|
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 ... |
844-1924 |
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: 1407.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 844 SRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDL 923
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 924 EARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDR 1003
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1004 IAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK 1083
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1084 KEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1163
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1164 LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGK 1243
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1244 GDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1323
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1324 NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQR 1403
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1404 HEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALS 1483
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1484 LARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 1563
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1564 NLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQL 1643
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1644 RKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1723
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1724 LEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGT 1803
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1804 VKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLE 1883
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 972988096 1884 EAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1924
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-767 |
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: 1355.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGF 334
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 335 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 414
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 415 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 494
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 495 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKADFCII 574
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 575 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 654
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 655 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 734
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 972988096 735 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
95-767 |
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: 1323.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSIT-GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYT-FLSNGFVPIPAAQDDEMFQETVEAMAIM 332
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 333 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 412
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 413 ADFAVEALAKATYERLFRWILTRVNKALDKThRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 492
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 493 EEYQREGIEWNFIDFGLDLQPCIELIERPNnpPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK-FQKPKQLKDKADF 571
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPN--MGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 572 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsETALPGAFKTRKGMFRTVGQ 651
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 652 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 731
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 972988096 732 IPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
95-767 |
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: 1283.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGF 334
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 335 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 414
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 415 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 494
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 495 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKADFCII 574
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 575 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 654
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 655 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 734
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 972988096 735 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-767 |
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: 1251.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSIT----GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 250
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 251 YIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMA 330
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 331 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 410
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 411 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 490
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 491 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKAD 570
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 571 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtALPGAFKTRKGMFRTVG 650
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 651 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 730
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 972988096 731 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-767 |
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: 1237.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGF 334
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 335 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 414
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 415 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 494
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 495 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKADFCII 574
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 575 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 654
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 655 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 734
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 972988096 735 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-767 |
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: 1202.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTS----ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 250
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 251 YIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMA 330
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 331 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 410
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 411 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 490
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 491 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKAD 570
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 571 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtaLPGAFKTRKGMFRTVG 650
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 651 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 730
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 972988096 731 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
95-767 |
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: 1146.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASS---------HKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 245
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 246 FDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQET 325
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 326 VEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 405
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 406 KAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 485
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 486 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKpKQL 565
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 566 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAgMSETALpGAfKTRKGM 645
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF-GA-RTRKGM 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 646 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 725
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 972988096 726 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14911 633 LLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
83-767 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1123.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 83 VEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSML 162
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 163 QDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFI 242
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN----VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 243 RINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN-GFVPIPAAQDDEM 321
Cdd:pfam00063 157 EIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 322 FQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGR 401
Cdd:pfam00063 237 FKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 402 DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 481
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 482 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQK 561
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 562 PKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVagmsETALPGAFKT 641
Cdd:pfam00063 474 PRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 642 RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFR 721
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 972988096 722 QRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-767 |
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: 1109.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAaQDDEMFQETVEAMAIMGF 334
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 335 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 414
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 415 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 494
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 495 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKADFCII 574
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 575 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalPGAFKTRKGMFRTVGQLYK 654
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 655 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 734
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 972988096 735 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
76-779 |
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: 1012.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 76 NPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIAD 155
