd:pfam17380 397 -----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1672 EKKLKSmeaemiqlqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRR-LEARIAQLEEELEEEQGNTELIND 1750
Cdd:pfam17380 472 RKRKKL----------ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1751 RLKKANL----QIDQINTDLNLERSHAQKNENARQQLeRQNKELKVKLQEMEGT 1800
Cdd:pfam17380 542 RRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1009-1225 |
2.11e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1009 TEEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA 1088
Cdd:COG3883 16 PQIQAKQKELSELQAE----LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1089 LARVEE------------------EAAQKNMALKKIRELESQ-ISELQEDLESERASRNKAEKQKrdlgEELEALKTELE 1149
Cdd:COG3883 92 ARALYRsggsvsyldvllgsesfsDFLDRLSALSKIADADADlLEELKADKAELEAKKAELEAKL----AELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1150 DTLDSTAAQQElrskreqEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENE 1225
Cdd:COG3883 168 AAKAELEAQQA-------EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1658-1923 |
2.46e-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: 52.76 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1658 RASREEiLAQAKENEKKLKSMEAEMIQ----LQEELAAAERAKRQAQQERDELADEIANSSGKgalALEEKRRLEARIAQ 1733
Cdd:TIGR02169 173 EKALEE-LEEVEENIERLDLIIDEKRQqlerLRREREKAERYQALLKEKREYEGYELLKEKEA---LERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1734 LEEELEEEQGNTELINDRLKKANLQIDQINTDLNlershaQKNENARQQLERQNKELKvklqemegtvkskykASITALE 1813
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIK------DLGEEEQLRVKEKIGELE---------------AEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1814 AKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASR 1893
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270
....*....|....*....|....*....|
gi 12667788 1894 RKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
860-1559 |
2.67e-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: 52.45 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 860 KQLAAENRLTEMETLQSQ--LMAEKLQLQEQLQAETELCAEAEELRARLTAKkqelEEICHDLEARVEEEEERCQHLQAE 937
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKmrLEAQAMELDALAVAEKAGQAEAEGLRAALAGA----EMVRKNLEEGSQRELEEIQRLHQE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 938 kkkmQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQncklaKEKKLLEDRIAEfttnLTEEEEKSKS 1017
Cdd:pfam07111 152 ----QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQ-----KEAELLRKQLSK----TQEELEAQVT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQ---AALARVEE 1094
Cdd:pfam07111 219 LVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTrkiQPSDSLEP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1095 EAAQKNMALkkIRELESQISELQEDLESERASRNKAEKQKRDLGEELealkteledtldstaaqQELRSKREQEVNILKK 1174
Cdd:pfam07111 299 EFPKKCRSL--LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL-----------------QEQVTSQSQEQAILQR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1175 TLEEeaKTHEAQIQEMRQKHSQAveELAEQLEQTKRVKANLEKAKQTLENERGELanevkvllqgkgdsehkrKKVEAQL 1254
Cdd:pfam07111 360 ALQD--KAAEVEVERMSAKGLQM--ELSRAQEARRRQQQQTASAEEQLKFVVNAM------------------SSTQIWL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1255 QELQVKFNEGERVRTELADKVTKLQVELDNVTGL------LSQSDSKSSKLTKDFSALESQLQ-DTQELLQEENRQKLSL 1327
Cdd:pfam07111 418 ETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLmarkvaLAQLRQESCPPPPPAPPVDADLSlELEQLREERNRLDAEL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1328 STKLKQVEDEKNSFREQ----LEEEEEAKHNLEKQIATLHAQVADMKKKMEDSV-GCLETAEE---VKRKLQKDLEGLSQ 1399
Cdd:pfam07111 498 QLSAHLIQQEVGRAREQgeaeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARqGQQESTEEaasLRQELTQQQEIYGQ 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1400 RHEEKVAaydkleKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISakyaEERDRAEAEAREKEtkAL 1479
Cdd:pfam07111 578 ALQEKVA------EVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERN----QELRRLQDEARKEE--GQ 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1480 SLARALEE----------AMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV---EEMKTQLEELED 1546
Cdd:pfam07111 646 RLARRVQElerdknlmlaTLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPIPAAVptrESIKGSLTVLLD 725
|
730
....*....|...
gi 12667788 1547 ELQATEDAKLRLE 1559
Cdd:pfam07111 726 NLQGLSEAISREE 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
858-1099 |
2.90e-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: 51.69 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 858 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcaeaEELRARLTAKKQELeeicHDLEARVEEEEERCQHLQAE 937
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQL----------AALERRIAALARRI----RALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 938 KKKMQQNIqeleeqleeeesARQKLQLEKVTTEA-KLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEE-EEKS 1015
Cdd:COG4942 92 IAELRAEL------------EAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEElRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1016 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEE 1095
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAE 235
|
....
gi 12667788 1096 AAQK 1099
Cdd:COG4942 236 AAAA 239
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1199-1821 |
2.99e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1199 EELAEQLEQTKRVKANLEKAKQTLENERGELAN--EVKVLLQGKGDS-EHKRKKVEAQLQELQVKFNEGERVRTELADKV 1275
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNidYLEEKLKSSNLElENIKKQIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1276 TKLQVELDNVTGLLSQSDSKSsKLTKDFSALESQLQdtqeLLQEENRQKLSLSTKLKQVEDEKnsfreqleeeEEAKHNL 1355
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKN-RYESEIKTAESDLS----MELEKNNYYKELEERHMKIINDP----------VYKNRNY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1356 EKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQkDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDhqrqs 1435
Cdd:PRK01156 297 INDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLK----- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1436 acNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAreketkalslaralEEAMEQKAELERLNKQFRTEMEDLMSSKDD 1515
Cdd:PRK01156 371 --SIESLKKKIEEYSKNIERMSAFISEILKIQEIDP--------------DAIKKELNEINVKLQDISSKVSSLNQRIRA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1516 VGKSVHELEKSKRALEQQ----VEEMKTQLEELEDELQATEDAKLRLEVNLQamkaQFERDLQGRDEQSEEKKKQLVRQV 1591
Cdd:PRK01156 435 LRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIR----EIEIEVKDIDEKIVDLKKRKEYLE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1592 REMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRE-------------LDDTR 1658
Cdd:PRK01156 511 SEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYE----EIKNRYKSLKLEDLDSKRTswlnalavislidIETNR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1659 ASREEILAQAKENEKKLKSMEAEMiqlqeelaaaERAKRQAQQERDELADEIANSSGKGALALEEKRRLEaRIAQLEEEL 1738
Cdd:PRK01156 587 SRSNEIKKQLNDLESRLQEIEIGF----------PDDKSYIDKSIREIENEANNLNNKYNEIQENKILIE-KLRGKIDNY 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1739 EEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYK--ASITALEAKI 1816
Cdd:PRK01156 656 KKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINEtlESMKKIKKAI 735
|
....*
gi 12667788 1817 AQLEE 1821
Cdd:PRK01156 736 GDLKR 740
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
918-1921 |
3.04e-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: 52.75 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 918 HDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlEKVTTEAK----LKKLEEEQIILEDQNCKLAKE 993
Cdd:TIGR01612 561 HEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELK-EKIKNISDkneyIKKAIDLKKIIENNNAYIDEL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 994 KKLLEDRIAEFTTNL-----TEEEEKSK----SLAKLKN--------------KHEAMITDLEERLRREEKQRQELEKTR 1050
Cdd:TIGR01612 640 AKISPYQVPEHLKNKdkiysTIKSELSKiyedDIDALYNelssivkenaidntEDKAKLDDLKSKIDKEYDKIQNMETAT 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1051 RKL-----EGDSTDLSDQIAELQAQI-AELKMQLAK-------KEEELQAALARVEEEAAQKNMALKKIRELESQISElQ 1117
Cdd:TIGR01612 720 VELhlsniENKKNELLDIIVEIKKHIhGEINKDLNKiledfknKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND-Q 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1118 EDLESerasrNKAEKQKRDLGEELEALKTeledtldsTAAQQELRSKREQEVnilkKTLEEEAKTHEAQIQEMRQKHSQA 1197
Cdd:TIGR01612 799 INIDN-----IKDEDAKQNYDKSKEYIKT--------ISIKEDEIFKIINEM----KFMKDDFLNKVDKFINFENNCKEK 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1198 VEELAEQL-EQTKRVKANLEKAKQTLE----NERGELANEVKVLLQGKGDSEHKRKKVEaqlQELQVKFNEGERVRtELA 1272
Cdd:TIGR01612 862 IDSEHEQFaELTNKIKAEISDDKLNDYekkfNDSKSLINEINKSIEEEYQNINTLKKVD---EYIKICENTKESIE-KFH 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1273 DKVTKLQVELDNVTGLLSQSDS---------------KSSKLTKDFS--ALESQLQDTQELLQEENRQKLSLSTklkqve 1335
Cdd:TIGR01612 938 NKQNILKEILNKNIDTIKESNLieksykdkfdntlidKINELDKAFKdaSLNDYEAKNNELIKYFNDLKANLGK------ 1011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1336 DEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVgcLETAEEVKRKLQKDLEGLSQRHEEKV-AAYDKLEKT 1414
Cdd:TIGR01612 1012 NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI--YNIIDEIEKEIGKNIELLNKEILEEAeINITNFNEI 1089
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1415 KTRLqqelddllvdldhqrqsacnlekKQKKFDQLLAEEktiSAKYAEERDRAEAEAREKETKALSLARALEEAmeqKAE 1494
Cdd:TIGR01612 1090 KEKL-----------------------KHYNFDDFGKEE---NIKYADEINKIKDDIKNLDQKIDHHIKALEEI---KKK 1140
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1495 LERLNKQFRTEMEDLMSSKDDV--GKSVHELEKSKRALEQQVEEMKTQLEELE---DELQATEDAKLRLEvNLQAMKAQF 1569
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDVADKAisNDDPEEIEKKIENIVTKIDKKKNIYDEIKkllNEIAEIEKDKTSLE-EVKGINLSY 1219
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1570 ERDLQGRD-EQSEEKKKQLVRQVREMEAELE--DERKQRSMAVAARKKLEMDLK------------DLEAHIDSanKNRD 1634
Cdd:TIGR01612 1220 GKNLGKLFlEKIDEEKKKSEHMIKAMEAYIEdlDEIKEKSPEIENEMGIEMDIKaemetfnishddDKDHHIIS--KKHD 1297
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1635 EAIKQLRKLQAQM-KDCMRE--LDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAEraKRQAQQERDELADEIA 1711
Cdd:TIGR01612 1298 ENISDIREKSLKIiEDFSEEsdINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNK--IKKIIDEVKEYTKEIE 1375
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1712 NSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDrlKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELK 1791
Cdd:TIGR01612 1376 ENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDD--KDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVL 1453
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1792 VKLQEMEGT-------VKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKlKDVLLQVDDE---------- 1854
Cdd:TIGR01612 1454 LLFKNIEMAdnksqhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELFEQYKKDvtellnkysa 1532
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1855 ---RRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1921
Cdd:TIGR01612 1533 laiKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSL 1602
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
859-1320 |
3.55e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.50 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 859 EKQLAAENR--------LTEMETLQSQLMAEKLQLQEQLQAET---------ELCAEAEELR----------ARLTAKKQ 911
Cdd:PRK10246 232 EKQLLTAQQqqqqslnwLTRLDELQQEASRRQQALQQALAAEEkaqpqlaalSLAQPARQLRphweriqeqsAALAHTRQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 912 ELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlEKVTTEAKLKKLEEEQIILEDQNCKLA 991
Cdd:PRK10246 312 QIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNN-ELAGWRAQFSQQTSDREQLRQWQQQLT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 992 KEKKLLeDRIAEFTTNLTeEEEKSKSLAKLKNKHEamitdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQI 1071
Cdd:PRK10246 391 HAEQKL-NALPAITLTLT-ADEVAAALAQHAEQRP-----LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1072 AELKMQLAKKEEELQAALARVEEEAaqknmalkKIRELESQISELQE---------------------DLESERASRNKA 1130
Cdd:PRK10246 464 NEMRQRYKEKTQQLADVKTICEQEA--------RIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLDAL 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1131 EKQKRDLGEE-------LEALKTEL---EDTLDSTAAQQELRSKREQEV----NILKKTLEE------EAKTHEAQIQEM 1190
Cdd:PRK10246 536 EKEVKKLGEEgaalrgqLDALTKQLqrdESEAQSLRQEEQALTQQWQAVcaslNITLQPQDDiqpwldAQEEHERQLRLL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1191 RQKHS-QAveELAEQLEQTKRVKANLEKAKQTLENERGELAnevkVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRT 1269
Cdd:PRK10246 616 SQRHElQG--QIAAHNQQIIQYQQQIEQRQQQLLTALAGYA----LTLPQEDEEASWLATRQQEAQSWQQRQNELTALQN 689
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12667788 1270 ELAdkvtklqvELDNVTGLLSQSDSKSS-----------KLTKDFSALESQLQDTQELLQEE 1320
Cdd:PRK10246 690 RIQ--------QLTPLLETLPQSDDLPHseetvaldnwrQVHEQCLSLHSQLQTLQQQDVLE 743
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1466-1879 |
3.68e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1466 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 1521
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDleqdyqaasdhlnlvqtalrqqekIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1587
Cdd:PRK04863 356 DLEELEERLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQQTRAIQYQQAvQALERAKQLcglpdl 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1588 -VRQVREMEAELEDERKQrsmAVAARKKLEMDLKDLEAhidsANKNRDEAIKQLRKLQAQMkdcmrelddtraSREEILA 1666
Cdd:PRK04863 436 tADNAEDWLEEFQAKEQE---ATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEV------------SRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1667 QAKENEKKLKSMEAEMIQLQE---ELAAAERAKRQaQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEeleeeqg 1743
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQlrmRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE------- 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1744 ntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKVKLQEMEgtvkSKYKASITALEAkIAQLEEQL 1823
Cdd:PRK04863 569 ---------------------SLSESVSEARER---RMALRQQLEQLQARIQRLA----ARAPAWLAAQDA-LARLREQS 619
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12667788 1824 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKAS-------TRLKQLKRQL 1879
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSqpggsedPRLNALAERF 682
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
962-1181 |
3.91e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.21 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 962 LQLEKVTTEAKLKKLEEEQI---ILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEE--KSKSLAkLKNKHEAM------IT 1030
Cdd:PLN02939 175 LEMRLSETDARIKLAAQEKIhveILEEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1031 DLEERLRREEKQRQELEKTRRKLEgdSTDLSDQiaELQAQIAELKMQ-LAKKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:PLN02939 254 ETEERVFKLEKERSLLDASLRELE--SKFIVAQ--EDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDL 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12667788 1110 ESQISELQEDLESERASRNKAEKQKRdLGEELEALKTELEDTLDSTAAQQELRSKREQEV-NILKKTLEEEAK 1181
Cdd:PLN02939 330 RDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFqDTLSKLKEESKK 401
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1044-1362 |
4.54e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.84 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1044 QELEKTRRKLegdstdlsDQIAELQAQIAELKMQLAKKEEELQ------AALARVEEEAAQKNMALKKIRELESQISELQ 1117
Cdd:PRK11281 63 QDLEQTLALL--------DKIDRQKEETEQLKQQLAQAPAKLRqaqaelEALKDDNDEETRETLSTLSLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1118 EDLESERASRNKAEKQkrdlgeeLEALKTELEDtldstaAQQEL--RSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHS 1195
Cdd:PRK11281 135 DQLQNAQNDLAEYNSQ-------LVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1196 QAVEELAEQLEQTKRVKANLekakQTLENERGELANEvkvllqgkgdsehKRKKVEAQLQELQVKFNEGERVRTElaDKV 1275
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNTQL----QDLLQKQRDYLTA-------------RIQRLEHQLQLLQEAINSKRLTLSE--KTV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1276 TKLQveldnvtgllsqsdsksskltkdfSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF-------REQLEEE 1348
Cdd:PRK11281 263 QEAQ------------------------SQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLtqqnlrvKNWLDRL 318
|
330
....*....|....