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 156 TAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKkdtsitGELEKQLLQANPILEAFGNAKTVKNDNS 235
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 236 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPA 315
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 316 AQDD-EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNT-AAQKVCHLMGINVTDFTRSIL 393
Cdd:smart00242 235 GIDDaEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 394 TPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCIN 473
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 474 YTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQ 553
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 554 GSHPKFQKPKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmset 633
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG--------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 634 alpGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 713
Cdd:smart00242 535 ---VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPY 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 714 RVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERD 779
Cdd:smart00242 612 RLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1154 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 905.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 32 VWVPSDKSGFEPASLKEEVGEEAIVEL---VENGKKVKVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKERYY 106
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 107 SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKK 186
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 187 VIQYLAVVASSHkgkkdTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSR 266
Cdd:COG5022 172 IMQYLASVTSSS-----TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 267 AIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETVEAMAIMGFSEEEQLSILKV 345
Cdd:COG5022 247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 346 VSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATY 425
Cdd:COG5022 327 LAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 426 ERLFRWILTRVNKALDKTHRQGaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 505
Cdd:COG5022 406 SNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 506 DFgLDLQPCIELIERpNNPPGVLALLDEECWFPKATDKSFVEKLCT--EQGSHPKFQKPKQLKDKadFCIIHYAGKVDYK 583
Cdd:COG5022 485 DY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 584 ADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIigldqvagmsetalpgafkTRKGMFRTVGQLYKEQLAKLMAT 663
Cdd:COG5022 561 VEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENI-------------------ESKGRFPTLGSRFKESLNSLMST 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 664 LRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS----IPKGFMDG 739
Cdd:COG5022 622 LNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDT 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 740 KQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKRQQQLTAMKVLQRNC 819
Cdd:COG5022 702 KNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGF 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 820 AAYLKLRNWQWWRLFTKVKPLLQVSRQEEEMMAKEEElvkVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelc 899
Cdd:COG5022 782 RLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLAC---IIKLQKTIKREKKLRETEEVEFSLKAEVLIQKF------- 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 900 AEAEELRAR-LTAKKQELEEIChdlEARVEEEEERCQHLQAEKKKMQQniqeleeqleeeeSARQKLQLEKVTTEAKLKK 978
Cdd:COG5022 852 GRSLKAKKRfSLLKKETIYLQS---AQRVELAERQLQELKIDVKSISS-------------LKLVNLELESEIIELKKSL 915
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 979 LEEEQIILEDQNCKLAKEKKLL------EDRIAEFTTNLTEEE--EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELE 1050
Cdd:COG5022 916 SSDLIENLEFKTELIARLKKLLnnidleEGPSIEYVKLPELNKlhEVESKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1051 KTRRKLegdsTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVEEEAAQKNMaLKKIRELESQISELQEDLEseraSR 1130
Cdd:COG5022 996 NFKKEL----AELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTELSI-LKPLQKLKGLLLLENNQLQ----AR 1065
|
1130 1140
....*....|....*....|....
gi 972988096 1131 NKAEKQKRDLGEELEALKTELEDT 1154
Cdd:COG5022 1066 YKALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
95-767 |
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: 882.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 173
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAVVASSHKGKKDTSiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL-----SNGFVPIPAAQDDEMFQETVEA 328
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 329 MAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNT--DQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 406
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 407 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQ-GASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 485
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 486 TMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQL 565
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 566 KDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriigldqvagmsetalpgafktrkgm 645
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 646 frtvgqlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 725
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 972988096 726 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
95-767 |
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: 782.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKD------TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 248
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKkaqflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 249 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETV 326
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 327 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 406
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 407 AQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 485
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 486 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKP-- 562
Cdd:cd14927 398 HMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrp 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 563 -KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKT 641
Cdd:cd14927 475 dKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY--------VGSDSTEDPKSGVKE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 642 RK---GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQ 718
Cdd:cd14927 547 KRkkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYA 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 972988096 719 EFRQRYEILTPNSIPK-GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14927 627 DFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
96-767 |
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: 770.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVASSH--KGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETVEAMAI 331
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 332 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 410
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 411 EQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 489
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 490 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 568
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVVKGR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-M 645
Cdd:cd14913 475 AEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FATADADSGKKKVAKKKGsS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 646 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 725
Cdd:cd14913 546 FQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 625
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 972988096 726 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14913 626 VLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
95-767 |
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: 757.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 413
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 414 DFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 493
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 494 EYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLK---DKA 569
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 570 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiGLDQVAGMSETAlpGAFKTRKGMFRTV 649
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAK--GGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 650 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 729
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 972988096 730 NSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
95-767 |
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: 743.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASShkGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAK-EKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 413
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 414 DFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 493
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 494 EYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK---A 569
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 570 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvselwkdvdriIGLDQVAGMSETALPGAFKTRKGM-FRT 648
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQKRGSsFMT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 649 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 728
Cdd:cd14934 541 VSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLN 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 972988096 729 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14934 621 PNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
96-767 |
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: 717.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSG-LIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKkdTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGE--TQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETVEAMAIMG 333
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQA 413
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 414 DFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 492
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 493 EEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK--FQKPKQLKDKad 570
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 571 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwkdvdriigldqvagmsetalpgafKTRKgmfRTVG 650
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------------KNRK---KTVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 651 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 730
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS 593
|
650 660 670
....*....|....*....|....*....|....*..
gi 972988096 731 SIPKGfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd01380 594 KEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
95-767 |
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: 711.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL---GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEkmRSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETVEAMAIM 332
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 333 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 412
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 413 ADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 491
Cdd:cd14929 316 VTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 492 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK-- 568
Cdd:cd14929 394 QEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfe 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGmseTALPGAFKTRK--GMF 646
Cdd:cd14929 471 AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD---SAIQFGEKKRKkgASF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 647 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 726
Cdd:cd14929 541 QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCI 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 972988096 727 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14929 621 LNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
96-767 |
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: 704.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVAS-SHKGKKDTSI-TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQTPgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETVEAMAI 331
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELL-DMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 332 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 410
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 411 EQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 490
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 491 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK- 568
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MF 646
Cdd:cd14917 476 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAPIEKGKGKAKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 647 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 726
Cdd:cd14917 547 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 972988096 727 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14917 627 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
97-767 |
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: 689.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGES 176
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 177 GAGKTENTKKVIQYLAVVASSHKGKKDTS--ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 412
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 413 ADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 492
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 493 EEYQREGIEWNFIDFGLDLQPCIELIERpnnPPGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDKAD- 570
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEK---PLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVVKGKAEa 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 571 -FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAfKTRKGMFRTV 649
Cdd:cd14918 478 hFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-------ASAEADSGAKKGA-KKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 650 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 729
Cdd:cd14918 550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 972988096 730 NSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14918 630 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-767 |
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: 687.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVASSHKGKKD---TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 252
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 253 VGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETVEAMA 330
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 331 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 409
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 410 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 489
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 490 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 568
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigLDQVAGMSETALPGAfKTRKGMF 646
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY-----AGAEAGDSGGSKKGG-KKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 647 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 726
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 972988096 727 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
96-767 |
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: 684.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVAS-SHKGKKD--TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 252
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 253 VGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEgfNN---YTFLSNGFVPIPAAQDDEMFQETVEAM 329
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 330 AIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 408
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 409 TKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 488
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 489 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKD 567
Cdd:cd14916 398 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 568 K--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGM 645
Cdd:cd14916 475 KqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSS 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 646 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 725
Cdd:cd14916 548 FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 972988096 726 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14916 628 ILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-767 |
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: 681.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVASSHKGKKDT----SITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 251
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 252 IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMA 330
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 331 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 409
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 410 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 489
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 490 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 568
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVVKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAlpgafKTRKGMF 646
Cdd:cd14912 477 AEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGG-----KKKGSSF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 647 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 726
Cdd:cd14912 552 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 972988096 727 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14912 632 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-767 |
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: 679.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVASSHKGKKDT----SITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 251
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 252 IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMA 330
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 331 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 409
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 410 KEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 489
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 490 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKDK 568
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqvAGMSETALPGAFK--TRKG 644
Cdd:cd14910 477 veAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG----------AAAAEAEEGGGKKggKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 645 -MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQR 723
Cdd:cd14910 547 sSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 972988096 724 YEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14910 627 YKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-767 |
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: 669.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 251
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 252 IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMrSDLLLEGFNNYTF--LSNGFVPIPAAQDDEMFQETVEAM 329
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 330 AIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 408
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 409 TKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 488
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 489 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLKD 567
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 568 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMSETALPGAFKTRKGM 645
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 646 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 725
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 972988096 726 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
96-767 |
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: 664.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVASSHKgkkdtsitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 255
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 256 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKE--KMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFQETVEAMAIM 332
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 333 GFSEEEQLSILKVVSSVLQLGNIVFKK-ERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 411
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 412 QADFAVEALAKATYERLFRWILTRVNKALDK---THRqgasFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 488
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPgqkNSR----FIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 489 ILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDK 568
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAGMSETALPGAfKTRKGMfRT 648
Cdd:cd14883 466 TEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSR-GTSKGK-PT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 649 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 728
Cdd:cd14883 543 VGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLD 622
|
650 660 670
....*....|....*....|....*....|....*....