gi 12667788 1349 EEAKHNLEKQIATL 1362
Cdd:PRK11281 319 TQSERNIKEQISVL 332
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1148-1923 |
5.15e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1148 LEDTLDSTAAQQELRSKREQEVNILKKTLEEEAkTHEAQIQEMRQKHSQAVEELA------EQLEQTKRVKANLEKAkqt 1221
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELA-ELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEEL--- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1222 leNERGELANEVKVLLQGKGDsEHKRKKVEAQLqelqvkfnEGERVRTELADKVTKLQVE-------------LDNVTGL 1288
Cdd:PRK04863 361 --EERLEEQNEVVEEADEQQE-ENEARAEAAEE--------EVDELKSQLADYQQALDVQqtraiqyqqavqaLERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1289 LSQSDSKSSKLTKDFSALESQLQD-TQELLQEEnrQKLSLSTKLKQV-----------------EDEKNSFREQLEEEEE 1350
Cdd:PRK04863 430 CGLPDLTADNAEDWLEEFQAKEQEaTEELLSLE--QKLSVAQAAHSQfeqayqlvrkiagevsrSEAWDVARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1351 AKHnLEKQIATLHAQVADMKKKMEDsvgcletaeevKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLD 1430
Cdd:PRK04863 508 QRH-LAEQLQQLRMRLSELEQRLRQ-----------QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1431 HQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAeAREKETKALSLARALEEAMEQKAELERlnkQFRTEMEdlm 1510
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR-LREQSGEEFEDSQDVTEYMQQLLERER---ELTVERD--- 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1511 sskddvgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQATEDAKLRLEVNLQ-----------AMKAQFERD 1572
Cdd:PRK04863 649 -----------ELAARKQALDEEIERLSqpggsedPRLNALAERFGGVLLSEIYDDVSLEdapyfsalygpARHAIVVPD 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1573 LQGrdeqseekkkqlvrqVREMEAELEDerkqrsmavaarkkLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDcmR 1652
Cdd:PRK04863 718 LSD---------------AAEQLAGLED--------------CPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--R 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1653 ELddtRASR--EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgALALE-----EKR 1725
Cdd:PRK04863 767 QW---RYSRfpEVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHL---AVAFEadpeaELR 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1726 RLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQIN-----TDLNLERSHAQKNENARQQLERqnkelkvkLQEMEGT 1800
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprLNLLADETLADRVEEIREQLDE--------AEEAKRF 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1801 VKsKYKASITALEAKIAQL---EEQLDNETKERQAAcKQVRRTEKKLKDVLLQVDdERRNAEQYKDQAD---KASTRLKQ 1874
Cdd:PRK04863 913 VQ-QHGNALAQLEPIVSVLqsdPEQFEQLKQDYQQA-QQTQRDAKQQAFALTEVV-QRRAHFSYEDAAEmlaKNSDLNEK 989
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 12667788 1875 LKRQLEeaeeeaqRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:PRK04863 990 LRQRLE-------QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
993-1288 |
5.21e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.38 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 993 EKKL--LEDRIAEFTTnLTEE---EEKSKSLAKLKNKheamITDLEERLRREEKQRQELEktrrklegdsTDLSDQIAEL 1067
Cdd:PRK04778 171 EKQLenLEEEFSQFVE-LTESgdyVEAREILDQLEEE----LAALEQIMEEIPELLKELQ----------TELPDQLQEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1068 QAQIAELKMQ--------LAKKEEELQAALARVEEEAAQKNM--ALKKIRELESQISELQEDLESERASRNKAEKQKRDL 1137
Cdd:PRK04778 236 KAGYRELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDLdeAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1138 GEELEALKTELEDTldstaaQQELRskREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEK 1217
Cdd:PRK04778 316 PDFLEHAKEQNKEL------KEEID--RVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEE 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1218 AKQTL---ENERGELANEVKVLlqgkgdsehkrKKVEAQLQElqvkfnEGERVRTELADkvTKLQVELDNVTGL 1288
Cdd:PRK04778 388 ILKQLeeiEKEQEKLSEMLQGL-----------RKDELEARE------KLERYRNKLHE--IKRYLEKSNLPGL 442
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1456-1657 |
5.75e-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: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1456 ISAKYAEERDRAEAEAREkeTKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkddvgksvhELEKSKRALEQQVE 1535
Cdd:COG2433 355 VEKKVPPDVDRDEVKARV--IRGLSIEEALEELIEKELPEEEPEAEREKEHEERELT---------EEEEEIRRLEEQVE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1536 EMKTQLEELEDELQATEDAKLRLEvnlqaMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsmavaARKKL 1615
Cdd:COG2433 424 RLEAEVEELEAELEEKDERIERLE-----RELSEARSEERREIRKDREISRLDREIERLERELEEERE-------RIEEL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 12667788 1616 EMDLKDLEAHIDSANKNRDEAIKQLRKLQaqmKDCMRELDDT 1657
Cdd:COG2433 492 KRKLERLKELWKLEHSGELVPVKVVEKFT---KEAIRRLEEE 530
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1462-1704 |
5.93e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1462 EERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1541
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1542 EELEDELQATEDAKLRLEvNLQAMKAQFERDLQGRDeQSEEKKKQLVRQVREMEAELEDERKQRsmavaarkKLEMDLKD 1621
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKAL--------EKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1622 LEAHIDSANKNRDEAIKQLRKLQ-------AQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL----- 1689
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELrelrk 244
|
250 260
....*....|....*....|....
gi 12667788 1690 ---------AAAERAKRQAQQERD 1704
Cdd:COG1340 245 elkklrkkqRALKREKEKEELEEK 268
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1009-1269 |
6.07e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1009 TEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAA 1088
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLR-------EELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1089 LARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQE 1168
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1169 VNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK 1248
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260
....*....|....*....|.
gi 12667788 1249 KVEAQLQELQVKFNEGERVRT 1269
Cdd:COG4372 239 LDALELEEDKEELLEEVILKE 259
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
991-1733 |
7.61e-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: 7.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 991 AKEKKLLEDRIAEFTTNLTEEEEKsksLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQ--IAELQ 1068
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQ---LAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQekIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESE-------RASRNKAEKQKR------ 1135
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyQQAVQALEKARAlcglpd 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1136 ----DLGEELEALKTElEDTLDST---------------------------------------AAQQELRSKREQevnil 1172
Cdd:COG3096 434 ltpeNAEDYLAAFRAK-EQQATEEvleleqklsvadaarrqfekayelvckiageversqawqTARELLRRYRSQ----- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1173 kKTLEEEAKTHEAQIQEMRQKHS--QAVEELAEQLEQTKRVK----ANLEKAKQTLENERGELANEVKVLLQGKGDSEHK 1246
Cdd:COG3096 508 -QALAQRLQQLRAQLAELEQRLRqqQNAERLLEEFCQRIGQQldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1247 RKKVEAQLQELQVKfnegERVRTELADKVTKLQ----VELDNVTGLLSQSDSKSSKLTKdFSALESQLQDTQELLQEENR 1322
Cdd:COG3096 587 LEQLRARIKELAAR----APAWLAAQDALERLReqsgEALADSQEVTAAMQQLLERERE-ATVERDELAARKQALESQIE 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1323 QKL----SLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATL----HAQVAD----MKKKMEDSVGCLETAEEVKRKL 1390
Cdd:COG3096 662 RLSqpggAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYFSALYgparHAIVVPdlsaVKEQLAGLEDCPEDLYLIEGDP 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1391 QKDLEGLSQRHEEKVAAYDKLEKTKTRlqqelddllvdldHQRQSACNL---EKKQKKFDQLLAEEKTISAKYAEER--- 1464
Cdd:COG3096 742 DSFDDSVFDAEELEDAVVVKLSDRQWR-------------YSRFPEVPLfgrAAREKRLEELRAERDELAEQYAKASfdv 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1465 ---DRAEAEAREKETKALSLA------RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEK--------SK 1527
Cdd:COG3096 809 qklQRLHQAFSQFVGGHLAVAfapdpeAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllAD 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1528 RALEQQVEEMKTQLEELED---ELQATEDAKLRLEVNLQAMK---AQFERdLQGRDEQSEEKKKQLVRQVREMEaeledE 1601
Cdd:COG3096 889 ETLADRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----E 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1602 RKQRSMAVAARKKLEM-----DLKD-LEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASReeilaQAKENEkkL 1675
Cdd:COG3096 963 VVQRRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR-----DAKQQT--L 1035
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1676 KSMEAEMIQLqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1733
Cdd:COG3096 1036 QELEQELEEL--GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1450-1599 |
8.28e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1450 LAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEdlmsskddvgksvhELEKSKRA 1529
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQ--------------KLEKRLLQ 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1530 LEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ--------SEEKKKQLVRQVREmEAELE 1599
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEILLEKVEE-EARHE 170
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1198-1611 |
8.99e-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: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1198 VEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1277
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1278 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEenrqklslstklkqVEDEKNSFREQLEEEEEAKHNLEK 1357
Cdd:pfam19220 116 KTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQR--------------AEGELATARERLALLEQENRRLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1358 QIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDkLEKTKTRLQQELDDLLVDLDHQRQSAC 1437
Cdd:pfam19220 182 LSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLE-EAVEAHRAERASLRMKLEALTARAAAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1438 nlekkqkkfDQLLAEEKTisakyaEERDRAEaEAREKEtkalslaRALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVG 1517
Cdd:pfam19220 261 ---------EQLLAEARN------QLRDRDE-AIRAAE-------RRLKEASIERDTLERRLAGLEADLERRTQQFQEMQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1518 KSVHELEKSKRALEQQVEEMKTQLEELEDELQatedaklrlevNLQAMKAQFERDLqgrdeqsEEKKKQLVRQVREMEAE 1597
Cdd:pfam19220 318 RARAELEERAEMLTKALAAKDAALERAEERIA-----------SLSDRIAELTKRF-------EVERAALEQANRRLKEE 379
|
410
....*....|....
gi 12667788 1598 LEDERKQRSMAVAA 1611
Cdd:pfam19220 380 LQRERAERALAQGA 393
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
837-1369 |
9.71e-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: 50.74 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 837 LLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEI 916
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQL 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 917 CHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKvTTEAKLKKLEEEQIILEDQNCKLAKEKKL 996
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 997 LEDRIAEFTTNLTEEEEkSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKM 1076
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1077 QLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDL----GEELEALKTELEDTL 1152
Cdd:TIGR00618 585 DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtalhALQLTLTQERVREHA 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1153 DSTAAQQELRSKREQevnilkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANE 1232
Cdd:TIGR00618 665 LSIRVLPKELLASRQ-------LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1233 VKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDN-------VTGLLSQSDSKSSKLTKDFsa 1305
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFfnrlreeDTHLLKTLEAEIGQEIPSD-- 815
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1306 lESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADM 1369
Cdd:TIGR00618 816 -EDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1620-1923 |
9.80e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1620 KDLEAHIDSANKNRDeaikqlrkLQAQMKDCMRELDDTRASREEILAQAKENEkklksmeaemiQLQEELAAAERAKRQA 1699
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETE-----------QLKQQLAQAPAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1700 QQERDELADEiANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANLQIDQINTDL-----NLERSHAQ 1774
Cdd:PRK11281 100 QAELEALKDD-NDEETRETLSTLSLRQLESRLAQ--------------TLDQLQNAQNDLAEYNSQLvslqtQPERAQAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1775 KNENAR--QQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNET-------KERQAACKQVRRTEKKLK 1845
Cdd:PRK11281 165 LYANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlqdllqKQRDYLTARIQRLEHQLQ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1846 dvLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANasrRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:PRK11281 245 --LLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEIN---LQLSQRLLKATEKLNTLTQQNLRVKNWLDR 317
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1522-1683 |
1.02e-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: 48.77 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDlqgrdeqseEKKKQLVRQVREMEA---EL 1598
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---------EEQLGNVRNNKEYEAlqkEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1599 EDERKQRSmavaarkklemdlkDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSM 1678
Cdd:COG1579 99 ESLKRRIS--------------DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*
gi 12667788 1679 EAEMI 1683
Cdd:COG1579 165 REELA 169
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1618-1712 |
1.04e-05 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 50.07 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1618 DLKDLEAHIDS-----ANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEI---LAQAKENEKKLKSMEAEMIQLQEEL 1689
Cdd:PRK05431 3 DIKLIRENPEAvkealAKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEI 82
|
90 100
....*....|....*....|...
gi 12667788 1690 AAAERAKRQAQQERDELADEIAN 1712
Cdd:PRK05431 83 KALEAELDELEAELEELLLRIPN 105
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1056-1167 |
1.15e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1056 DSTDLSDQIAELQAQIAELKMQLAKKE---------EELQAALARVEEEAAQKNMALKKIRELESQ--ISelQEDLESER 1124
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVS--QQELDEAR 154
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 12667788 1125 ASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ 1167
Cdd:COG1566 155 AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAA 197
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
859-1131 |
1.21e-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: 50.07 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 859 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 937
Cdd:pfam19220 124 ERQLAAETEQNRALEEENKALREEAQAAEKALQRAEgELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 938 KKKMQQNIQELEEQLEEEESARQKL------QLEKVTTE--AKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTtnlt 1009
Cdd:pfam19220 204 LDATRARLRALEGQLAAEQAERERAeaqleeAVEAHRAEraSLRMKLEALTARAAATEQLLAEARNQLRDRDEAIR---- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1010 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAL 1089
Cdd:pfam19220 280 AAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELT 359
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 12667788 1090 ARVEEEAAqknmalkkirELESQISELQEDLESERASRNKAE 1131
Cdd:pfam19220 360 KRFEVERA----------ALEQANRRLKEELQRERAERALAQ 391
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1104-1922 |
1.21e-05 |
|
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: 50.82 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1104 KKIRELESQISELQEDLESERASRNKAEKQKRDLGE---ELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEA 1180
Cdd:TIGR00606 217 EKACEIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVF 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1181 KTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL-LQGKGDSEHKRKKvEAQLQELQV 1259
Cdd:TIGR00606 297 QGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqLQADRHQEHIRAR-DSLIQSLAT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1260 kfnegeRVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTkdfSALESQLQDTQELLQEEnrqklslstkLKQVEDEKN 1339
Cdd:TIGR00606 376 ------RLELDGFERGPFSERQIKNFHTLVIERQEDEAKTA---AQLCADLQSKERLKQEQ----------ADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1340 SFREQLEEEeeaKHNLEKQIAtlhaQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQrhEEKVAAYDKLEKTKTRLQ 1419
Cdd:TIGR00606 437 GLGRTIELK---KEILEKKQE----ELKFVIKELQQLEGSSDRILELDQELRKAERELSK--AEKNSLTETLKKEVKSLQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1420 QELDdllvdldhqrqsacNLEKKQKKFDQLLAEEKtisakyaeerdraeaEAREKETKALSLARALEEAMEQKAELERLN 1499
Cdd:TIGR00606 508 NEKA--------------DLDRKLRKLDQEMEQLN---------------HHTTTRTQMEMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1500 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ 1579
Cdd:TIGR00606 559 SDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1580 SEekkkqlvrqVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRA 1659
Cdd:TIGR00606 639 SD---------LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1660 SREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalalEEKRRLEARIAQLEEELE 1739
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ----------RLKNDIEEQETLLGTIMP 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1740 EEQGNTELINDrlkKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKskykasitaleaKIAQL 1819
Cdd:TIGR00606 780 EEESAKVCLTD---VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD------------TVVSK 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1820 EEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRE 1899
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
810 820
....*....|....*....|....*..
gi 12667788 1900 LEDATETADAMNR----EVSSLKNKLR 1922
Cdd:TIGR00606 925 KEELISSKETSNKkaqdKVNDIKEKVK 951
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
972-1921 |
1.25e-05 |
|
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: 50.82 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 972 KLKKLEEEQIILEDQNCKLAKEKklLEDRIAEFTTNLTEE--EEKSKSLAKLKNKHEamitDLEERLRREEKQRQELEKT 1049
Cdd:TIGR01612 711 KIQNMETATVELHLSNIENKKNE--LLDIIVEIKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKY 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1050 RRKLEGDSTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVEEEAAQ-----KNMA---LKKIRELESQISELQEDLE 1121
Cdd:TIGR01612 785 KSKISEIKNHYNDQINIDNIKDEDAK-QNYDKSKEYIKTISIKEDEIFKiinemKFMKddfLNKVDKFINFENNCKEKID 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1122 SERAS----RNKAEKQKRDlgEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE--EEAKTHEAQIQEMRQKHS 1195
Cdd:TIGR01612 864 SEHEQfaelTNKIKAEISD--DKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEyiKICENTKESIEKFHNKQN 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1196 QAVEELAEQLEQTKRV----KANLEKAKQTLENERGELANEVKVLlqGKGDSEHKRKKVEAQLQELQV------------ 1259
Cdd:TIGR01612 942 ILKEILNKNIDTIKESnlieKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAKNNELIKYFNDLKAnlgknkenmlyh 1019
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1260 KFNEGERVRTELADKVTKLQVELDNV-----TGLLSQSDSKSSKLTKDFSALESQLQDTQELLQ---EENRQKLSLSTKL 1331
Cdd:TIGR01612 1020 QFDEKEKATNDIEQKIEDANKNIPNIeiaihTSIYNIIDEIEKEIGKNIELLNKEILEEAEINItnfNEIKEKLKHYNFD 1099
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1332 KQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETA----EEVKRKL--QKDLEGLSQRHEEKV 1405
Cdd:TIGR01612 1100 DFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQindlEDVADKAisNDDPEEIEKKIENIV 1179
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1406 AAYDK-----------------LEKTKTRLQ------------------QELDDLLVDLDHQRQSacnLEKKQKKFDQLL 1450
Cdd:TIGR01612 1180 TKIDKkkniydeikkllneiaeIEKDKTSLEevkginlsygknlgklflEKIDEEKKKSEHMIKA---MEAYIEDLDEIK 1256
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1451 AEEKTISAKYAEERD-RAEAEA--------------REKETKALSLAR----ALEEAMEQKAELERLNKQFRTEMEDLMS 1511
Cdd:TIGR01612 1257 EKSPEIENEMGIEMDiKAEMETfnishdddkdhhiiSKKHDENISDIRekslKIIEDFSEESDINDIKKELQKNLLDAQK 1336
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1512 SKDDVGKSVHE---------LEKSKRALEQqVEEMKTQLEE----LEDELQATED--AKLRLEVNLQAMKAQFERDLQGR 1576
Cdd:TIGR01612 1337 HNSDINLYLNEianiynilkLNKIKKIIDE-VKEYTKEIEEnnknIKDELDKSEKliKKIKDDINLEECKSKIESTLDDK 1415
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1577 D-EQSEEKKKQLVRQVREMEA-----------------------ELEDERKQRSMAVA---ARKKLEMDLKDLEAHIDSA 1629
Cdd:TIGR01612 1416 DiDECIKKIKELKNHILSEESnidtyfknadennenvlllfkniEMADNKSQHILKIKkdnATNDHDFNINELKEHIDKS 1495
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1630 NKNRDEAIKQLRKLQA------QMKDCMREL-------------DDTRASREEILAQAKE-----------NEKKLKSME 1679
Cdd:TIGR01612 1496 KGCKDEADKNAKAIEKnkelfeQYKKDVTELlnkysalaiknkfAKTKKDSEIIIKEIKDahkkfileaekSEQKIKEIK 1575
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1680 AEMIQLQEELAAAERAKRQA---QQERDELAD---EIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIN---- 1749
Cdd:TIGR01612 1576 KEKFRIEDDAAKNDKSNKAAidiQLSLENFENkflKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNlnsl 1655
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1750 ----DRLKKANLQIDQINTDLNLERSHAQKNENARQQlERQNKELKV--KLQEMEGTVKSKYKASITALEAKIAQLEEQL 1823
Cdd:TIGR01612 1656 qeflESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQ-HKKNYEIGIieKIKEIAIANKEEIESIKELIEPTIENLISSF 1734
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1824 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA 1903
Cdd:TIGR01612 1735 NTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKKSKSYLDDI 1814
|
1130
....*....|....*...