gi 972988096 729 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14883 623 PRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
96-767 |
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: 654.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVASSHkgkkDTSItGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 255
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS----ESEV-ERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 256 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEM-FQETVEAMAIMGF 334
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAAdFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 335 SEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG---RDVVQKAQTKE 411
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 412 QADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 491
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 492 QEEYQREGIEWNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWFP-KATDKSFVEKLCTEQGSHPKFQKPKQLKD--K 568
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalpgafKTRKGMFRT 648
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 649 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 728
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 972988096 729 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
96-767 |
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: 649.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVASSHKGkkdtsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 255
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 256 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFQETVEAMAIMGF 334
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 335 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 414
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 415 FAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 494
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 495 YQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPkqlKDKAdFCII 574
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RGGA-FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 575 HYAGKVDYKADEWLMKNMDPLNDNIATLL----HQSSDKFVSELWKDVDRIigldqvagmsetALPGAFKTRKGMFRTVG 650
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLLsscsCQLPQLFASKMLDASRKA------------LPLTKASGSDSQKQSVA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 651 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 730
Cdd:cd01383 532 TKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPE 611
|
650 660 670
....*....|....*....|....*....|....*..
gi 972988096 731 SIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd01383 612 DV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
95-767 |
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: 620.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 173
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAvvassHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA-----YMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGFvPIPAAQDDEMFQETVEAMAI 331
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 332 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQ--KVC-HLMGINVTDFTRSiLTPRIKVGRD-VVQKA 407
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFhlKAAaELLMCDEKALEDA-LCKRVIVTPDgIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 408 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 487
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 488 FILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKqlKD 567
Cdd:cd01384 393 FKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 568 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalPGAFKTRKgmFR 647
Cdd:cd01384 468 RTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR---------------EGTSSSSK--FS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 648 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 727
Cdd:cd01384 531 SIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 972988096 728 TPNsIPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 767
Cdd:cd01384 611 APE-VLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
95-767 |
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: 613.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHkgkkdTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQH-----SWI----EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKK--ERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 411
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 412 QADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAS--FLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 489
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 490 LEQEEYQREGIEWNFIDFgLDLQPCIELI-ERPNNppgVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDK 568
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdVDRIIGLDQVAGMSetalpgafkTRKgmfR- 647
Cdd:cd01381 468 S-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF-------LKQLFNEDISMGSE---------TRK---Ks 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 648 -TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 726
Cdd:cd01381 528 pTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRV 607
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 972988096 727 LTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd01381 608 LVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-767 |
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 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 173
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAVVASSHkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG--------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLegfnnytflsngfvpIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKERNT-------DQASMPDNTAAQKvchLMGINVTDF-----TRSILTPRIKVGR 401
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQTTRGGAKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 402 DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALdkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 481
Cdd:cd01382 295 TVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCI--PFETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 482 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQK 561
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 562 P--------KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagMSET 633
Cdd:cd01382 450 PrksklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTN---------NNKD 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 634 ALPgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPN 713
Cdd:cd01382 521 SKQ---KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 972988096 714 RVVFQEFRQRYEILTPNSIPKgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd01382 598 RTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
95-767 |
9.63e-180 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 559.78 E-value: 9.63e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASShkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS---------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSnGFVPIPAAQDDEMFQETVEAMAIMGF 334
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLS-GCIEVEGVDDVADFEEVVLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 335 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQAS---MPDNTAAQKVCHLMGINVTDFTRSILTPRIKV-GRDVVQKAQTK 410
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 411 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 490
Cdd:cd14872 311 AQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 491 EQEEYQREGIEWNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKAD 570
Cdd:cd14872 391 EEALYQSEGVKFEHIDF-IDNQPVLDLIE--KKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 571 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalpGAFKTRKGmfrTVG 650
Cdd:cd14872 468 FIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-----------------GDQKTSKV---TLG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 651 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtPN 730
Cdd:cd14872 528 GQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VK 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 972988096 731 SIPKGFM-DGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14872 607 TIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
95-767 |
2.52e-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: 2.52e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQ----DREDQS 169
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 170 ILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSIT----------GELEKQLLQANPILEAFGNAKTVKNDNSSRFG 239
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 240 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDD 319
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 320 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmpDNTAAQ---KVCHLMGINVTDFTRSILTPR 396
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQslkLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 397 IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTN 476
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 477 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIE-RPNNPPGVLALLDeECWFPKAT--DKSFVEKL---- 549
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 550 ---------CTEQGSHPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwkdvDR 620
Cdd:cd14890 476 grksgsggtRRGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS------------RR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 621 IIgldqvAGMSetalpgafktrkgmfrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGV 700
Cdd:cd14890 543 SI-----REVS-----------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 701 LEGIRICRQGFPNRVVFQEFRQRYEILTPNSipkgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
95-767 |
1.45e-176 |
|
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: 551.67 E-value: 1.45e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASShkgkKDTSITgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 254
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR----RNNLVT----EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQ---ASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 410
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 411 EQADFAVEALAKATYERLFRWILTRVN----KALDKTHRqgasfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 486
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNaivySGTQDTLS-----IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 487 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlk 566
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 567 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldQVAGMSETALP----GAFKTR 642
Cdd:cd01387 462 PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPrlgkGRFVTM 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 643 KGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 722
Cdd:cd01387 533 KPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFID 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 972988096 723 RYEILTPNSIPKGfMDGKQACVLMIKALELD-SNLYRIGQSKVFFR 767
Cdd:cd01387 613 RYRCLVALKLPRP-APGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
96-767 |
2.77e-171 |
|
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: 536.47 E-value: 2.77e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVasshkGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 255
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANN---RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 256 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSD---LLLEGFNNYTFLSNGFVPIPAAQDD--EMFQETVEAMA 330
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 331 IMGFSEEEQLSILKVVSSVLQLGNIVFK---KERNTDQASM-PDNTAAQKVCHLMGINVTDFtRSILTPRIKVGR-DVVQ 405
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADEL-QEALTSHSVVTRgETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 406 KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL--DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 483
Cdd:cd01379 313 RNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 484 NHTMFILEQEEYQREGIEWNFIDFG-----LDLqpcieLIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPk 558
Cdd:cd01379 393 NQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 559 FQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpga 638
Cdd:cd01379 464 YWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 639 fktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQ 718
Cdd:cd01379 517 ---------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFA 587
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 972988096 719 EFRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 767
Cdd:cd01379 588 DFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-767 |
3.30e-171 |
|
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: 538.50 E-value: 3.30e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLavVASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGSG-----VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLsNGFVPIPAAQDDEM--FQETVEAMAIM 332
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYL-NQSDCYTLEGEDEKyeFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 333 GFSEEEQLSILKVVSSVLQLGNIVFKKER-NTDQASMPDNTAAQK-VCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 410
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 411 EQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQGASfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 486
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 487 MFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPkQLK 566
Cdd:cd01385 392 IFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 567 DKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriIGLDQVAGMSETALPGAFKT----- 641
Cdd:cd01385 468 EPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAVFRWAVLRAFFRAmaafr 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 642 RKGMFR-----------------------------TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVL 692
Cdd:cd01385 540 EAGRRRaqrtaghsltlhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVL 619
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 693 DQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnsIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd01385 620 RQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
95-767 |
6.47e-171 |
|
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: 535.43 E-value: 6.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKK-RHEMPPHIYAIADTAYRSMLQDREDQSILCT 173
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAvvasshkgKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd14897 81 GESGAGKTESTKYMIKHLM--------KLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDE-------MFQETV 326
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEeleyyrqMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 327 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 406
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 407 AQTKEQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 482
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 483 FNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKP 562
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 563 KqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagmsetalpgafktr 642
Cdd:cd14897 470 P--GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 643 kgmfrtvgQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 722
Cdd:cd14897 522 --------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 972988096 723 RYEILTPNSiPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 767
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
95-765 |
3.26e-170 |
|
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: 534.37 E-value: 3.26e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY------KGKKRHEMPPHIYAIADTAYRSMLQDRE-- 166
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 167 --DQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 244
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 245 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGFVPIPAAQDDEMF 322
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 323 QETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF-KKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGR 401
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 402 DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAS-FLGILDIAGFEIFEVNSFEQLCINYTNEKLQ 480
Cdd:cd14901 321 EYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEKLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 481 QLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSH 556
Cdd:cd14901 401 QLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEA--RPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 557 PKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalp 636
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 637 gafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 716
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 972988096 717 FQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNL-----YRIGQSKVF 765
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
95-767 |
5.86e-170 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 533.97 E-value: 5.86e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 173
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAVVASshkGKKDTSItgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI-----KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFlSNGFVPIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALSLIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASM--PDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 411