gi 12667788 1904 teTADAMNREVSSLKNKL 1921
Cdd:TIGR01612 1815 --EAKEFDRIINHFKKKL 1830
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
859-1233 |
1.31e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 859 EKQLA-AENRLTEMETLQSQLM--AEKLQLQEQLQAE--TELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQH 933
Cdd:COG4913 344 EREIErLERELEERERRRARLEalLAALGLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 934 LQAEKKKMQQNIQELEEQLEEEESA-RQKLQLekvtTEAKLK--------KLEEEQ---------------IILEDQNCK 989
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRDAlAEALGL----DEAELPfvgelievRPEEERwrgaiervlggfaltLLVPPEHYA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 990 LAKE--------KKLLEDRIAEFTTNLTEEEEKSKSLA-KLKNK-HEA--------------MITDLEERLRRE------ 1039
Cdd:COG4913 500 AALRwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAgKLDFKpHPFrawleaelgrrfdyVCVDSPEELRRHpraitr 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1040 -----------EKQRQELEKTRRKLEGDSTD----LSDQIAELQAQIAELKMQLAKKEEELQA--ALARVEEEAAQKNMA 1102
Cdd:COG4913 580 agqvkgngtrhEKDDRRRIRSRYVLGFDNRAklaaLEAELAELEEELAEAEERLEALEAELDAlqERREALQRLAEYSWD 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1103 LKKIRELESQISELQEDLESERASRNKAEKqkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1182
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1183 HEAQIQEMRQKHSQAVEELAEQL---EQTKRVKANLEKAKQTLENERGELANEV 1233
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1026-1281 |
1.33e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1106 IRELESQISELQEdlesERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQEL--RSKR-EQEVNILKKTLEEEAKT 1182
Cdd:COG1340 87 LNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1183 HE--AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLE--NERGELANEVKVLLQGKGDSEHKrkkveaQLQELQ 1258
Cdd:COG1340 163 KElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADelRKEADELHKEIVEAQEKADELHE------EIIELQ 236
|
250 260
....*....|....*....|...
gi 12667788 1259 VKFNEGERVRTELADKVTKLQVE 1281
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKRE 259
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
869-1593 |
1.38e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.18 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 869 TEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEIchdlearveEEEERCQHLQAEKKKMQQniQE 947
Cdd:PRK10246 198 TELEKLQAQASGVALLTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSL---------NWLTRLDELQQEASRRQQ--AL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 948 LEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQiilEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEA 1027
Cdd:PRK10246 267 QQALAAEEKAQPQLAALSLAQPARQLRPHWERI---QEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1028 MITDLEERLRREEKQR---QELEKTRRKLEGDSTDlSDQIAELQAQIAELKMQLAKKEEelqAALARVEEEAAQKNMALK 1104
Cdd:PRK10246 344 QQQSLNTWLAEHDRFRqwnNELAGWRAQFSQQTSD-REQLRQWQQQLTHAEQKLNALPA---ITLTLTADEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1105 KIRELESQISELQEDLeserasrnkAEKQKRdlgeelealKTELEDTLDSTAAQQELRskreqevnilkktleeeakthE 1184
Cdd:PRK10246 420 EQRPLRQRLVALHGQI---------VPQQKR---------LAQLQVAIQNVTQEQTQR---------------------N 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1185 AQIQEMRQKHSQAVEELAeqleqtkRVKA--NLEKAKQTLENERGELANEVKVLLQGKgdSEHKrkkVEAQLQELQVKFN 1262
Cdd:PRK10246 461 AALNEMRQRYKEKTQQLA-------DVKTicEQEARIKDLEAQRAQLQAGQPCPLCGS--TSHP---AVEAYQALEPGVN 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1263 EgeRVRTELADKVTKLQVEldnVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVED-----E 1337
Cdd:PRK10246 529 Q--SRLDALEKEVKKLGEE---GAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDiqpwlD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1338 KNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETaeevkrklQKDLEGLSQRHEEKVAAYDKLEKTKTR 1417
Cdd:PRK10246 604 AQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLT--------ALAGYALTLPQEDEEASWLATRQQEAQ 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1418 LQQelddllvdldhQRQSacNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEA---REKETKALSLARALEEAMEQKA- 1493
Cdd:PRK10246 676 SWQ-----------QRQN--ELTALQNRIQQLTPLLETLPQSDDLPHSEETVALdnwRQVHEQCLSLHSQLQTLQQQDVl 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1494 ELERLNK---QFRTEMED---------LMSSKDDvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQAtedaklrlevN 1561
Cdd:PRK10246 743 EAQRLQKaqaQFDTALQAsvfddqqafLAALLDE--ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQ----------H 810
|
730 740 750
....*....|....*....|....*....|..
gi 12667788 1562 LQAMKAQFerDLQGRDEQSEEKKKQLVRQVRE 1593
Cdd:PRK10246 811 QQHRPDGL--DLTVTVEQIQQELAQLAQQLRE 840
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1522-1706 |
1.49e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALEQQVEEMKTQLEELEDELQA----------TEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVR 1589
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQqlSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1590 QVREMEAELEDE-----RKQRSMAVAARKKLEM-------DLKDLEAHIDSANKNRDEAIKQ-LRKLQAQMkdcmRELDD 1656
Cdd:COG3206 252 GPDALPELLQSPviqqlRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRiLASLEAEL----EALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 12667788 1657 TRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL 1706
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
997-1715 |
1.55e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 997 LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITD---LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAE 1073
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1074 LKmQLAKKEEELQAALARVEEeaaQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALkteledTLD 1153
Cdd:PRK04863 598 LA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL------SQP 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1154 STAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHS-QAVeelaeqleqtkrVKANLEKAKQTLENERGELanE 1232
Cdd:PRK04863 668 GGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALYGPArHAI------------VVPDLSDAAEQLAGLEDCP--E 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1233 VKVLLQGKGDS-EHKRKKVEAQLQELQVKFNE--------------GERVRTELADkvtKLQVELDNVTGLLSQSDSKSS 1297
Cdd:PRK04863 734 DLYLIEGDPDSfDDSVFSVEELEKAVVVKIADrqwrysrfpevplfGRAAREKRIE---QLRAEREELAERYATLSFDVQ 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1298 KLTKDFSALESQL---------QDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEeeeeakhNLEKQIATLhaqvad 1368
Cdd:PRK04863 811 KLQRLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLE-------QAKEGLSAL------ 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1369 mkKKMEDSVGCLetaeevkrklqkDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLdhqrQSACNLEKKQKKFDQ 1448
Cdd:PRK04863 878 --NRLLPRLNLL------------ADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLE----PIVSVLQSDPEQFEQ 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1449 LlaeektisakyaeERDRAEAEAREKETKAlsLARALEEAMEQKAELERLNKQFRTEMEDLMSSKddvgksvheLEKSKR 1528
Cdd:PRK04863 940 L-------------KQDYQQAQQTQRDAKQ--QAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEK---------LRQRLE 995
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1529 ALEQQVEEMKTQLEELEDelQATEDAKLrlevnLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMA 1608
Cdd:PRK04863 996 QAEQERTRAREQLRQAQA--QLAQYNQV-----LASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDELHAR 1068
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1609 VAA----RKKLEMDLKDLEAHIDSANknrdeaiKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN--EKKLKSMEAEM 1682
Cdd:PRK04863 1069 LSAnrsrRNQLEKQLTFCEAEMDNLT-------KKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERRLHRRELAY 1141
|
730 740 750
....*....|....*....|....*....|....*.
gi 12667788 1683 IQLQEELAAAERAK---RQAQQERDELADEIANSSG 1715
Cdd:PRK04863 1142 LSADELRSMSDKALgalRLAVADNEHLRDVLRLSED 1177
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1440-1922 |
1.77e-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: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1440 EKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKEtkalslaraleeamEQKAELERLNKQFRTEmedlmssKDDVGKS 1519
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQE--------------ERQETSAELNQLLRTL-------DDQWKEK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1520 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELE 1599
Cdd:pfam12128 303 RDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL----ENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1600 DERKQRSMAVAArkKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMrelddtrasrEEILAQAKENEKKLKSME 1679
Cdd:pfam12128 379 RRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL----------EAGKLEFNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1680 AEMIQLQEELAAAERAKRQ--AQQERDELADEIANSSGKGALALE-EKRRLEARIAQLEEELEEEQGNTELINDRLKKAN 1756
Cdd:pfam12128 447 GELKLRLNQATATPELLLQleNFDERIERAREEQEAANAEVERLQsELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1757 LQID-QINTDLNLERSHAQKNEN------ARQQLERQNKE----------------LKVKLQEMEgtvKSKYKASITALE 1813
Cdd:pfam12128 527 LQLFpQAGTLLHFLRKEAPDWEQsigkviSPELLHRTDLDpevwdgsvggelnlygVKLDLKRID---VPEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1814 AKIAQLEEQLDNETKERQAACKQVRRTEKKLkdvllqvdderrnaeqykdqaDKASTRLKQLKRQLEEAEEEAQRANASR 1893
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGEL---------------------EKASREETFARTALKNARLDLRRLFDEK 662
|
490 500 510
....*....|....*....|....*....|
gi 12667788 1894 RKLQRELEDATETA-DAMNREVSSLKNKLR 1922
Cdd:pfam12128 663 QSEKDKKNKALAERkDSANERLNSLEAQLK 692
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1184-1392 |
1.86e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1184 EAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnevkvllqgkgDSEHKRKKVEAQLQELQVKFNE 1263
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1264 GervRTELADKVTKLQVELDNVTGLLSQSDSKS-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1342
Cdd:COG3883 84 R---REELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 12667788 1343 EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQK 1392
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1443-1753 |
2.05e-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: 49.30 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1443 QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLN---KQFRTEMEDLMSSKDDVGKS 1519
Cdd:pfam19220 54 EALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1520 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER------DLQGRDEQSEEKKKQLVRQVRE 1593
Cdd:pfam19220 134 NRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEqaaelaELTRRLAELETQLDATRARLRA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1594 MEAELEDERKQRSMAVAA-----------RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRe 1662
Cdd:pfam19220 214 LEGQLAAEQAERERAEAQleeaveahraeRASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIER- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1663 eilaqaKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQ 1742
Cdd:pfam19220 293 ------DTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVER 366
|
330
....*....|.
gi 12667788 1743 GNTELINDRLK 1753
Cdd:pfam19220 367 AALEQANRRLK 377
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1083-1263 |
2.43e-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: 47.61 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1083 EELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldstaaqQELR 1162
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-------EARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1163 SKREQEVNILKKTLEEEAKTHEAQIQEMRQkhSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGD 1242
Cdd:COG1579 76 KKYEEQLGNVRNNKEYEALQKEIESLKRRI--SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|.
gi 12667788 1243 SEHKRKKVEAQLQELQVKFNE 1263
Cdd:COG1579 154 LEAELEELEAEREELAAKIPP 174
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1178-1907 |
2.81e-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: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1178 EEAKTHEAQIQEMRQKHSQAVEELAE---QLEQTKRVKANLEKAKQTLENERgELANEVKVLLQGKGDSEHKRKKVEAQL 1254
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEeqyRLVEMARELEELSARESDLEQDY-QAASDHLNLVQTALRQQEKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1255 QELQVKFNEGERVRTELADKVTKLQVELDNVTgllSQSDSKSSKLTKDFSALESQ-------------LQDTQELLQEEN 1321
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAE---EEVDSLKSQLADYQQALDVQqtraiqyqqavqaLEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1322 ---------------------RQKLSLSTKLKQVEDEKNSF-----------------------REQLEEEEEAKHNLEk 1357
Cdd:COG3096 434 ltpenaedylaafrakeqqatEEVLELEQKLSVADAARRQFekayelvckiageversqawqtaRELLRRYRSQQALAQ- 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1358 QIATLHAQVADmkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAC 1437
Cdd:COG3096 513 RLQQLRAQLAE-----------LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1438 NLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLA--RALEEAMEQKAELERLNKQfrtemedlmsSKDd 1515
Cdd:COG3096 582 ELRQQL---EQLRARIKELAARAPAWLAAQDALERLREQSGEALAdsQEVTAAMQQLLEREREATV----------ERD- 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1516 vgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQAT-----------EDA--------KLR---LEVNLQAMK 1566
Cdd:COG3096 648 ------ELAARKQALESQIERLSqpggaedPRLLALAERLGGVllseiyddvtlEDApyfsalygPARhaiVVPDLSAVK 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1567 AQF-------------ERDLQGRDEQS----EEKKKQLV----RQVR--------------------EMEAELEDERKQR 1605
Cdd:COG3096 722 EQLagledcpedlyliEGDPDSFDDSVfdaeELEDAVVVklsdRQWRysrfpevplfgraarekrleELRAERDELAEQY 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1606 SMAVAARKKLEMDLKDLEA----HIDSA-NKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1680
Cdd:COG3096 802 AKASFDVQKLQRLHQAFSQfvggHLAVAfAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLP 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1681 EMIQLQEElAAAERAkRQAQQERDElADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQID 1760
Cdd:COG3096 882 QANLLADE-TLADRL-EELREELDA-AQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIF 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1761 QInTDLnLERSHAQKNENARQQLERQ---NKELKVKLQEMEgTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQV 1837
Cdd:COG3096 959 AL-SEV-VQRRPHFSYEDAVGLLGENsdlNEKLRARLEQAE-EARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTL 1035
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1838 RRTEKKLKDVLLQVDDE-----RRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETA 1907
Cdd:COG3096 1036 QELEQELEELGVQADAEaeeraRIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1462-1704 |
2.95e-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: 47.72 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1462 EERDRAEAEAREKETKalsLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTql 1541
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1542 eeLEDELQATEDAKLRLEVNLQAMKaqferdlqGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDL-- 1619
Cdd:pfam00261 83 --LENRALKDEEKMEILEAQLKEAK--------EIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1620 -----KDLEAHIDSANKNRDEAIKQLRKLQAQMKdcmrelddtrasreEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1694
Cdd:pfam00261 153 vgnnlKSLEASEEKASEREDKYEEQIRFLTEKLK--------------EAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|
gi 12667788 1695 AKRQAQQERD 1704
Cdd:pfam00261 219 KYKAISEELD 228
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1491-1920 |
3.17e-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: 48.86 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1491 QKAELERLNKQFRTEMEDLMSSKD---DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKA 1567
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKelkNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1568 QFERDLQGRDEQSEEKKKqlvrqvreMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQM 1647
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNK--------LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1648 KDCMRELDDTRASR---EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEK 1724
Cdd:TIGR04523 183 LNIQKNIDKIKNKLlklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1725 RRLEARIAQLeeeleeeQGNTELINDRLKKANLQIDQINTDLnlERSHAQKNENARQQLERQNKELKVKLQEMEGTVkSK 1804
Cdd:TIGR04523 263 NKIKKQLSEK-------QKELEQNNKKIKELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI-SQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1805 YKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVL--------------LQVDDERRNAEQYKDQADKAST 1870
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsykqeiknleSQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 12667788 1871 RLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1920
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1033-1212 |
3.28e-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: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1033 EERLRREEKQRQ-ELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlAKKEEELQAALARVEEEAAQKNMalkkirELES 1111
Cdd:COG2268 211 ETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEERRE-AETARAEAEAAYEIAEANAEREV------QRQL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1112 QISELQEDLESERASRNKAEKQ-KRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVniLKKTLEEEAKTHEAQIQEM 1190
Cdd:COG2268 284 EIAEREREIELQEKEAEREEAElEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG--KRALAEAWNKLGDAAILLM 361
|
170 180
....*....|....*....|...
gi 12667788 1191 R-QKHSQAVEELAEQLEQTKRVK 1212
Cdd:COG2268 362 LiEKLPEIAEAAAKPLEKIDKIT 384
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1088-1297 |
3.30e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1088 ALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKR-- 1165
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1166 -----EQEVNILKKTLE----EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1236
Cdd:COG3883 94 alyrsGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1237 LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSS 1297
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1019-1153 |
3.33e-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: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1019 AKLKNKHEAM---ITDLEERLRREEKQRQELEKtrrklegdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1095
Cdd:COG0542 400 ARVRMEIDSKpeeLDELERRLEQLEIEKEALKK-------------EQDEASFERLAELRDELAELEEELEALKARWEAE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1096 aaqknmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLD 1153
Cdd:COG0542 467 -----------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
650-674 |
4.32e-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: 4.32e-05
10 20
....*....|....*....|....*
gi 12667788 650 YKEQLAKLMATLRNTNPNFVRCIIP 674
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1462-1718 |
4.33e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 48.83 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1462 EERDRAEAEareketKALSLAR-ALEEAMEQKA---ELERLNKQFRTEMEDLMsskddvgksvhelekskRALEQQVEEM 1537
Cdd:pfam13779 480 EDGDLSDAE------RRLRAAQeRLSEALERGAsdeEIAKLMQELREALDDYM-----------------QALAEQAQQN 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1538 KTQLEELEDELQATEDAKlrlevNLQAMKAQFERDLQ-GRDEQSEekkkQLVRQVREMEAELEDERKQRSMAVAARKKLE 1616
Cdd:pfam13779 537 PQDLQQPDDPNAQEMTQQ-----DLQRMLDRIEELARsGRRAEAQ----QMLSQLQQMLENLQAGQPQQQQQQGQSEMQQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1617 MdLKDLEAHIDSANKNRDEAIKQLRKLQAQmkdcmrelDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK 1696
Cdd:pfam13779 608 A-MDELGDLLREQQQLLDETFRQLQQQGGQ--------QQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAE 678
|
250 260
....*....|....*....|....
gi 12667788 1697 RQAQ--QERDELADEIANSSGKGA 1718
Cdd:pfam13779 679 RQQAlrRRLEELQDELKELGGKEP 702
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
995-1230 |
4.68e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 995 KLLEDRIAEFTtnlteeeEKSKSLAKLKNKHEAMITDLEERLRREEKQRQEL-EKTRRklegdstDLSDQIAELQAQIAE 1073
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIE-------DLRRQLDTLTVERAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1074 LKMQLAKKEEELQAALARVEEEAAQKnmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELED--- 1150
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1151 -------------------TLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAV----EELAE---- 1203
Cdd:pfam00038 146 elqaqvsdtqvnvemdaarKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALrsakEEITElrrt 225
|
250 260 270
....*....|....*....|....*....|...
gi 12667788 1204 ------QLEQTKRVKANLEKAKQTLEnERGELA 1230
Cdd:pfam00038 226 iqsleiELQSLKKQKASLERQLAETE-ERYELQ 257
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1056-1240 |
5.02e-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: 47.42 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1056 DSTDLSDQIAELQAQIAelkmqlakkeeELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEkqkr 1135
Cdd:pfam00529 52 DPTDYQAALDSAEAQLA-----------KAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQ---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1136 dlgEELEALKTELEDTlDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK-RVKAN 1214
Cdd:pfam00529 117 ---AQLAQAQIDLARR-RVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELsGAQLQ 192
|
170 180
....*....|....*....|....*..
gi 12667788 1215 LEKAKQTLENERGELAN-EVKVLLQGK 1240
Cdd:pfam00529 193 IAEAEAELKLAKLDLERtEIRAPVDGT 219
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1438-1790 |
6.25e-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: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1438 NLEKKQKKFDQLLAEEKTISA---KYAEERDRAEAEAREKEtkALSLARALEEAMEQKAElERLNKqfrteMEDLMSSKD 1514
Cdd:COG3096 276 HANERRELSERALELRRELFGarrQLAEEQYRLVEMARELE--ELSARESDLEQDYQAAS-DHLNL-----VQTALRQQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1515 DVGKSVHELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQ------------- 1574
Cdd:COG3096 348 KIERYQEDLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQTRAIQyqqavqalekara 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1575 -------------GRDEQSEEKKKQLVRQVREMEAEL---EDERKQ----------------RSMAVAARKKLEMDLKDL 1622
Cdd:COG3096 428 lcglpdltpenaeDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQfekayelvckiageveRSQAWQTARELLRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1623 EAHIDSANKNRDEaIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQE 1702
Cdd:COG3096 508 QALAQRLQQLRAQ-LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1703 RDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKanlqidqiNTDLNLERSHAQKnenARQQ 1782
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER--------EREATVERDELAA---RKQA 655
|
....*...
gi 12667788 1783 LERQNKEL 1790
Cdd:COG3096 656 LESQIERL 663
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1381-1664 |
8.09e-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: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1381 ETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTR----LQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLA--EEK 1454
Cdd:pfam05667 215 ELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRiaeqLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTtdTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQK--AELERLNKQFrtemEDLMSSKDDVGKSVHELEKSKRALEQ 1532
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQreEELEELQEQL----EDLESSIQELEKEIKKLESSIKQVEE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1533 QVEEMKTQLEELEDELQATE-------DAKLRLEvNLQAMKAQFERDLQGRDEQSEEKKKQLV---RQVREMEAELEDER 1602
Cdd:pfam05667 371 ELEELKEQNEELEKQYKVKKktldllpDAEENIA-KLQALVDASAQRLVELAGQWEKHRVPLIeeyRALKEAKSNKEDES 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1603 KQ------------RSMAVAARKKLEMdLKDLEAHIDSANK--NRD-------EAIKQLRKlqaQMKDCMRELDDTRASR 1661
Cdd:pfam05667 450 QRkleeikelrekiKEVAEEAKQKEEL-YKQLVAEYERLPKdvSRSaytrrilEIVKNIKK---QKEEITKILSDTKSLQ 525
|
...
gi 12667788 1662 EEI 1664
Cdd:pfam05667 526 KEI 528
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1466-1874 |
8.46e-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: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1466 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 1521
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDleqdyqaasdhlnlvqtalrqqekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1587
Cdd:COG3096 355 DLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQTRAIQYQQAvQALEKARALcglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1588 -VRQVREMEAELEDERKQRSMAV-AARKKLEMDlkdleahiDSANKNRDEAIKQLRKLQAQMkdcmrELDDTRASREEIL 1665
Cdd:COG3096 435 tPENAEDYLAAFRAKEQQATEEVlELEQKLSVA--------DAARRQFEKAYELVCKIAGEV-----ERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1666 AQAKEnekkLKSMEAEMIQLQEELAAAERAKRQaQQERDELADEIANSSGK---GALALEE-KRRLEARIAqleeeleee 1741
Cdd:COG3096 502 RRYRS----QQALAQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQqldAAEELEElLAELEAQLE--------- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1742 qgntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKVKLQEMEgtvkSKYKASITALEAkIAQLEE 1821
Cdd:COG3096 568 -----------------------ELEEQAAEAVEQ---RSELRQQLEQLRARIKELA----ARAPAWLAAQDA-LERLRE 616
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 12667788 1822 QLDNETKERQAACKQVRRTEKKLKdvllQVDDERRNAEQYKDQADKASTRLKQ 1874
Cdd:COG3096 617 QSGEALADSQEVTAAMQQLLERER----EATVERDELAARKQALESQIERLSQ 665
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1439-1598 |
8.89e-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: 46.07 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1439 LEKKQKKFDQLLAEEKTISAKYAE---ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD- 1514
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAEledELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1515 -DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVRE 1593
Cdd:COG1579 92 eALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
....*
gi 12667788 1594 MEAEL 1598
Cdd:COG1579 172 IPPEL 176
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1480-1587 |
8.90e-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: 44.61 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1480 SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE 1559
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90 100
....*....|....*....|....*...
gi 12667788 1560 VNLQAMKAQFERDLQGRDEQSEEKKKQL 1587
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRDREIEKLKERL 149
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1578-1733 |
9.58e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.59 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQ-----LRKLQAQMKDCMR 1652
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1653 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSSGKGALALEEkrRLEARIA 1732
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL-KARAKAAKAQEKVNEALSGIDSDDATSALE--RMEEKIE 175
|
.
gi 12667788 1733 Q 1733
Cdd:COG1842 176 E 176
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1075-1221 |
1.09e-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: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1075 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEdleserasrnkaekQKRDLGEELEALK---TELEDT 1151
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA--------------EVEELEAELEEKDeriERLERE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1152 LDSTAAQQELRSKREQEVNIlkktLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKANLEKAKQT 1221
Cdd:COG2433 450 LSEARSEERREIRKDREISR----LDREIERLERELEEERER----IEELKRKLERLKELWKLEHSGELV 511
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1464-1729 |
1.11e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.23 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1464 RDRAEAEAREKETKALSLARALEEAMEQkaeLERLNKQFRTEMEDLMS-SKDDVGKSVHELEKSKRALEQQVEEMKTQLE 1542
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEALDK---LRSYLPKLNPLREEKKKvSVKSLEELIKDVEEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1543 ELEDELQATEDAKLRLEVnLQAMKAQFERDLQGR---------DEQSEEKKKQLVRQVremEAELEDERKQRSMAVAArk 1613
Cdd:PRK05771 111 ELENEIKELEQEIERLEP-WGNFDLDLSLLLGFKyvsvfvgtvPEDKLEELKLESDVE---NVEYISTDKGYVYVVVV-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1614 klemdlkdleahidSANKNRDEAIKQLRKLQAQMKdcmrELDDTRASREEIlaqaKENEKKLKSMEAEMIQLQEELAAae 1693
Cdd:PRK05771 185 --------------VLKELSDEVEEELKKLGFERL----ELEEEGTPSELI----REIKEELEEIEKERESLLEELKE-- 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 12667788 1694 rakrqaqqERDELADEIANSSGkgaLALEEKRRLEA 1729
Cdd:PRK05771 241 --------LAKKYLEELLALYE---YLEIELERAEA 265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1467-1715 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1467 AEAEAREKETKALSLARALEEAMEQKAELERlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELED 1546
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1547 EL-------QATEDAKLRLEVNLQA-------MKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsmAVAAR 1612
Cdd:COG3883 87 ELgeraralYRSGGSVSYLDVLLGSesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1613 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1692
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260
....*....|....*....|...
gi 12667788 1693 ERAKRQAQQERDELADEIANSSG 1715
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1051-1339 |
1.22e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.16 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1051 RKLEGDSTDlsdqIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKnmaLKKirELESQISE------LQEDLESER 1124
Cdd:PLN03229 422 KKREAVKTP----VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LKK--EIDLEYTEaviamgLQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1125 ASRNKAEKQK----RDLGEELEALKTELEDTLDSTAAQQELRSKRE--QEVNILKKTLEEEAKTHEAQiQEMRQKhSQAV 1198
Cdd:PLN03229 493 EEFSKANSQDqlmhPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKK-FKEV 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1199 EELAEQLEQTKRVKANLEKA------------KQTLENERGELANEVKVLLQGKG-DSEHKRKKveaQLQELQVKFNEGE 1265
Cdd:PLN03229 571 MDRPEIKEKMEALKAEVASSgassgdeldddlKEKVEKMKKEIELELAGVLKSMGlEVIGVTKK---NKDTAEQTPPPNL 647
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1266 RVRTE-LADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSL---STKLKQVEDEKN 1339
Cdd:PLN03229 648 QEKIEsLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEalnSSELKEKFEELE 725
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
989-1151 |
1.22e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 989 KLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:PHA02562 196 QIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1069 --------------------------AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLES 1122
Cdd:PHA02562 276 kvikmyekggvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT 355
|
170 180 190
....*....|....*....|....*....|....*.
gi 12667788 1123 ERASRNKAEK-------QKRDLGEELEALKTELEDT 1151
Cdd:PHA02562 356 LVDKAKKVKAaieelqaEFVDNAEELAKLQDELDKI 391
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1387-1622 |
1.23e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1387 KRKLQKDLEGLSQrheekVAAYDKLEKTKTR-LQQELDDLLVDLDH---------------QRQSACNLEKKQKKFDQLL 1450
Cdd:PHA02562 152 RRKLVEDLLDISV-----LSEMDKLNKDKIReLNQQIQTLDMKIDHiqqqiktynknieeqRKKNGENIARKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1451 AEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKqfrtemEDLMSSKDDV----GKSVHELEKS 1526
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK------VIKMYEKGGVcptcTQQISEGPDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1527 KRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAqfeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRS 1606
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250
....*....|....*.
gi 12667788 1607 MAVAARKKLEMDLKDL 1622
Cdd:PHA02562 376 DNAEELAKLQDELDKI 391
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1184-1420 |
1.39e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1184 EAQIQEMRQKHSQAVEELAEQLEQtkrVKANLEKAKQTLENERGElanevkvllQGKGDSEHKRKKVEAQLQELQVKFNE 1263
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1264 gerVRTELADkvtkLQVELDNVTGLLSQSDSKSSKLTKD--FSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF 1341
Cdd:COG3206 231 ---ARAELAE----AEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1342 REQLEEE-EEAKHNLEKQIATLHAQVADMKKKMEdsvgclETAEEVKR--KLQKDLEGLSQRHEEKVAAYDKLEKtktRL 1418
Cdd:COG3206 304 RAQLQQEaQRILASLEAELEALQAREASLQAQLA------QLEARLAElpELEAELRRLEREVEVARELYESLLQ---RL 374
|
..
gi 12667788 1419 QQ 1420
Cdd:COG3206 375 EE 376
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1041-1276 |
1.50e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAEL-KMQLAKKE-EELQAA---LARVEEEAAQKNMALKKIRELE----S 1111
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELeAAALQPGEeEELEEErrrLSNAEKLREALQEALEALSGGEggalD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1112 QISELQEDLesERASRnkAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQ-EVNilkktlEEE-AKTHE--AQI 1187
Cdd:COG0497 245 LLGQALRAL--ERLAE--YDPSLAELAERLESALIELEE------AASELRRYLDSlEFD------PERlEEVEErlALL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1188 QEMRQKHSQAVEEL-------AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLlqgkgdSEhKRKK--------VEA 1252
Cdd:COG0497 309 RRLARKYGVTVEELlayaeelRAELAELENSDERLEELEAELAEAEAELLEAAEKL------SA-ARKKaakklekaVTA 381
|
250 260 270
....*....|....*....|....*....|.
gi 12667788 1253 QLQEL-------QVKFNEGERVRTELADKVT 1276
Cdd:COG0497 382 ELADLgmpnarfEVEVTPLEEPGPNGADQVE 412
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1627-1931 |
1.55e-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: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1627 DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRE-EILAQAK---ENEKKLKSMEAEMIQLQEElaaaERAKRQAQQE 1702
Cdd:pfam17380 291 EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAiyaEQERMAMERERELERIRQE----ERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1703 RDELADEIANSSGKGALALEEKRRLEaRIAQLEEELEEEQGNTELINDRLKKANLQIDQINTdlnlERSHAQKNENARQQ 1782
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA----EQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1783 LERQNKELKVKLQEMEgtvKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRT-EKKLKDVLLQ-VDDERRNAEQ 1860
Cdd:pfam17380 442 EERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRKLL 518
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1861 YKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETA---DAMNREVSSLK----NKLRRGDLPFVVP 1931
Cdd:pfam17380 519 EKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMMRqiveSEKARAEYEATTP 596
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1074-1221 |
1.71e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1074 LKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQ--ISELQEDLESE-RASRNKAEKQKRDLGEELEALKTELED 1150
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1151 TLDStaaQQELrSKREQEVNILKKTLEEEAKTHEAQIQEMRQK--------HSQAVEELAEQLEQ------TKRVKANLE 1216
Cdd:PRK12704 105 LEKR---EEEL-EKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEILLEKVEEearheaAVLIKEIEE 180
|
....*
gi 12667788 1217 KAKQT 1221
Cdd:PRK12704 181 EAKEE 185
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
990-1115 |
1.85e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 990 LAKEKKL-LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLrreekqrQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:PRK09039 71 LERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQ-------KNMAL-KKIRELESQISE 1115
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKiadlgrrLNVALaQRVQELNRYRSE 198
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1618-1712 |
2.00e-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: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1618 DLKDLEAHIDS-----ANKNRDEAIKQLRKLQAQMKDCMRELDDTRASR----EEIlAQAKENEKKLKSMEAEMIQLQEE 1688
Cdd:COG0172 3 DIKLIRENPEAvkealAKRGFDLDVDELLELDEERRELQTEVEELRAERnalsKEI-GKAKKKGEEAEALIAEVKELKEE 81
|
90 100
....*....|....*....|....
gi 12667788 1689 LAAAERAKRQAQQERDELADEIAN 1712
Cdd:COG0172 82 IKELEEELKELEEELDELLLSIPN 105
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1374-1923 |
2.01e-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: 46.58 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1374 EDSVGCLETAEEVKRKLQKDLEglSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEE 1453
Cdd:TIGR00606 159 EDSNWPLSEGKALKQKFDEIFS--ATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1454 KTISAKYAEERDRAEAEAREKE---TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD---------------- 1514
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDeqlndlyhnhqrtvre 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1515 ------DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKK--- 1585
Cdd:TIGR00606 317 kerelvDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKnfh 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1586 QLVRQVREMEAEL---------EDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDE---AIKQLRKLQAQMKDCMrE 1653
Cdd:TIGR00606 397 TLVIERQEDEAKTaaqlcadlqSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDRIL-E 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1654 LDDTRASREEILAQAKENEKkLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANS------SGKGALALEEKRRL 1727
Cdd:TIGR00606 476 LDQELRKAERELSKAEKNSL-TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRtqmemlTKDKMDKDEQIRKI 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1728 EARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDL---NLERSHAQKNENA-RQQLERQNKEL------------- 1790
Cdd:TIGR00606 555 KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLaklNKELASLEQNKNHiNNELESKEEQLssyedklfdvcgs 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1791 ---KVKLQEMEGTVK--SKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQA 1865
Cdd:TIGR00606 635 qdeESDLERLKEEIEksSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1866 DKASTRLKqlKRQLEEAEEEAQRANASRRKLqreledatetadamnREVSSLKNKLRR 1923
Cdd:TIGR00606 715 ESELKKKE--KRRDEMLGLAPGRQSIIDLKE---------------KEIPELRNKLQK 755
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1304-1512 |
2.01e-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: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1304 SALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETA 1383
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1384 EEVKRKLQ-----KDLEGLSQRHE--EKVAAYDK-----LEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLA 1451
Cdd:COG3883 99 GGSVSYLDvllgsESFSDFLDRLSalSKIADADAdlleeLKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1452 EEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS 1512
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
960-1395 |
2.10e-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: 46.58 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 960 QKLQLEKVTTEAKLKKLE---EEQIILEDQNCKLAKEKKLLEDRIAEFTTnLTEEEEKSKSLAKLKNKHEAMITDLEErl 1036
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEIENEMGIEMDIKAEMET-FNISHDDDKDHHIISKKHDENISDIRE-- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1037 rreekqrqeleKTRRKLEGDS--TDLSDQIAELQAQIAELKMQLAKKEEELQ--AALARVEEEAAQKNMaLKKIRELESQ 1112
Cdd:TIGR01612 1306 -----------KSLKIIEDFSeeSDINDIKKELQKNLLDAQKHNSDINLYLNeiANIYNILKLNKIKKI-IDEVKEYTKE 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1113 ISELQEDLESERASRNKAEKQKRDlGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKK-----TLEEEAKTHEAQI 1187
Cdd:TIGR01612 1374 IEENNKNIKDELDKSEKLIKKIKD-DINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEesnidTYFKNADENNENV 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1188 Q------EMRQKHSQAV----------------EELAEQLEQTKRVKANLEKAKQTLENER---GELANEVKVLL----- 1237
Cdd:TIGR01612 1453 LllfkniEMADNKSQHIlkikkdnatndhdfniNELKEHIDKSKGCKDEADKNAKAIEKNKelfEQYKKDVTELLnkysa 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1238 --------QGKGDSE---------HKRKKVEAQLQELQVKFNEGERVRTElaDKVTK----------LQVELDNV-TGLL 1289
Cdd:TIGR01612 1533 laiknkfaKTKKDSEiiikeikdaHKKFILEAEKSEQKIKEIKKEKFRIE--DDAAKndksnkaaidIQLSLENFeNKFL 1610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1290 SQSD--SKSSKLTKDFSALESQLQ----DTQEllqeenrqklslsTKLKQVEDEKNSFREQLEEEEEAKHNLEKQ----- 1358
Cdd:TIGR01612 1611 KISDikKKINDCLKETESIEKKISsfsiDSQD-------------TELKENGDNLNSLQEFLESLKDQKKNIEDKkkeld 1677
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 12667788 1359 -----IATLHAQVADMKKKMEdsVGCLETAEEVKRKLQKDLE 1395
Cdd:TIGR01612 1678 eldseIEKIEIDVDQHKKNYE--IGIIEKIKEIAIANKEEIE 1717
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
970-1318 |
2.35e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 970 EAKLKKLEEEQ------IILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR 1043
Cdd:PRK01156 325 HAIIKKLSVLQkdyndyIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1044 QELEKTRRKLEGDSTDLSDQIAELQAQIAEL---KMQLAKKEEELQA-------------------------ALARVEEE 1095
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALrenLDELSRNMEMLNGqsvcpvcgttlgeeksnhiinhyneKKSRLEEK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1096 AAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeLEALKTELEDTLDSTAAQQE--------------- 1160
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDkhdkyeeiknryksl 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1161 ----LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1236
Cdd:PRK01156 559 kledLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEI 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1237 LQGKGDSEHKRKKVE------AQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQL 1310
Cdd:PRK01156 639 QENKILIEKLRGKIDnykkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
....*...