Cdd:cd14903 232 VSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 412 QADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 491
Cdd:cd14903 312 QAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 492 QEEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLcteQGSHPKFQK----PKqlKD 567
Cdd:cd14903 391 QIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKL---SSIHKDEQDviefPR--TS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 568 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdrIIGLDQVAGMSETALPGAFKTRKGMFR 647
Cdd:cd14903 462 RTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALTTT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 648 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 727
Cdd:cd14903 539 TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 972988096 728 TPNSiPKGFMDGKQACVLMIKALELDS-NLYRIGQSKVFFR 767
Cdd:cd14903 619 LPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
95-767 |
2.90e-169 |
|
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: 531.68 E-value: 2.90e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 173
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFQETVEAMAIM 332
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 333 GFSEEEQLSILKVVSSVLQLGNIVFKkerNTDQASMPDNTAAQKVCHLMGINVTDFTrSILTPRIKVGR-DVVQKAQTKE 411
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLT-DALTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 412 QADFAVEALAKATYERLFRWILTRVNKALDKthRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 491
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRIKG--KEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 492 QEEYQREGIEWNFIDFgLDLQPCIELIERpnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDkaDF 571
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEK---KLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 572 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWkdvdriiglDQVAGMSETALPGAFKTRKGmfRTVGQ 651
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRR--PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 652 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 731
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 972988096 732 IPKGFMDGKqaCVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
95-729 |
2.90e-168 |
|
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: 529.65 E-value: 2.90e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 173
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAVVASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVT---- 249
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL-----VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 250 -----GYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP------------ 312
Cdd:cd14888 155 msgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidmssfephl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 313 ------------IPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQ---KV 377
Cdd:cd14888 235 kfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 378 CHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIA 457
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 458 GFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWF 537
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 538 PKATDKSFVEKLCTEQGSHPKFQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD 617
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 618 -VDRIIGLdqvagmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 696
Cdd:cd14888 550 yLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670
....*....|....*....|....*....|...
gi 972988096 697 CNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 729
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-767 |
8.82e-162 |
|
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: 511.61 E-value: 8.82e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEM---PPHIYAIADTAYRSMLQDR----ED 167
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 168 QSILCTGESGAGKTENTKKVIQYLAV----VASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 243
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATasklAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 244 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMF 322
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 323 QETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFkkERNTDQ----ASMPDNTAAQKVCHLMGINVTDFTRSILTPRIK 398
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 399 VGR-DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQ---------GASFLGILDIAGFEIFEVNSFE 468
Cdd:cd14892 319 TARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 469 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFP-KATDKSFVE 547
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 548 KL-CTEQGSHPKFQKPKQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriigldq 626
Cdd:cd14892 476 IYhQTHLDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 627 vagmsetalpgafktrkgmFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 706
Cdd:cd14892 536 -------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 707 CRQGFPNRVVFQEFRQRYEILTPNS-IPKGFMDGKQACVLMIKALE-----LDSNLYRIGQSKVFFR 767
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNKaGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
97-767 |
9.62e-154 |
|
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: 489.80 E-value: 9.62e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSML----QDREDQSILC 172
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 173 TGESGAGKTENTKKVIQYLAVVASSHKgkkdtsitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYI 252
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGNS---------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 253 VGANIETYLLEKSRAIRQARDERTFHIFYYMIAG--AKEKMRSDLLLEGFnnYTFLSNGFvpipaAQDDEM------FQE 324
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA-----GCKREVqywkkkYDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 325 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFkkERNTDQASMPDNTA---AQKVCHLMGINVTDFTRSiLTPRIKVGR 401
Cdd:cd14889 226 VCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSngwLKAAAGQFGVSEEDLLKT-LTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 402 -DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQG--ASFLGILDIAGFEIFEVNSFEQLCINYTNEK 478
Cdd:cd14889 303 gEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 479 LQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK 558
Cdd:cd14889 383 LQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 559 FQKPKQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK-DVDRIIGLDQVAGMSETALPG 637
Cdd:cd14889 460 YGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLPQAGSDN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 638 AFKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVF 717
Cdd:cd14889 538 FNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 972988096 718 QEFRQRYEIL--TPNsIPKgfmdGKQACVLMIKALELDSnlYRIGQSKVFFR 767
Cdd:cd14889 615 AEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
95-730 |
9.35e-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: 476.06 E-value: 9.35e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH--------EMPPHIYAIADTAYRSMLQDR 165
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 166 EDQSILCTGESGAGKTENTKKVIQYLaVVASSHKGKKDTSITGE------------LEKQLLQANPILEAFGNAKTVKND 233
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFL-TQLSQQEQNSEEVLTLTssiratskstksIEQKILSCNPILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 234 NSSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEG---FNNYTFLS-N 308
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLKkS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 309 GFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQA--SMPDNTAAQKVCHLMGINVT 386
Cdd:cd14907 240 NCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 387 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL------DKTHRQGASF-LGILDIAGF 459
Cdd:cd14907 320 ELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 460 EIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWF 537
Cdd:cd14907 400 EVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLD--KPPIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 538 PKATDKSFVEKLCTEQGSHPKFQKPKQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD 617
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 618 VDRiigldqvagmSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 697
Cdd:cd14907 556 EDG----------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670
....*....|....*....|....*....|...