gi 12667788 1311 QDTQELLQ 1318
Cdd:PRK01156 719 NDINETLE 726
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
973-1207 |
2.36e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 973 LKKLEEEQII-LEDQNCKLAKEK--KLLEDRI-AEFTTN-LTEEEEKSKSLAKLKNKHEamITDLEERLRREEKQRQELE 1047
Cdd:PRK05771 22 LEALHELGVVhIEDLKEELSNERlrKLRSLLTkLSEALDkLRSYLPKLNPLREEKKKVS--VKSLEELIKDVEEELEKIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1048 KTRRKLEGDSTDLSDQIAELQAQIAELK--------MQLAKKEEELQAALARVEEEaaqknmalkKIRELESQISELQED 1119
Cdd:PRK05771 100 KEIKELEEEISELENEIKELEQEIERLEpwgnfdldLSLLLGFKYVSVFVGTVPED---------KLEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1120 LESERASRN-----KAEKQKRDLGEELEALKTELEDTLDSTAAQQELrSKREQEVNILKKTLEEEakthEAQIQEMRQKH 1194
Cdd:PRK05771 171 YISTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSELI-REIKEELEEIEKERESL----LEELKELAKKY 245
|
250
....*....|...
gi 12667788 1195 SQAVEELAEQLEQ 1207
Cdd:PRK05771 246 LEELLALYEYLEI 258
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1026-1709 |
2.43e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.36 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1026 EAMITDLEERLRREEKQRQE-LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakKEEELQAALARvEEEAAQKNMALK 1104
Cdd:NF041483 505 ERVRTEAIERATTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAAREL--REETERAIAAR-QAEAAEELTRLH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1105 KirELESQISELQEDLeseRASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE------------------------ 1160
Cdd:NF041483 582 T--EAEERLTAAEEAL---ADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEqeaerlrteaaadasaaraegenv 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1161 ---LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQK-HSQAVEELAEQLEQTKRVKAnleKAKQTLENERGELANEVKvl 1236
Cdd:NF041483 657 avrLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQERE-- 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1237 lQGKGDSEH----KRKKVEAQLQELQVKFNEGERVRTEL--ADKVTKLQVElDNVTGLLSQSDSKSSKLTkdfSALESQL 1310
Cdd:NF041483 732 -RAREQSEEllasARKRVEEAQAEAQRLVEEADRRATELvsAAEQTAQQVR-DSVAGLQEQAEEEIAGLR---SAAEHAA 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1311 QDTQELLQEENRQKLS--LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIAT-------LHAQVADMKKKM--EDSVGC 1379
Cdd:NF041483 807 ERTRTEAQEEADRVRSdaYAERERASEDANRLRREAQEETEAAKALAERTVSEaiaeaerLRSDASEYAQRVrtEASDTL 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1380 LETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAK 1459
Cdd:NF041483 887 ASAEQDAARTRADAREDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEA 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1460 YAE-ERDRAEAeareketkALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVheLEKSKRALEQQVEEMK 1538
Cdd:NF041483 967 TGEaERLRAEA--------AETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRT--LDEARKDANKRRSEAA 1036
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1539 TQLEELEDElQATEDAKLRLEVNLQAMKAQFERDLQGrDEQSEEKKKQLVRQVREMEAE----LEDERKQ--------RS 1606
Cdd:NF041483 1037 EQADTLITE-AAAEADQLTAKAQEEALRTTTEAEAQA-DTMVGAARKEAERIVAEATVEgnslVEKARTDadellvgaRR 1114
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1607 MAVAARKKLEMDLKDLEAHIDSAN-KNRDEAIKQLR----KLQAQMKDCMRELDDTRASREEILAQA------------K 1669
Cdd:NF041483 1115 DATAIRERAEELRDRITGEIEELHeRARRESAEQMKsageRCDALVKAAEEQLAEAEAKAKELVSDAnseaskvriaavK 1194
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 12667788 1670 ENEKKLKSMEAEMIQLQEElaaAERAKRQAQQERDELADE 1709
Cdd:NF041483 1195 KAEGLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEE 1231
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
992-1148 |
2.74e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 992 KEKKL--LEDRIAEFTTNLTEEEEKSKSLaklknkhEAMITDLEERLRREEKQRQelektrrKLEGDSTDLSDQIAELQA 1069
Cdd:PRK09039 51 KDSALdrLNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERS-------RLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12667788 1070 QIAELKMQLAKKEEELQAALARVEEeaaqknmalkkireLESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL 1148
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVEL--------------LNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1036-1167 |
3.29e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1036 LRRE-EKQRQELEKTRRKLegdsTDLSDQIA-------ELQAQIAELKMQLAKKEEE---LQAALARVEEEAAqknmalk 1104
Cdd:PRK09039 44 LSREiSGKDSALDRLNSQI----AELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGAGA------- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1105 kirELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL---EDTLDstAAQQELRSKREQ 1167
Cdd:PRK09039 113 ---AAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALD--ASEKRDRESQAK 173
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
858-1192 |
3.34e-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: 45.27 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 858 REKQLAAENRLtEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 937
Cdd:pfam07888 59 KEKERYKRDRE-QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 938 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKS 1017
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD-------QIAEL---QAQIAELKMQLAKKEEELQA 1087
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrTQAELhqaRLQAAQLTLQLADASLALRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1088 ALAR--VEEEAAQKNMALKK--IRELESQISELQEDLESERASRNKaekqkrdlgeeleaLKTELEDTLDSTAAQQELRS 1163
Cdd:pfam07888 298 GRARwaQERETLQQSAEADKdrIEKLSAELQRLEERLQEERMEREK--------------LEVELGREKDCNRVQLSESR 363
|
330 340
....*....|....*....|....*....
gi 12667788 1164 KREQEVNILKKTLEEEAKTHEAQIQEMRQ 1192
Cdd:pfam07888 364 RELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
999-1270 |
3.47e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 999 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERL-RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQ 1077
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKReERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1078 LAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRD--LGEELEALKTELEDTLDST 1155
Cdd:pfam02029 114 SWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEnfAKEEVKDEKIKKEKKVKYE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1156 AAQQELRSKREQEVnilkKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQlEQTKRVKAnlEKAKQTLENERGELANEVKV 1235
Cdd:pfam02029 194 SKVFLDQKRGHPEV----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREE-EAEVFLEA--EQKLEELRRRRQEKESEEFE 266
|
250 260 270
....*....|....*....|....*....|....*
gi 12667788 1236 LLQgkgdseHKRKKVEAQLQELQVKFNEGERVRTE 1270
Cdd:pfam02029 267 KLR------QKQQEAELELEELKKKREERRKLLEE 295
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1057-1213 |
3.78e-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: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1057 STDLSDQIAELQAQIAELKMQLA--KKEEELQAALARVEEEAAQKNMALKKIRELESQIS--ELQEDLESERASRNKAEK 1132
Cdd:pfam09731 282 NDDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRES 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1133 QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNIlKKTLEEEAKTHEAQIQEMRQK---HSQAVEELAEQLEQTK 1209
Cdd:pfam09731 362 YEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDI-KEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENR 440
|
....
gi 12667788 1210 RVKA 1213
Cdd:pfam09731 441 KAQQ 444
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1500-1923 |
3.81e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1500 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQferdlqgrdeq 1579
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQ----------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1580 seEKKKQLVRQVREMEAELEderkQRSMAVA-ARKKLEMdlkdLEAHIDSANKNRDEaikqlrkLQAQMKDCMRELD--D 1656
Cdd:PRK04863 348 --EKIERYQADLEELEERLE----EQNEVVEeADEQQEE----NEARAEAAEEEVDE-------LKSQLADYQQALDvqQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1657 TRASREEILAQAKENEKKL-KSMEAEMIQLQEELAAAERAKRQAQQERDEL------ADEIANSSGKgalALEEKRRLEA 1729
Cdd:PRK04863 411 TRAIQYQQAVQALERAKQLcGLPDLTADNAEDWLEEFQAKEQEATEELLSLeqklsvAQAAHSQFEQ---AYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1730 RIAQLEEELEEEQGNTELINDRLKKANLQidQINTDLN-LERSHAQknenaRQQLERQNKELKVKLQEMEgtvkskykAS 1808
Cdd:PRK04863 488 EVSRSEAWDVARELLRRLREQRHLAEQLQ--QLRMRLSeLEQRLRQ-----QQRAERLLAEFCKRLGKNL--------DD 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1809 ITALEAKIAQLEEQLD--NETKERQAAckqvRRTEkkLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEA 1886
Cdd:PRK04863 553 EDELEQLQEELEARLEslSESVSEARE----RRMA--LRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS 626
|
410 420 430
....*....|....*....|....*....|....*..
gi 12667788 1887 QRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1923
Cdd:PRK04863 627 QDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1520-1907 |
4.00e-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: 45.40 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1520 VHELEKSKRAleqqVEEMKTQLEELE-DELQATED---AKLRLEvnlqamkaqfERDLQGRDEQSEEKKkqlvrqvreme 1595
Cdd:pfam05701 69 LEELESTKRL----IEELKLNLERAQtEEAQAKQDselAKLRVE----------EMEQGIADEASVAAK----------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1596 AELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQ-------LRKLQAQMKDCMRELDDTRASREeiLAQA 1668
Cdd:pfam05701 124 AQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRaeeavsaSKEIEKTVEELTIELIATKESLE--SAHA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1669 KENEKKLKSMEAEMIQLQEELAAaERAKRQAQQERDELADEIANS-------SGKGALALEEKRRLEARIAQLEEELEEE 1741
Cdd:pfam05701 202 AHLEAEEHRIGAALAREQDKLNW-EKELKQAEEELQRLNQQLLSAkdlksklETASALLLDLKAELAAYMESKLKEEADG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1742 QGNTELINDRLKKA-----------NLQIDQINTDLNLERSHAqknENARQQLERQNKELkVKLQEMEGtvkskyKASIT 1810
Cdd:pfam05701 281 EGNEKKTSTSIQAAlasakkeleevKANIEKAKDEVNCLRVAA---ASLRSELEKEKAEL-ASLRQREG------MASIA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1811 aleakIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRAN 1890
Cdd:pfam05701 351 -----VSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVE 425
|
410
....*....|....*..
gi 12667788 1891 ASRRKLQRELEDATETA 1907
Cdd:pfam05701 426 SRLEAVLKEIEAAKASE 442
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
942-1238 |
4.26e-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: 44.80 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 942 QQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKL 1021
Cdd:pfam15905 38 QPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKD-QKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1022 KNKHEAMITDLEERLRrEEKQRQELEKTRRKLEGDSTDLSDQIAELqaqiaelkMQLAKK-EEELQAALARVEEEAAQKN 1100
Cdd:pfam15905 117 KTSLSASVASLEKQLL-ELTRVNELLKAKFSEDGTQKKMSSLSMEL--------MKLRNKlEAKMKEVMAKQEGMEGKLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1101 MALKKIRELESQISELQEDLESERASRNKAEKQKRDLGE---ELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE 1177
Cdd:pfam15905 188 VTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEyitELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLE 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1178 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQ 1238
Cdd:pfam15905 268 EKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1537-1726 |
4.69e-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: 43.76 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1537 MKTQLEELEDeLQATEDAKLRLEVNLQAMKAQFERdlqgrdeqSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLE 1616
Cdd:COG1579 2 MPEDLRALLD-LQELDSELDRLEHRLKELPAELAE--------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1617 MDLKDLEAHIDSANKNRD-EAI-KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1694
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEyEALqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|..
gi 12667788 1695 AKRQAQQERDELADEIANSSGKGALALEEKRR 1726
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
971-1160 |
4.72e-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: 43.51 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 971 AKLKKLEEEQIILE----DQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR-QE 1045
Cdd:pfam04012 15 EGLDKAEDPEKMLEqairDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEkKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1046 LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARveEEAAQKNMALKK----------IRELEsQISE 1115
Cdd:pfam04012 95 LEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTslgslstssaTDSFE-RIEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 12667788 1116 LQEDLESERASRNKAEkQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:pfam04012 172 KIEEREARADAAAELA-SAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1656-1954 |
5.50e-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: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1656 DTRASREEILAQAKENEKKLKSMEAEMIQLQEElAAAERAKRQAQQERDELADEIANSSGKgaLALEEKRRLEAriaQLE 1735
Cdd:NF012221 1532 DNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALET---NGQ 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1736 EELEEEQGNTELINDRLKKANLQIDQINTDLNlershaQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAK 1815
Cdd:NF012221 1606 AQRDAILEESRAVTKELTTLAQGLDALDSQAT------YAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQR 1679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1816 IAQLEEQLDNETKERQAAckqVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAeeeaqrANASRRK 1895
Cdd:NF012221 1680 HVDNQQKVKDAVAKSEAG---VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAA------ANDAQSR 1750
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1896 LQRELEDATETADAMNREVSSLknKLRRGDLPfvvprrmARKGA-GDG-SDEEVDGKADGA 1954
Cdd:NF012221 1751 GEQDASAAENKANQAQADAKGA--KQDESDKP-------NRQGAaGSGlSGKAYSVEGVAE 1802
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1335-1581 |
5.68e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1335 EDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLekt 1414
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1415 kTRLQQELDDLLVdldhqrqsacnlekkqkKFDQLLAeektiSAKYAEERDRAEAEAREKETKalslARALEEAMEQKAE 1494
Cdd:COG3883 92 -ARALYRSGGSVS-----------------YLDVLLG-----SESFSDFLDRLSALSKIADAD----ADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1495 LERLNKQFRTEMEDLMSSKDdvgksvhELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQ 1574
Cdd:COG3883 145 LEAKKAELEAKLAELEALKA-------ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
....*..
gi 12667788 1575 GRDEQSE 1581
Cdd:COG3883 218 AAAAAAA 224
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
860-1193 |
5.99e-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: 44.73 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 860 KQLAAENRLTEMETLQSQL------MAEKLQLQEQLQAETELCAEAE----ELRARLTAKKQELEEI--CHDLEARVEEE 927
Cdd:pfam05557 123 AELELQSTNSELEELQERLdllkakASEAEQLRQNLEKQQSSLAEAEqrikELEFEIQSQEQDSEIVknSKSELARIPEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 928 EERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlekvtteaKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTN 1007
Cdd:pfam05557 203 EKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE--------REEKYREEAATLELEKEKLEQELQSWVKLAQDTGLN 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1008 LTEEEEKSKSLAKLKNK---HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA---KK 1081
Cdd:pfam05557 275 LRSPEDLSRRIEQLQQReivLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLlltKE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1082 EEELQAALARVEEEAAQKNMALKK---IRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELedTLDSTAAQ 1158
Cdd:pfam05557 355 RDGYRAILESYDKELTMSNYSPQLlerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL--QALRQQES 432
|
330 340 350
....*....|....*....|....*....|....*
gi 12667788 1159 QELRSKREQEVNILKKTLEEeaktHEAQIQEMRQK 1193
Cdd:pfam05557 433 LADPSYSKEEVDSLRRKLET----LELERQRLREQ 463
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1006-1270 |
6.14e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1006 TNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIA-------ELQAQIAELKMQL 1078
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQelrekrdELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1079 AKKEEELQAALARVEE---EAAQKNMALKKIRELESQISELQEDLESERASRNKAEK---QKRDLGEELEALKTELEDTL 1152
Cdd:COG1340 81 DELNEKLNELREELDElrkELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKElveKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1153 DSTAAQQELRSKREQ--EVNILKKTLEEEAKTHEAQIQEMRQKH---SQAVEELAEQLEQTKRVKANLEKAKQTLENERG 1227
Cdd:COG1340 161 KLKELRAELKELRKEaeEIHKKIKELAEEAQELHEEMIELYKEAdelRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 12667788 1228 ELANEVKVLLQGKGDSEHKRKK--VEAQLQELQVKFNEGERVRTE 1270
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLKKGEKLTTE 285
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
969-1112 |
6.83e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 969 TEAKLKKLEEEQIILEDQNcKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEK 1048
Cdd:PRK01156 617 IDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKA 695
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1049 TRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKeEELQAALARVEE--EAAQKNMALKKIRELESQ 1112
Cdd:PRK01156 696 NRARLESTIEILRTRINELSDRINDINETLESM-KKIKKAIGDLKRlrEAFDKSGVPAMIRKSASQ 760
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
839-1073 |
7.15e-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: 43.98 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 839 QVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcaeaEELRARLTAKKQELEEich 918
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI----------AELRAELEAQKEELAE--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 919 dlearveeeeercqHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeqiiLEDQNCKLAKEKKLLE 998
Cdd:COG4942 109 --------------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 999 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAE 1073
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAA 238
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1527-1699 |
7.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1527 KRALEQQVEEMKTQ----LEELEDELQATEDAKLrLEVN--LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELED 1600
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1601 ERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDcmrelddtrASREEILAQAKEnekKLKSMEA 1680
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEILLEKVEE---EARHEAA 172
|
170
....*....|....*....
gi 12667788 1681 EMIQLQEELAAAErAKRQA 1699
Cdd:PRK12704 173 VLIKEIEEEAKEE-ADKKA 190
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1538-1829 |
7.33e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1538 KTQLEELEDELQATEDAKLRLEvnlqAMKAQFERDLQGRdeqsEEKKKQLVRQVRemeAELEDERkQRSMAVAARKKLEM 1617
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFE----ARQARLEREKAAR----EARHKKAAEARA---AKDKDAV-AAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1618 DLKDLEAHIDSANKNRDEAIKQLRKLQAqmkdcmrelddtRASREEILAQAKENEKKLKsmeaemIQlqeelAAAERAK- 1696
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQA------------RARQAEKQAAAAADPKKAA------VA-----AAIARAKa 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1697 RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIdqintdlnlershaqkn 1776
Cdd:PRK05035 560 KKAAQQAANAEAEEEVDPKKAAVA-AAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAI----------------- 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 12667788 1777 enARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKE 1829
Cdd:PRK05035 622 --ARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1037-1408 |
7.55e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1037 RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISEL 1116
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1117 QEDLESERASRNKAEkqkrdlgEELEALKTE---LEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQK 1193
Cdd:COG4372 86 NEQLQAAQAELAQAQ-------EELESLQEEaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1194 hsqaVEELAEQLEQTKRVKANLEKAKQTLE-NERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA 1272
Cdd:COG4372 159 ----LESLQEELAALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1273 DKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAK 1352
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1353 HNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAY 1408
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
905-1489 |
8.65e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 905 RLTAKKQELEEICHDLEARVEEEeercQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILE 984
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 985 D---QNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDleerlrREEKQRQELeKTRRKLEGDSTDLS 1061
Cdd:PRK01156 239 SalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIND------PVYKNRNYI-NDYFKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1062 DQIAELQAQIAELKmQLAKKEEELQAALARVEEEAAQKNmalkkirELESQISELQEDLESERASRNKAEKQKRDLGE-- 1139
Cdd:PRK01156 312 QILSNIDAEINKYH-AIIKKLSVLQKDYNDYIKKKSRYD-------DLNNQILELEGYEMDYNSYLKSIESLKKKIEEys 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1140 -ELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQkHSQAVEELAEQL------------- 1205
Cdd:PRK01156 384 kNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRE-NLDELSRNMEMLngqsvcpvcgttl 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1206 --EQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEA-QLQELQVKFNEGERVRTELADKVTKLQvEL 1282
Cdd:PRK01156 463 geEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARADLEDIKIKIN-EL 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1283 DNVTGLLSQSDSKSSKLtkDFSALESQLQDTQELLQEENrqklslSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATL 1362
Cdd:PRK01156 542 KDKHDKYEEIKNRYKSL--KLEDLDSKRTSWLNALAVIS------LIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1363 HAQVADMKKKMEDSVGCLET----AEEVKR---KLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQS 1435
Cdd:PRK01156 614 KSYIDKSIREIENEANNLNNkyneIQENKIlieKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA 693
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1436 ACNLEKKQKKFDQLLAEEKTISAKYAEERDRaeAEAREKETKALSLARALEEAM 1489
Cdd:PRK01156 694 KANRARLESTIEILRTRINELSDRINDINET--LESMKKIKKAIGDLKRLREAF 745
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1001-1226 |
8.76e-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: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1001 IAEFTTNLTEEEEKSKSLAKlknkhEAMITDLEE--------RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA 1072
Cdd:pfam15709 302 TFVVTGNMESEEERSEEDPS-----KALLEKREQekasrdrlRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMRE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1073 ELKMQLAKKEEELQAALARVEEEAAQknmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTL 1152
Cdd:pfam15709 377 ELELEQQRRFEEIRLRKQRLEEERQR--------QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAE 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1153 DSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVkANLEKAKQTLENER 1226
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARL-ALEEAMKQAQEQAR 521
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1663-1837 |
8.83e-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: 42.99 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1663 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEEKRRLEARIAQLEEELEEEQ 1742
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-------LEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1743 GNTElindrLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKykasITALEAKIAQLEEQ 1822
Cdd:COG1579 87 NNKE-----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----KAELDEELAELEAE 157
|
170
....*....|....*
gi 12667788 1823 LDNETKERQAACKQV 1837
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
833-1131 |
8.97e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 833 KVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETL---QSQLMAEKLQLQEQLQAETELCAEAEELRARLTAK 909
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 910 KQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKlqlekvttEAKLKKLEEEQIILEDQNCK 989
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--------AEALKKEAEEAKKAEELKKK 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 990 LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDqiaELQA 1069
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE---ELDE 1787
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12667788 1070 QIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELEsqISELQEDLESERASRNKAE 1131
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME--DSAIKEVADSKNMQLEEAD 1847
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1304-1733 |
1.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1304 SALESQLQ-DTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEeeakHNLEKQIATLHAQVADMKKKmedsvgcLET 1382
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAE-------LEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1383 AEEVKRKLQKDLEgLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAE 1462
Cdd:COG4717 114 LREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1463 ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMED-----------------------------LMSSK 1513
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaaleerlkearlllliaaallallglggsLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1514 DDVGK------SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQL 1587
Cdd:COG4717 273 LTIAGvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1588 VRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIdsanknrdEAIKQLRKLQAQMKDCMRELDDTRASREEILAQ 1667
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL--------EQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1668 AKENEkklksMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGAL--ALEEKRRLEARIAQ 1733
Cdd:COG4717 425 LDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRE 487
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1468-1879 |
1.19e-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: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1468 EAEAREKETKALSLARALEE--AMEQKAELERLNKQFRTEMEDLMSSK-DDVGKSVHELE---------KSKRAL---EQ 1532
Cdd:pfam06160 14 ELEERKNELMNLPVQEELSKvkKLNLTGETQEKFEEWRKKWDDIVTKSlPDIEELLFEAEelndkyrfkKAKKALdeiEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1533 QVEEMKTQLEELEDELQA--TEDAKLRLEVN-LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELE--DERKQRSM 1607
Cdd:pfam06160 94 LLDDIEEDIKQILEELDEllESEEKNREEVEeLKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSqfEELTESGD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1608 AVAARK---KLEMDLKDLEAHIDS-------ANKNRDEAIKQLRKLQAQMKDCMRELDDtrasrEEILAQAKENEKKLKS 1677
Cdd:pfam06160 174 YLEAREvleKLEEETDALEELMEDipplyeeLKTELPDQLEELKEGYREMEEEGYALEH-----LNVDKEIQQLEEQLEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1678 MEAEMIQLqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANL 1757
Cdd:pfam06160 249 NLALLENL--ELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEH--------------AEEQNKELKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1758 QIDQINTDLNL---ERSHAQKNENARQQLERQNKELKVKLQEMEGT---VKSKYK---ASITALEAKIAQLEEQLDNETK 1828
Cdd:pfam06160 313 ELERVQQSYTLnenELERVRGLEKQLEELEKRYDEIVERLEEKEVAyseLQEELEeilEQLEEIEEEQEEFKESLQSLRK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1829 ERQAACKQVRRTEKKLKDVLLQVddERRN----AEQYKDQADKASTRLKQLKRQL 1879
Cdd:pfam06160 393 DELEAREKLDEFKLELREIKRLV--EKSNlpglPESYLDYFFDVSDEIEDLADEL 445
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
972-1145 |
1.21e-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: 43.08 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 972 KLKKLEEEQIILEDQNCKL-AKE------KKLLEDRIAEFTTNLT----EEEEKSKSLAKLKNKHEAmITDLEERLRREE 1040
Cdd:smart00787 110 DVKLLMDKQFQLVKTFARLeAKKmwyewrMKLLEGLKEGLDENLEglkeDYKLLMKELELLNSIKPK-LRDRKDALEEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1041 KQRQELEKTRRKLEGDSTD-LSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkirELESQISELQED 1119
Cdd:smart00787 189 RQLKQLEDELEDCDPTELDrAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKS-------ELNTEIAEAEKK 261
|
170 180
....*....|....*....|....*.
gi 12667788 1120 LESERASRNKAEKQKRDLGEELEALK 1145
Cdd:smart00787 262 LEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1533-1921 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1533 QVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLvRQVREMEAELEDERKQRSMAVAAR 1612
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI-RLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1613 KK----LEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEaemiQLQEE 1688
Cdd:pfam05557 82 KKyleaLNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE----QLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1689 LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLeARIAQLEEELeeeqgntelinDRLKKANLQIDQINTDLNL 1768
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKEL-----------ERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1769 ershaqknenarqqLERQNKELKVKLQEMEgtvksKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEK-KLKDV 1847
Cdd:pfam05557 226 --------------LKEEVEDLKRKLEREE-----KYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDlSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1848 LLQVDDERRNAEQYKDQADKASTR---------LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLK 1918
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEkarreleqeLAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYD 366
|
...
gi 12667788 1919 NKL 1921
Cdd:pfam05557 367 KEL 369
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1047-1277 |
1.25e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1047 EKTRRKLEGDSTDLSDQIAELQAQiaelKMQLAKKEEELQAALARVEEeaaqknmalkkirelesqiseLQEDLEseras 1126
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEEL----ERELEQKAEEAEALLKEAEK---------------------LKEELE----- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1127 rnkaeKQKRDLGEELEALKTELEDtldstAAQQELRSKREQEVNILKKTLEEEAKTHEA----QIQEMRQKHSQAVEELA 1202
Cdd:PRK00409 555 -----EKKEKLQEEEDKLLEEAEK-----EAQQAIKEAKKEADEIIKELRQLQKGGYASvkahELIEARKRLNKANEKKE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1203 EQLEQTKRVKANLEKakqtlenerGElanEVKVL-LQGKGDSEHKRKKVEAQLQE----LQVKFNEGERVRTELADKVTK 1277
Cdd:PRK00409 625 KKKKKQKEKQEELKV---------GD---EVKYLsLGQKGEVLSIPDDKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKK 692
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1050-1179 |
1.33e-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: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1050 RRKLEGDSTdlSDQIAELQAQIAELKMQlakkeeelQAALARVEEEAAQKnmalkKIRELESQISELQEDLESERAsRNK 1129
Cdd:COG0542 401 RVRMEIDSK--PEELDELERRLEQLEIE--------KEALKKEQDEASFE-----RLAELRDELAELEEELEALKA-RWE 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 12667788 1130 AEKQkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEE 1179
Cdd:COG0542 465 AEKE---LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1029-1168 |
1.33e-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: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1029 ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK-KIR 1107
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELA 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1108 ELESQISELQEDLES-------ERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQE 1168
Cdd:pfam12795 160 ALKAQIDMLEQELLSnnnrqdlLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1455-1909 |
1.42e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1455 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV 1534
Cdd:COG5278 72 TGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALM 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1535 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKK 1614
Cdd:COG5278 152 DEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1615 LEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1694
Cdd:COG5278 232 LELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1695 AKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQ 1774
Cdd:COG5278 312 AAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1775 KNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDE 1854
Cdd:COG5278 392 VLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1855 RRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1909
Cdd:COG5278 472 AALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1058-1135 |
1.42e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 1.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1058 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKR 1135
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
1032-1160 |
1.45e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 43.30 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1032 LEERLRREEKQR--QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlakKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:PRK00247 288 AEQRAQYREKQKekKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKT---RTAEKNEAKARKKEIAQKRRAAEREINRE 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1110 ESQisELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:PRK00247 365 ARQ--ERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQV 413
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
908-1390 |
1.47e-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: 43.52 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 908 AKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEE-SARQKLQLEKVtteakLKKLEEEQIILEDQ 986
Cdd:pfam05622 7 EEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTpGGKKYLLLQKQ-----LEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 987 NCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAmitdLEERLRREEKQRQELEKTRRKLEgDSTDLSDQIAE 1066
Cdd:pfam05622 82 RDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDI----LRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1067 LQAQIAELKMQLAKKEEELQAAlarveeeaaqkNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKT 1146
Cdd:pfam05622 157 LEERNAEYMQRTLQLEEELKKA-----------NALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1147 EledtldstaaQQELRSKREqevnILKKTLEE-----EAKTHEAQIQEMRQKHSQAVEELAEQLeQTKRVKANLEKakqt 1221
Cdd:pfam05622 226 E----------KERLIIERD----TLRETNEElrcaqLQQAELSQADALLSPSSDPGDNLAAEI-MPAEIREKLIR---- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1222 lenergeLANEVKVL-LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKssklT 1300
Cdd:pfam05622 287 -------LQHENKMLrLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSK----A 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1301 KDFSALESQLQDTQELLQEENRQklsLSTKLKQVEDEKNSFREQLEEEEEakhNLEkqiATLHAQVADMKKKMEDSVGCL 1380
Cdd:pfam05622 356 EDSSLLKQKLEEHLEKLHEAQSE---LQKKKEQIEELEPKQDSNLAQKID---ELQ---EALRKKDEDMKAMEERYKKYV 426
|
490
....*....|
gi 12667788 1381 ETAEEVKRKL 1390
Cdd:pfam05622 427 EKAKSVIKTL 436
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1169-1497 |
1.49e-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: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1169 VNILKKTLEEEAKTHEAQIQEMRQKHSQaveelaEQLEQTKRVKA-NLEKAKQTLENERgelANEVKVLLQGKGDSEHKR 1247
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQ------ERLRQEKEEKArEVERRRKLEEAEK---ARQAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1248 KKVEAQLQ----ELQVKFNEGERVRTEladkvtKLQVELDNVTGLlsqsdsksskltkdfsaleSQLQDTQELLQEENRQ 1323
Cdd:pfam17380 342 MAMEREREleriRQEERKRELERIRQE------EIAMEISRMREL-------------------ERLQMERQQKNERVRQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1324 KLSLSTKLKQVEDEKN-SFREQLEEEEEAKHNLEKqiatlhAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHE 1402
Cdd:pfam17380 397 ELEAARKVKILEEERQrKIQQQKVEMEQIRAEQEE------ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1403 E---KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR------- 1472
Cdd:pfam17380 471 ErkrKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRkqqemee 550
|
330 340
....*....|....*....|....*....
gi 12667788 1473 ----EKETKALSLARALEEAMEQKAELER 1497
Cdd:pfam17380 551 rrriQEQMRKATEERSRLEAMEREREMMR 579
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1460-1640 |
1.55e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1460 YAEERDRAEAEAREKEtkalslARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1539
Cdd:PRK12705 26 KKRQRLAKEAERILQE------AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1540 qLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVrqVREMEAELEDERKQRSMAVAARKKLEMDL 1619
Cdd:PRK12705 100 -LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLL--LKLLDAELEEEKAQRVKKIEEEADLEAER 176
|
170 180
....*....|....*....|.
gi 12667788 1620 KDLEAHIDSANKNRDEAIKQL 1640
Cdd:PRK12705 177 KAQNILAQAMQRIASETASDL 197
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1395-1632 |
1.64e-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: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1395 EGLSQRHEEKVAAYDK--LEKTKTRLQQELddllvdldhQRQSAcNLEKKQKKFDQllAEEKTISAKYAEERDRAEAEAR 1472
Cdd:NF012221 1549 KHAKQDDAAQNALADKerAEADRQRLEQEK---------QQQLA-AISGSQSQLES--TDQNALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1473 EKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMssKDDVGKSvheLEKSKRALEQQVEEMKTQleeLEDELQATE 1552
Cdd:NF012221 1617 AVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQEQ---LDDAKKISGKQLADAKQR---HVDNQQKVK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1553 DAKLRLEVNL-QAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAElEDERKQRSMAVAARKKLEMDLKDLEAHIDSANK 1631
Cdd:NF012221 1689 DAVAKSEAGVaQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQ-QAESDANAAANDAQSRGEQDASAAENKANQAQA 1767
|
.
gi 12667788 1632 N 1632
Cdd:NF012221 1768 D 1768
|
|
| Cortex-I_coil |
pfam09304 |
Cortexillin I, coiled coil; Members of this family are predominantly found in the ... |
1050-1153 |
1.67e-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: 39.99 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1050 RRKLEGDSTDLSDQIAELQAQIAELKM---QLAKKEEELQAALARVEEEAAQKNmalKKIRELESQISELQEDLESERAS 1126
Cdd:pfam09304 4 KERLEASKNSLANKLAGLENSLESEKTsreQLIKQKDELESLLASLEQENAERE---KRLRELEAKLDEALKNLELEKLA 80
|
90 100
....*....|....*....|....*..
gi 12667788 1127 RNKAEKQKRDLGEELEALKTELEDTLD 1153
Cdd:pfam09304 81 RMELESRLSKTEKDKAILELKLAEALD 107
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1110-1326 |
1.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1110 ESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELrskreqevnilkKTLEEEAKTHEAQIQE 1189
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE------LQAEL------------EALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1190 MRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER-GELANEVKVLLQ-GKGDSE------HKRKKVEAQLQELQVKF 1261
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKiADADADlleelkADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1262 NEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
856-1236 |
1.86e-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: 43.29 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 856 KVREKQlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQ 935
Cdd:pfam12128 475 RAREEQ---EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 936 AEKKKMQQNIQELEEQLEEEESARQ-------KLQLEKV----------TTEAKLKKLEE----EQIILEDQNCKLAKEK 994
Cdd:pfam12128 552 GKVISPELLHRTDLDPEVWDGSVGGelnlygvKLDLKRIdvpewaaseeELRERLDKAEEalqsAREKQAAAEEQLVQAN 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 995 KLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE----EKQRQELEKTRRKLEGDSTDLSDQIaelQAQ 1070
Cdd:pfam12128 632 GELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERkdsaNERLNSLEAQLKQLDKKHQAWLEEQ---KEQ 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1071 IAELKMQLAKK----EEELQAALARVEEEAAQKNMALKkireleSQISELQEDLESERASRNKAEKQKRDLGEELEALKT 1146
Cdd:pfam12128 709 KREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAK------AELKALETWYKRDLASLGVDPDVIAKLKREIRTLER 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1147 ELEDTldstaaqqelrSKREQEV----NILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL 1222
Cdd:pfam12128 783 KIERI-----------AVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKAS 851
|
410
....*....|....
gi 12667788 1223 ENERGELANEVKVL 1236
Cdd:pfam12128 852 EKQQVRLSENLRGL 865
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1052-1206 |
1.98e-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: 41.10 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1052 KLEGDSTDLSDQIAELQAQIA----ELKMQLAKKEEELQAALARVEEEAAQK---------NMALKKIRELESQISELQE 1118
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGpvaqELVDRLEKETEALRERLQKDLEEVRAKlepyleelqAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1119 DLEsERASRnKAEKQKRDLGEELEALKTELEDTLDSTAAQ-----QELRSKREQEVNILKKTLEEEAKTHEAQ----IQE 1189
Cdd:pfam01442 81 ELR-KRLNA-DAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQE 158
|
170
....*....|....*..