gi 972988096 698 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 730
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
96-733 |
2.09e-143 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 459.77 E-value: 2.09e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY-----------KGKKRHEMPPHIYAIADTAYRSM-- 161
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 162 --LQDREDQSILCTGESGAGKTENTKKVIQYLAVV------ASSHKGKKDTSITGelekQLLQANPILEAFGNAKTVKND 233
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlaASVSMGKSTSGIAA----KVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 234 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEkmrsdlllegfnnytflsngfvpi 313
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE------------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 314 pAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTD-QASMPDNTAAQKV------CHLMGINVT 386
Cdd:cd14900 214 -AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDAT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 387 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD----KTHRQGASFLGILDIAGFEIF 462
Cdd:cd14900 293 KLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmddsSKSHGGLHFIGILDIFGFEVF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 463 EVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKATD 542
Cdd:cd14900 373 PKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISQ--RPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 543 KSFVEKLCTEQGSHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndniatLLHQSSdkfvselwkdVDrii 622
Cdd:cd14900 450 TTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD--- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 623 gldqvagmsetalpgafktrkgMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLE 702
Cdd:cd14900 509 ----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660 670
....*....|....*....|....*....|.
gi 972988096 703 GIRICRQGFPNRVVFQEFRQRYEILTPNSIP 733
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
95-767 |
4.89e-143 |
|
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: 459.51 E-value: 4.89e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERyySGLI----YTYSGLFCVVINPYKNLPiysEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDRE---D 167
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 168 QSILCTGESGAGKTENTKKVIQYL---AVVASSHKG-------KKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSR 237
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttrAVGGKKASGqdieqssKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 238 FGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPA 315
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 316 AQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKK----ERNTDQASMPDNTAAQKVCHLMGINVTDFTRS 391
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 392 ILTPRIkVGRDVVQKAQ-TKEQADFAVEALAKATYERLFRWILTRVNKALDKtHRQGASFLGILDIAGFEIFE-VNSFEQ 469
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFEtKNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 470 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELI-ERPNnppGVLALLDEECWFPKATDKSFVEK 548
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPN---GILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 549 LCTEQGSHPKFQKPKQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHqSSDKFVselwkdvdriigldqv 627
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKFS---------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 628 agmsetalpgafktrkgmfrtvgqlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIC 707
Cdd:cd14891 532 ---------------------------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 708 RQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIK-ALELDSNLYRIGQSKVFFR 767
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
95-750 |
4.07e-140 |
|
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: 453.96 E-value: 4.07e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYK--------GKKRHEMPPHIYAIADTAYRSMLQ-D 164
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 165 REDQSILCTGESGAGKTENTKKVIQYLAVV-ASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 243
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 244 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN---GFVPIPAAQDD- 319
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKRAVADKy 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 320 -EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKE-RNTDQASMPDNTAAQ--KVCHLMGINVTDFTRSILTP 395
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 396 RIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD--------KTHRQGASFLGILDIAGFEIFEVNSF 467
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 468 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVE 547
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFD--DKSNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 548 KLCTEQGShpkfqkpkqlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSelwkdvdrIIGLDQV 627
Cdd:cd14902 478 KFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV--------AIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 628 AGMSETALPGAFKTRKGMFRT--VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 705
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 972988096 706 ICRQGFPNRVVFQEFRQRYEIL-----TPNSIPK-GFMDGKQA--CVLMIKAL 750
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFkcflsTRDRAAKmNNHDLAQAlvTVLMDRVL 670
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
95-767 |
8.68e-139 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 447.85 E-value: 8.68e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 173
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAVVASshkGKKDTSITgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGFVPIPAAQDDEMFQETVEAMAI 331
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 332 MGFSEEEQLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKVCHLMGINVTDF-----TRSILT--PRIKVGRDVV 404
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIeealcNRSVVTrnESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 405 QKAQTKeqadfavEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 484
Cdd:cd14904 312 EAEENR-------DALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 485 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCT---EQGSHPKFQK 561
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIRTnhqTKKDNESIDF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 562 PKQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvaGMSETALPGAFKT 641
Cdd:cd14904 461 PKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 642 RKGMfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFR 721
Cdd:cd14904 530 TKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELA 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 972988096 722 QRYEILTPNSIPKGfmDGKQACVLMIKALELDSNL-YRIGQSKVFFR 767
Cdd:cd14904 609 TRYAIMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
95-767 |
2.68e-138 |
|
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: 446.15 E-value: 2.68e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIVG 254
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQ--------TEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFV-PIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQ--ASMPDNTAAQKVCHLMGINvTDFTRSILTPRIKV-GRDVVQKAQTK 410
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 411 EQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 489
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 490 LEQEEYQREGIEWNFIDfGLDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlkDKA 569
Cdd:cd14896 391 QEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 570 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGmsetalpgafktrkgmfrTV 649
Cdd:cd14896 466 VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------------TL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 650 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 729
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS 607
|
650 660 670
....*....|....*....|....*....|....*...