gi 12667788 1190 MRQKHSQAVEELAEQLE 1206
Cdd:pfam01442 159 LREKLEPQAEDLREKLD 175
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1053-1662 |
2.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1053 LEGDSTDLSDQIAELQAQIaelkmqlakkeeelqaalarvEEEAAQKNMALKKIRELESQIselqedleserasrNKAEK 1132
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQI---------------------ADDEKSHSITLKEIERLSIEY--------------NNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1133 QKRDLGEELEALKTELE--DTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEaqiqemrqkhSQAVEELAEQLEQTKR 1210
Cdd:PRK01156 233 DYNNLKSALNELSSLEDmkNRYESEIKTAESDLSMELEKNNYYKELEERHMKII----------NDPVYKNRNYINDYFK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1211 VKANLEKAKQTLENERGELanevkvllqgkgDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLS 1290
Cdd:PRK01156 303 YKNDIENKKQILSNIDAEI------------NKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1291 QSDSKSSKL------TKDFSALESQLQDTQELLQEE-NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLH 1363
Cdd:PRK01156 371 SIESLKKKIeeysknIERMSAFISEILKIQEIDPDAiKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1364 AQVAdmkkkmeDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVaayDKLEKTKTRLQQElddllvdLDHQRQSACNLEKkq 1443
Cdd:PRK01156 451 GQSV-------CPVCGTTLGEEKSNHIINHYNEKKSRLEEKI---REIEIEVKDIDEK-------IVDLKKRKEYLES-- 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1444 KKFDQLLAEEKTISAKYAEERD--RAEAEAREKETKALSLARALE----EAMEQKAE--LERLNKQFRTEMEDLMSSKDD 1515
Cdd:PRK01156 512 EEINKSINEYNKIESARADLEDikIKINELKDKHDKYEEIKNRYKslklEDLDSKRTswLNALAVISLIDIETNRSRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1516 VGKSVHELEKSKRALEQQVEEMKT----QLEELEDELQATEDAKLRLEVNLQAMKA------QFERDLQGRDEQsEEKKK 1585
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIEKlrgkidNYKKQIAEIDSI-IPDLK 670
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1586 QLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRELDDTRASRE 1662
Cdd:PRK01156 671 EITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS----DRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1603-1897 |
2.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1603 KQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1682
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1683 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRlkKANLQIDQI 1762
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1763 NTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEK 1842
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1843 KLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQ 1897
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1035-1167 |
2.12e-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: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1035 RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKkeeeLQAALARVEEEAAQKNMALKKIRELESQIS 1114
Cdd:pfam00529 76 RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ----AQIDLARRRVLAPIGGISRESLVTAGALVA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1115 ELQEDLESERASRNKAEKQKRDLGEELEAL--KTELEDTLDSTAAQQELRSKREQ 1167
Cdd:pfam00529 152 QAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEAEAELKLAKLD 206
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
960-1248 |
2.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 960 QKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE 1039
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1040 EKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAalARVEEEAAQKNMALKKIRELESQISELQED 1119
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA--LEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1120 LESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVE 1199
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 12667788 1200 ELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK 1248
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1057-1279 |
2.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1057 STDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQIS-------ELQEDLESERASRNK 1129
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQelrekrdELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1130 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSK-----REQEVNILKKTLE----EEAKTHEAQIQEMRQKHSQAvEE 1200
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEierleWRQQTEVLSPEEEkelvEKIKELEKELEKAKKALEKN-EK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12667788 1201 LAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQ 1279
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1198-1331 |
2.27e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1198 VEELAEQLEQTKRVKANLEkakQTLENERGELANevkvllqgkgdSEHKRKKVEAQLqelqvkfNEGERVRTELADKVTK 1277
Cdd:PRK09039 62 IAELADLLSLERQGNQDLQ---DSVANLRASLSA-----------AEAERSRLQALL-------AELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12667788 1278 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELL-------QEENRQKLSLSTKL 1331
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQAKIADLGRRL 181
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1075-1225 |
2.38e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1075 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDS 1154
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQ 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1155 TAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEmrqkhsQAVEELAEQL------EQTKRVKANLEKAKQTLENE 1225
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPE------QARKLLLKLLdaeleeEKAQRVKKIEEEADLEAERK 177
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1453-1603 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1453 EKTISAKYAEERDRAEAEAREKETKAL-SLARALEEAMEQ------------KAELERLNKQFRTEM----------EDL 1509
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKRCQALLqELSAPLEEKISQgsysvpggyqlyLEDREKLVEKYRQVPrkgvkaeevlQEF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1510 MSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDL-QGRDEQSEEKKKQLV 1588
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLrQLKEKMEEERENLLK 255
|
170
....*....|....*
gi 12667788 1589 RQVREMEAELEDERK 1603
Cdd:cd16269 256 EQERALESKLKEQEA 270
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1050-1297 |
2.54e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1050 RRKLEGDSTDLS----------DQIAELQAQIAELKMQL----------AKKEEELQA-ALARVEEEAAQKNMALKKIRE 1108
Cdd:PHA02562 152 RRKLVEDLLDISvlsemdklnkDKIRELNQQIQTLDMKIdhiqqqiktyNKNIEEQRKkNGENIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1109 LESQISELQEDL-------ESERASRNKAEKQKRDLGEELEALKTEL----EDTLDSTAAQQelrskREQEVNILKKtLE 1177
Cdd:PHA02562 232 IKAEIEELTDELlnlvmdiEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQ-----ISEGPDRITK-IK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1178 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRV---KANLEKAKQTLENERGELanevkvllqgkgdsehkrKKVEAQL 1254
Cdd:PHA02562 306 DKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKA------------------KKVKAAI 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 12667788 1255 QELQVKF----NEGERVRTELADKVTKLQ------VELDNVTGLLSQSDSKSS 1297
Cdd:PHA02562 368 EELQAEFvdnaEELAKLQDELDKIVKTKSelvkekYHRGIVTDLLKDSGIKAS 420
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1632-1785 |
2.57e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1632 NRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEnekKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIA 1711
Cdd:PRK09039 50 GKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRA---SLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELD 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1712 NSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLerSHAQKNenarQQLER 1785
Cdd:PRK09039 127 SEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV--ALAQRV----QELNR 194
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1490-1638 |
2.81e-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: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1490 EQKAELERLNKQfrtEMEDLMSSKDDVgksVHELEKSKRALEQ---QVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK 1566
Cdd:pfam05911 677 DLKTEENKRLKE---EFEQLKSEKENL---EVELASCTENLEStksQLQESEQLIAELRSELASLKESNSLAETQLKCMA 750
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12667788 1567 AQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIK 1638
Cdd:pfam05911 751 ESYE-DLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDADQEDKK 821
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1103-1406 |
2.99e-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: 42.42 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1103 LKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELE----------ALKTELEDTLDSTAAQQELRSKREQEvniL 1172
Cdd:pfam17380 274 LLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVErrrkleeaekARQAEMDRQAAIYAEQERMAMERERE---L 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1173 KKTLEEEAKTHEAQIQE----MRQKHSQAVEELA-EQLEQTKRVKANLEKAKQT--LENERGELANEVKVLLQGKGDSEH 1245
Cdd:pfam17380 351 ERIRQEERKRELERIRQeeiaMEISRMRELERLQmERQQKNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1246 KRKKVEAQLQElQVKFNEGERVRTELADKVTKLQVELDNvtgllsQSDSKSSKLTKDFSALESQL--------------Q 1311
Cdd:pfam17380 431 EARQREVRRLE-EERAREMERVRLEEQERQQQVERLRQQ------EEERKRKKLELEKEKRDRKRaeeqrrkilekeleE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1312 DTQELLQEENRQKLSlstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQ 1391
Cdd:pfam17380 504 RKQAMIEEERKRKLL----EKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMR 579
|
330
....*....|....*
gi 12667788 1392 KDLEGLSQRHEEKVA 1406
Cdd:pfam17380 580 QIVESEKARAEYEAT 594
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1679-1846 |
3.01e-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: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1679 EAEMIQLQEELAAAERAKRQAQQERDELadeianssgkgalaleekRRLEARIAQLEEELEEEQGNTELINDRLKKANLQ 1758
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRL------------------QALESELAISRQDYDGATAQLRAAQAAVKAAQAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1759 IDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSK---YKASITALEAKIAQLEEQLDNETKERQAACK 1835
Cdd:pfam00529 119 LAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLdqiYVQITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
170
....*....|.
gi 12667788 1836 QVRRTEKKLKD 1846
Cdd:pfam00529 199 ELKLAKLDLER 209
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
882-1107 |
3.22e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 882 KLQLQEQLQAETELCAEAEELRARLTAKKQELEEIchDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQK 961
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEF--RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 962 LQLEKVTTEAKLKKLEEEQIILEdqnckLAKEKKLLEDRIAEFTTNLTEE--------EEKSKSLAKLKNKHEAMITDLE 1033
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNhpdvialrAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1034 ERLRREEKQRQELEKTRRKLEGDStdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIR 1107
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
958-1219 |
3.29e-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: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 958 ARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLED-------------RIAEFTTN----LTEEEEKSKSLAK 1020
Cdd:TIGR01612 1556 AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflKISDIKKKindcLKETESIEKKISS 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1021 LK-NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSdqiaELQAQIAELKMQLAKKEEELQAALARVEEEAAQK 1099
Cdd:TIGR01612 1636 FSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIA 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1100 NMalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSkreqevNILkKTLEEE 1179
Cdd:TIGR01612 1712 NK-----EEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIA------GCL-ETVSKE 1779
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 12667788 1180 AKTHEaqiqEMRQKHSQAVEELAEQLEQTKRVKANLEKAK 1219
Cdd:TIGR01612 1780 PITYD----EIKNTRINAQNEFLKIIEIEKKSKSYLDDIE 1815
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1438-1730 |
3.43e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1438 NLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFrtemEDLMSSKDDVG 1517
Cdd:PRK04778 120 DIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQF----VELTESGDYVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1518 KSVH--ELEKSKRALEQQVEEMKTQLEELEDELQA------------TED----AKLRLEVNLQAMKAQFERDL----QG 1575
Cdd:PRK04778 196 AREIldQLEEELAALEQIMEEIPELLKELQTELPDqlqelkagyrelVEEgyhlDHLDIEKEIQDLKEQIDENLalleEL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1576 RDEQSEEKKKQLVRQVREMEAELEDErkqrsmaVAARKKLEMDLKDLEAHIDSANKNRDEAI------------------ 1637
Cdd:PRK04778 276 DLDEAEEKNEEIQERIDQLYDILERE-------VKARKYVEKNSDTLPDFLEHAKEQNKELKeeidrvkqsytlnesele 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1638 ------KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIA 1711
Cdd:PRK04778 349 svrqleKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLH 428
|
330
....*....|....*....
gi 12667788 1712 NSsgkgalaleeKRRLEAR 1730
Cdd:PRK04778 429 EI----------KRYLEKS 437
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
865-1154 |
3.48e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 865 ENRLTEMETLQSQLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQN 944
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELK---ELAEKRDELNAQVKELREEAQE----LREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 945 IQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEdriaefttnlteeeeKSKSLAKLKNK 1024
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVE---------------KIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1025 HEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK 1104
Cdd:COG1340 152 AKKAL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 12667788 1105 KIRELESQISELQEDLESERASRNKAEKQKRDlgEELEALKTELEDTLDS 1154
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKK 278
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1432-1591 |
3.86e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1432 QRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARalEEAMEQKAELERLNKQFRTEMEDlms 1511
Cdd:PRK00409 532 LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK--KEADEIIKELRQLQKGGYASVKA--- 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1512 skddvgksvHELEKSKRALEQQVEEMKTQL---EELEDELQATEDAKLR--------------LEVNLQA----MKAQfE 1570
Cdd:PRK00409 607 ---------HELIEARKRLNKANEKKEKKKkkqKEKQEELKVGDEVKYLslgqkgevlsipddKEAIVQAgimkMKVP-L 676
|
170 180
....*....|....*....|.
gi 12667788 1571 RDLQGRDEQSEEKKKQLVRQV 1591
Cdd:PRK00409 677 SDLEKIQKPKKKKKKKPKTVK 697
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1057-1281 |
3.94e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1057 STDLSDQIAELQAQIAE--------------LKMQLaKKEEELQAALARveeeaaqknmalkKIRELESQISELQEDLES 1122
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAkeksvrqqqqqrasLLAQL-KKQEEAISQASR-------------KLRETQNTLNQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1123 ERASRNKAEKQK----RDLGEELEAL-----KTELEDTLDSTAAQQE---------LRSKREQEVNILKKTLEEEAkthe 1184
Cdd:PRK11637 108 LNASIAKLEQQQaaqeRLLAAQLDAAfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQTREELA---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1185 AQIQEMRQKHSQAVEELAEQLEQtkrvkanlekaKQTLENERGELANEVKVLlqgkgdsEHKRKKVEAQLQELQVkfNEg 1264
Cdd:PRK11637 184 AQKAELEEKQSQQKTLLYEQQAQ-----------QQKLEQARNERKKTLTGL-------ESSLQKDQQQLSELRA--NE- 242
|
250
....*....|....*..
gi 12667788 1265 ervrTELADKVTKLQVE 1281
Cdd:PRK11637 243 ----SRLRDSIARAERE 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1653-1892 |
4.18e-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: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1653 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalaleekrRLEARIA 1732
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------------EAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1733 QLeeeleeeqgnTELINDRLK---KANLQIDQINTDLN-------LERSHAQK--NENARQQLERQnKELKVKLQEMegt 1800
Cdd:COG3883 83 ER----------REELGERARalyRSGGSVSYLDVLLGsesfsdfLDRLSALSkiADADADLLEEL-KADKAELEAK--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1801 vKSKYKASITALEAKIAQLEEQ---LDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKR 1877
Cdd:COG3883 149 -KAELEAKLAELEALKAELEAAkaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250
....*....|....*
gi 12667788 1878 QLEEAEEEAQRANAS 1892
Cdd:COG3883 228 AAAAAAAAAAAAAAA 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1137-1524 |
4.25e-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: 41.80 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1137 LGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANle 1216
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1217 kakqtleneRGELANEVKVLLQGKGDSEHKRKKVEAQLQELqvkfnegervrtelADKVTKLQVELDNVTgllsQSDSKS 1296
Cdd:pfam07888 110 ---------SEELSEEKDALLAQRAAHEARIRELEEDIKTL--------------TQRVLERETELERMK----ERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1297 SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDS 1376
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1377 VGCLETAEEVKRKLQKDLEGL-SQR-------HEEKVAAYD---KLEKTKTRLQQELDDLLVDLDHQRQSAcnlEKKQKK 1445
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSMaAQRdrtqaelHQARLQAAQltlQLADASLALREGRARWAQERETLQQSA---EADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1446 FDQLLAEEKTISAKYAEER---DRAEAE-AREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVH 1521
Cdd:pfam07888 320 IEKLSAELQRLEERLQEERmerEKLEVElGREKDCNRVQLSESRRELQELKASLRVAQK----EKEQLQAEKQELLEYIR 395
|
...
gi 12667788 1522 ELE 1524
Cdd:pfam07888 396 QLE 398
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
856-1145 |
4.28e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 856 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEeeeercqhlQ 935
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA---------E 1684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 936 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEaKLKKLEEEQIILEDQNCKLAKEKKlledRIAEfttNLTEEEEKS 1015
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDK----KKAE---EAKKDEEEK 1756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1016 KSLAKLKNKHEAMITDLEERLRR--EEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAlarVE 1093
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSA---IK 1833
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1094 EEAAQKNMALKKIRELESQI----SELQEDLESErASRNKAEKQKRDLGEELEALK 1145
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKfnknNENGEDGNKE-ADFNKEKDLKEDDEEEIEEAD 1888
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
1019-1212 |
4.42e-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: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1019 AKLKNKHEAmITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQI--AELQAQIAELKMQLAKKEEELQAALARVEEEA 1096
Cdd:pfam06705 5 VKLSNMNER-VSGFHDKMENEIEVKRVDEDTRVKMIKEAIAHLEKLiqTESKKRQESFEDIQEEFKKEIDNMQETIKEEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1097 AQKNMALKK-IRELESQISELQEDLESERASRNKAekqkrdlgeeLEALKTELEDTL-DSTAAQQELRSKREQEVNILKK 1174
Cdd:pfam06705 84 DDMAANFRKaLAELNDTINNVETNLQNEIAIHNDA----------IEALRKEALKSLnDLETGIATENAERKKMYDQLNK 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 12667788 1175 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVK 1212
Cdd:pfam06705 154 KVAEGFARISAAIDTEKNARDSAVSAATTELTNTKLVE 191
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1442-1611 |
4.45e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1442 KQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVH 1521
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAQFERDLqgrdeqsEEKKKQLVRQVREmEAELEDE 1601
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELY--RVAGLTPEQARKLLLKLLDAEL-------EEEKAQRVKKIEE-EADLEAE 175
|
170
....*....|
gi 12667788 1602 RKQRSMAVAA 1611
Cdd:PRK12705 176 RKAQNILAQA 185
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1063-1158 |
4.45e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 41.19 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1063 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalkkIRELESQISELQEDLESERASRNKAEKQkrDLGEELE 1142
Cdd:COG4223 1 EIAALEAAVAELPAQLTALEQRLAALEAAPAAAAA--------TAALEARLAALRAALAAAREAVAAAAAA--ALEARLA 70
|
90
....*....|....*.
gi 12667788 1143 ALKTELEDTLDSTAAQ 1158
Cdd:COG4223 71 ALEAKAAAPEAEAAAA 86
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1578-1782 |
4.52e-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: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMREL--D 1655
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1656 DTRASREEILAQAK---------ENEKKLKSMEAEMIQ----LQEELAAAERAKRQAQQERDELADEIANSSGKGALALE 1722
Cdd:COG3883 99 GGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEelkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1723 EKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQ 1782
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1014-1200 |
4.60e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1014 KSKSLAKLKNKHEAMITDLEERLRREE--------KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL 1085
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEaikkeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1086 QaalarveeeaaqknmalKKIRELESQISELQEDLESerasrnkAEKQKrdlgEELEALKTELEDTLDSTAAQQelrskR 1165
Cdd:PRK12704 106 E-----------------KREEELEKKEKELEQKQQE-------LEKKE----EELEELIEEQLQELERISGLT-----A 152
|
170 180 190
....*....|....*....|....*....|....*
gi 12667788 1166 EQEVNILKKTLEEEAKtHEAQIQeMRQKHSQAVEE 1200
Cdd:PRK12704 153 EEAKEILLEKVEEEAR-HEAAVL-IKEIEEEAKEE 185
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
883-1218 |
4.79e-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: 41.60 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 883 LQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQqniqeleeqleEEESARQKL 962
Cdd:pfam05622 62 LLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMD-----------ILRESSDKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 963 QLEKVTTEAKLKKLEEeqiiLEDqnckLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEA---MITDLEERLRRE 1039
Cdd:pfam05622 131 KKLEATVETYKKKLED----LGD----LRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETykrQVQELHGKLSEE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1040 EKQRQELEKTRRKLEG--------------DSTDLSDQIAEL---QAQIAELKMQLAKKEE---------------ELQA 1087
Cdd:pfam05622 203 SKKADKLEFEYKKLEEklealqkekerliiERDTLRETNEELrcaQLQQAELSQADALLSPssdpgdnlaaeimpaEIRE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1088 ALARVEEEaaQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQ 1167
Cdd:pfam05622 283 KLIRLQHE--NKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEEL---QKALQEQGSKAED 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 12667788 1168 EVNILKKTLEEEAKTHEAQIQemRQKHSQAVEELAEQLEQTKRVK-ANLEKA 1218
Cdd:pfam05622 358 SSLLKQKLEEHLEKLHEAQSE--LQKKKEQIEELEPKQDSNLAQKiDELQEA 407
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1523-1727 |
4.95e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1523 LEKSK-RALEQQVEEMKTQLEELEDELQATEDaklrLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDE 1601
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNK----NIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1602 RKQRSMAVAARKKLEMDLKDLEAHIDSANK----------------NRDEAIKQLRKLQAQMKDC---MRELDDTRASRE 1662
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELqhsLEKLDTAIDELE 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1663 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRL 1727
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
860-1097 |
5.15e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 860 KQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKK 939
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNE---EYNELQAELEALQAEIDK----LQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 940 K----MQQNIQELEEQLEEEES-----ARQKLQLEKVTTEAKLKKLEEeqiiLEDQNCKLAKEKKLLEDRIAEFTTNLTE 1010
Cdd:COG3883 90 EraraLYRSGGSVSYLDVLLGSesfsdFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1011 EEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKtrrklegdstdlsdQIAELQAQIAELKMQLAKKEEELQAALA 1090
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA--------------ELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*..
gi 12667788 1091 RVEEEAA 1097
Cdd:COG3883 232 AAAAAAA 238
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1247-1578 |
5.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1247 RKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1327 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVA 1406
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1407 AydKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALE 1486
Cdd:COG4372 179 A--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1487 EAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK 1566
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330
....*....|..
gi 12667788 1567 AQFERDLQGRDE 1578
Cdd:COG4372 337 AELADLLQLLLV 348
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
962-1133 |
5.44e-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: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 962 LQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEK 1041
Cdd:pfam15619 16 LQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1042 QRQELEKTRRKLEGDSTDLS-DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAA----QKNMALKKIRELESQISEL 1116
Cdd:pfam15619 96 ELLRLRDQLKRLEKLSEDKNlAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfrrQLAAEKKKHKEAQEEVKIL 175
|
170
....*....|....*..
gi 12667788 1117 QEDLESERASRNKAEKQ 1133
Cdd:pfam15619 176 QEEIERLQQKLKEKERE 192
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
984-1089 |
5.58e-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: 41.18 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 984 EDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRklegdstdlsdQ 1063
Cdd:smart00435 276 EKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKK-----------Q 344
|
90 100
....*....|....*....|....*.
gi 12667788 1064 IAELQAQIAELKMQLAKKEEELQAAL 1089
Cdd:smart00435 345 IERLEERIEKLEVQATDKEENKTVAL 370
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
884-1226 |
5.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 884 QLQEQLQAETELCAEAEELRARLTAKKQELEEIchdlEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQ 963
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQL----EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 964 LEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR 1043
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1044 QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESE 1123
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1124 RASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAE 1203
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330 340
....*....|....*....|...
gi 12667788 1204 QLEQTKRVKANLEKAKQTLENER 1226
Cdd:COG4372 348 VGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1062-1279 |
5.91e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1062 DQIAELQAQIAELKMQLAkkeeelqaalarVEEEAAQknmalkkirELESQISELQEDLESerasrnkaekqkrdlgeeL 1141
Cdd:PRK09039 53 SALDRLNSQIAELADLLS------------LERQGNQ---------DLQDSVANLRASLSA------------------A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1142 EALKTELEDTLDSTAAQQELRSKREQEvniLKKTLEEEAKTHEaqiQEMRQkhsqaVEELAEQLEQTKRVKANLEKAKQt 1221
Cdd:PRK09039 94 EAERSRLQALLAELAGAGAAAEGRAGE---LAQELDSEKQVSA---RALAQ-----VELLNQQIAALRRQLAALEAALD- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 12667788 1222 lenergelanevkvllqgkgDSEHKRKKVEAQLQELqvkfneGERVRTELADKVTKLQ 1279
Cdd:PRK09039 162 --------------------ASEKRDRESQAKIADL------GRRLNVALAQRVQELN 193
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1047-1284 |
6.07e-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: 41.20 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1047 EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQI----------SEL 1116
Cdd:pfam15742 33 EKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVlkqaqsiksqNSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1117 QEDLESERASRNKAEKQKRDLGEELE-ALKTELEDTLDSTAAQQELRSKREQEVnilkktlEEEAKTHEAQIQEMRQKHS 1195
Cdd:pfam15742 113 QEKLAQEKSRVADAEEKILELQQKLEhAHKVCLTDTCILEKKQLEERIKEASEN-------EAKLKQQYQEEQQKRKLLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1196 QAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKV 1275
Cdd:pfam15742 186 QNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKEALQEELQQVL 265
|
....*....
gi 12667788 1276 TKLQVELDN 1284
Cdd:pfam15742 266 KQLDVHVRK 274
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
960-1400 |
6.35e-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: 41.20 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 960 QKLQLEKvttEAKLKKLEEEQII-------LEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDL 1032
Cdd:pfam15070 7 KQLQTER---DQYAENLKEEGAVwqqkmqqLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAGPSEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1033 EERLRRE-EKQRQELEKTRRKLEG---DSTDLSDQIAELQAQIAELKMQL---AKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:pfam15070 84 EQRLQEEaEQLQKELEALAGQLQAqvqDNEQLSRLNQEQEQRLLELERAAerwGEQAEDRKQILEDMQSDRATISRALSQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1106 IRELESQISELQED--------------LESERASRNKAEKQKRDLGEELEALKTELEdtLDSTAAqQELRSKREQEVNi 1171
Cdd:pfam15070 164 NRELKEQLAELQNGfvkltnenmeltsaLQSEQHVKKELAKKLGQLQEELGELKETLE--LKSQEA-QSLQEQRDQYLA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1172 lkkTLEEEAKTHEAQIQEMRQKHSQAVE--ELAEQLEQTK-RVKANLEKAKQTLENERGELANEVKvllqgkgdsehKRK 1248
Cdd:pfam15070 240 ---HLQQYVAAYQQLASEKEELHKQYLLqtQLMDRLQHEEvQGKVAAEMARQELQETQERLEALTQ-----------QNQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1249 KVEAQLQELQVKfNEGERVRTELADKvtklqveldnvtgllsqsDSKSSKLT--KDFsalesqlqDTQELLQEenrqklS 1326
Cdd:pfam15070 306 QLQAQLSLLANP-GEGDGLESEEEEE------------------EAPRPSLSipEDF--------ESREAMVA------F 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12667788 1327 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLetAEEVKRKLQKDLEGLSQR 1400
Cdd:pfam15070 353 FNSALAQAEEERAELRRQLKEQKRRCRRLAQQAAPAQEEPEHEAHAPGTGGDSV--PVEVHQALQVAMEKLQSR 424
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1513-1648 |
6.36e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1513 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1592
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1593 EMEAELEDERKQRSMAVAARkklemDLKDLEAHIDSANKNRDEAIKQLRKLQAQMK 1648
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1031-1377 |
6.58e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1031 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA-----ELKMQLAKKEEELQAALARVE--EEAAQKNM-- 1101
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSyeedsELKPSGQGGLDEEEAFLDRTAkrEERRQKRLqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1102 ALKKIRELESQISELQEDLESERASRNKAEKqkrdlgeelealkteledtldSTAAQQELRSKREQEVNILKKTLEEEAK 1181
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEEN---------------------SSWEKEEKRDSRLGRYKEEETEIREKEY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1182 THEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA--NEVKVLL-QGKGDSEHKRKKVEAQLQELQ 1258
Cdd:pfam02029 141 QENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvkYESKVFLdQKRGHPEVKSQNGEEEVTKLK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1259 VKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQE-----ENRQKLSLSTKLKQ 1333
Cdd:pfam02029 221 VTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEElkkkrEERRKLLEEEEQRR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 12667788 1334 VEDEKnsfrEQLEEEEEAKHNLEKQIATLHAQVADMKKKM-EDSV 1377
Cdd:pfam02029 301 KQEEA----ERKLREEEEKRRMKEEIERRRAEAAEKRQKLpEDSS 341
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
854-1224 |
6.63e-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: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 854 LVKVREKQLAAENRLTEMETLQSQLMAEklqLQEQLQAETELCAEAEELRARL-TAKKQ-------------ELEEICHD 919
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQILEE---LDELLESEEKNREEVEELKDKYrELRKTllanrfsygpaidELEKQLAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 920 LEARVEEEEERC---QHLQAEK--KKMQQNIQELEEQLEEEESARQKL------QLEKVttEAKLKKLEEEQIILEDQNc 988
Cdd:pfam06160 158 IEEEFSQFEELTesgDYLEAREvlEKLEEETDALEELMEDIPPLYEELktelpdQLEEL--KEGYREMEEEGYALEHLN- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 989 kLAKEKKLLEDRIAEFTTNL--TEEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAE 1066
Cdd:pfam06160 235 -VDKEIQQLEEQLEENLALLenLELDEAEEALEEIEER----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1067 LQAQIAELKM--QLAKKEEELQAAL-ARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEA 1143
Cdd:pfam06160 310 LKEELERVQQsyTLNENELERVRGLeKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1144 L-KTELEdtldstaAQQELrSKREQEVNILKKTLEeeaKTH----EAQIQEMRQKHSQAVEELAEQLEQT----KRVKAN 1214
Cdd:pfam06160 390 LrKDELE-------AREKL-DEFKLELREIKRLVE---KSNlpglPESYLDYFFDVSDEIEDLADELNEVplnmDEVNRL 458
|
410
....*....|
gi 12667788 1215 LEKAKQTLEN 1224
Cdd:pfam06160 459 LDEAQDDVDT 468
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1526-1721 |
6.84e-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: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1526 SKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdEQSEEkkkqlvrQVREMEAELEDERkqr 1605
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEA----ESSRE-------QLQELEEQLATER--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1606 smavAARKKLEMDLKDLEAHIDSankNRDEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSMEAEM 1682
Cdd:pfam09787 107 ----SARREAEAELERLQEELRY---LEEELRRSKATLQSRIKDREAEIEKLRNqltSKSQSSSSQSELENRLHQLTETL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 12667788 1683 IQLQEELAA--AERAKRQAQQERDELADEIANSSGKGALAL 1721
Cdd:pfam09787 180 IQKQTMLEAlsTEKNSLVLQLERMEQQIKELQGEGSNGTSI 220
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1083-1190 |
7.22e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.21 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1083 EELQAALARVEEEAAqknmaLKKIRELESQISELQEDLESERASRNKAEKQ----KRDlGEELEALKteledtldstaaq 1158
Cdd:PRK05431 12 EAVKEALAKRGFPLD-----VDELLELDEERRELQTELEELQAERNALSKEigqaKRK-GEDAEALI------------- 72
|
90 100 110
....*....|....*....|....*....|....*
gi 12667788 1159 qelrskreQEVNILK---KTLEEEAKTHEAQIQEM 1190
Cdd:PRK05431 73 --------AEVKELKeeiKALEAELDELEAELEEL 99
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
867-1226 |
7.47e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.32 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 867 RLTEMETLQSQLMAEKLQLQEQLQA----ETELCAEAEELRARLTAKKQELEE---IChDLEARVEEEEERCQHLQAEKK 939
Cdd:PRK10246 427 RLVALHGQIVPQQKRLAQLQVAIQNvtqeQTQRNAALNEMRQRYKEKTQQLADvktIC-EQEARIKDLEAQRAQLQAGQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 940 -----KMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEEQIILEDQNCKLAKEKKLLED---RIAEFTTNLTEE 1011
Cdd:PRK10246 506 cplcgSTSHPAVEAYQALEPGVNQSRLDALEK-----EVKKLGEEGAALRGQLDALTKQLQRDESeaqSLRQEEQALTQQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1012 -EEKSKSLAKLKNKHEamitDLEERLRREEKQRQELEKTRRKLEgdstdLSDQIAELQAQIAELKMQLAKKEEELQAALA 1090
Cdd:PRK10246 581 wQAVCASLNITLQPQD----DIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1091 RveeeaaqknMALkKIRELESQISELQEDlESERASRNKAEKQKRDLGEELEALKTELE-----DTLDSTAAQQELRSKR 1165
Cdd:PRK10246 652 G---------YAL-TLPQEDEEASWLATR-QQEAQSWQQRQNELTALQNRIQQLTPLLEtlpqsDDLPHSEETVALDNWR 720
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12667788 1166 EQEVNILkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQT--------------KRVKANLEKAKQTLENER 1226
Cdd:PRK10246 721 QVHEQCL--SLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASvfddqqaflaalldEETLTQLEQLKQNLENQR 793
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1500-1710 |
7.65e-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: 40.01 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1500 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATED-AKLRLEVNLQAMKAQFERD-----L 1573
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEErLAEALEKLEEAEKAADESErgrkvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1574 QGRDEQSEEKKKQLVRQVRemEAELEDERKQRSMAVAARKklemdLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRE 1653
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLK--EAKEIAEEADRKYEEVARK-----LVVVEGDLERAEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 12667788 1654 LDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1710
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDEL 213
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1002-1142 |
7.83e-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: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1002 AEFTTNLTE--EEEKSKSlAKLKNKHEAMITDLEERLRRE--------EKQRQELEKTRRKLEGDSTDLSDQIAELQAQI 1071
Cdd:pfam03148 203 EKFTQDNIEraEKERAAS-AQLRELIDSILEQTANDLRAQadavnfalRKRIEETEDAKNKLEWQLKKTLQEIAELEKNI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1072 AELKMQLAKKEEELQAALARVEEEAAQKNMAL----------KKIRELESQISELQEDLESERASRNKAEKQKRDLGEEL 1141
Cdd:pfam03148 282 EALEKAIRDKEAPLKLAQTRLENRTYRPNVELcrdeaqyglvDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDI 361
|
.
gi 12667788 1142 E 1142
Cdd:pfam03148 362 A 362
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
957-1219 |
7.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 957 SARQKL--QLEKVTTEAKLKKLEEEQI-ILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKlknKHEAMITDLE 1033
Cdd:PHA02562 150 PARRKLveDLLDISVLSEMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA---RKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1034 ERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA--KKEEE--------------LQAALARVEEEAA 1097
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKmyekggvcptctqqISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1098 QKNMALKKIRELESQISELQEdLESErasRNKAEKQKRDLGEELEALKTELedtldstaaqqelrskreqevnilkKTLE 1177
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEE-IMDE---FNEQSKKLLELKNKISTNKQSL-------------------------ITLV 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 12667788 1178 EEAKTHEAQIQEM---RQKHSQAVEELAEQLEQTKRVKANLEKAK 1219
Cdd:PHA02562 358 DKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1438-1647 |
7.99e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1438 NLEKKQKKFDQLLAEEKTISAkyAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKddvg 1517
Cdd:COG3206 190 ELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP---- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1518 kSVHELEKSKRALEQQVEEMKTQLEELEDELQAtedaklrlevnLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAE 1597
Cdd:COG3206 264 -VIQQLRAQLAELEAELAELSARYTPNHPDVIA-----------LRAQIAALRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 12667788 1598 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQM 1647
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1578-1714 |
8.15e-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: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1578 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRD------------EAIKQLRKLQA 1645
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaaltkgneelarEALAEKKSLEK 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12667788 1646 QMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSS 1714
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA-KAQEAVQTSLGSLSTSSATDS 165
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1611-1924 |
8.46e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1611 ARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELa 1690
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1691 aaeRAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQleeeleeeqgntelindrlkkanLQIDQINTDLNLER 1770
Cdd:COG1340 81 ---DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER-----------------------LEWRQQTEVLSPEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1771 shaqknenaRQQLERQNKELKVKLQEMEgtVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQ 1850
Cdd:COG1340 135 ---------EKELVEKIKELEKELEKAK--KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12667788 1851 VDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA--TETADAMNREVSSLKNKLRRG 1924
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALkrEKEKEELEEKAEEIFEKLKKG 279
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1216-1364 |
8.56e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1216 EKAKQTLenerGELANEVKVLLQGkgdSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNvtgLLSQSDSK 1295
Cdd:PRK00409 505 EEAKKLI----GEDKEKLNELIAS---LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKE 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12667788 1296 SSKLTKdfSALESQLQDTQELLQEENRQKLSLstKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1364
Cdd:PRK00409 575 AQQAIK--EAKKEADEIIKELRQLQKGGYASV--KAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1522-1707 |
8.72e-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: 40.60 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1522 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKlrlevnlqamkaqferdlqgRDEQSEEKKKQLVRQVREMEAELEDE 1601
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1602 RKQRSMAVAARKKLEmdlkdleahiDSANKNRDEAIKqlrKLQAQMKdcmRELDDTRASREEILAQAKENEKKLKSMEAE 1681
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 12667788 1682 MIQLQEELAAAERAKRQAQQERDELA 1707
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1467-1733 |
9.27e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.09 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1467 AEAEAREKETKALSLARALEEA----MEQKaELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLE 1542
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEArqarLERE-KAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1543 EledelqatedaklrlevNLQAMKAQFERDLQGRDEQSEEKkkqlvrqvremEAELEDERKQRSMAVAAR---KKLEMDL 1619
Cdd:PRK05035 515 D-----------------NSAVIAAREARKAQARARQAEKQ-----------AAAAADPKKAAVAAAIARakaKKAAQQA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12667788 1620 KDLEAHIDSANK----NRDEAIKQLRKLQAQMKD-----CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1690
Cdd:PRK05035 567 ANAEAEEEVDPKkaavAAAIARAKAKKAAQQAASaepeeQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA 646
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 12667788 1691 AAE----RAK-RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQ 1733
Cdd:PRK05035 647 AVAaaiaRAKaRKAAQQQANAEPEEAEDPKKAAVA-AAIARAKAKKAA 693
|
|
| |