gi 972988096 730 NSIPkGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14896 608 ERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
96-767 |
9.58e-137 |
|
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: 444.01 E-value: 9.58e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPiyseeivEMYKGKKRHE-------MPPHIYAIADTAYRSMLQ----- 163
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 164 --DREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTS----ITGElekQLLQANPILEAFGNAKTVKNDNSSR 237
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKrrraISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 238 FGKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTF--LSNG- 309
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFqyISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 310 -FVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERntDQASMPDNTAAQKVCHLMGINVTDF 388
Cdd:cd14895 232 cYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASS--EDEGEEDNGAASAPCRLASASPSSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 389 T-------------------RSILTPR-IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDK------ 442
Cdd:cd14895 310 TvqqhldivsklfavdqdelVSALTTRkISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfaln 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 443 ----THRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIELI 518
Cdd:cd14895 390 pnkaANKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEML 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 519 ERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLN 596
Cdd:cd14895 469 EQ--RPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPN 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 597 DNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalpgafKTRKGMFRTV--GQLYKEQLAKLMATLRNTNPNFVRC 674
Cdd:cd14895 545 AELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKL------RRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRC 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 675 IIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELds 754
Cdd:cd14895 619 IKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL-- 696
|
730
....*....|...
gi 972988096 755 nlyriGQSKVFFR 767
Cdd:cd14895 697 -----GKTRVFLR 704
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
93-810 |
2.38e-135 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 444.09 E-value: 2.38e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 93 NEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHE-MPPHIYAIADTAYRSMLQDREDQSIL 171
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 172 CTGESGAGKTENTKKVIQYLAvvaSSHKGKKDTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 251
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 252 IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAI 331
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 332 MGFSEEEQLSILKVVSSVLQLGNIVF--KKERNTDQASM--PDNTAA-QKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 406
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 407 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDKThrQG-ASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 485
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPP--GGfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVD 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 486 TMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQL 565
Cdd:PTZ00014 499 IVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVD 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 566 KDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRKGM 645
Cdd:PTZ00014 576 SNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQ 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 646 FrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 725
Cdd:PTZ00014 639 L--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFK 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 726 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR---AGVLAHLEEERDLKITDVIIGFQACCRGYLARKAF 802
Cdd:PTZ00014 717 YLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKV 796
|
....*...
gi 972988096 803 AKRQQQLT 810
Cdd:PTZ00014 797 RKNIKSLV 804
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
95-767 |
7.39e-135 |
|
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: 438.19 E-value: 7.39e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK--GKKRHE-------MPPHIYAIADTAYRSMLQD- 164
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 165 REDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSitGELEK-----QLLQANPILEAFGNAKTVKNDNSSRFG 239
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEG--EELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 240 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRS--------DLLLEGFNNYTFLSNGFV 311
Cdd:cd14908 159 KFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 312 P-IPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQK----VCHLMGINVT 386
Cdd:cd14908 239 PdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 387 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVN 465
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 466 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFP-KATDKS 544
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDAN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 545 FVEKL--------CTEQGSHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdniatllhqssdkfvselw 615
Cdd:cd14908 475 YASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 616 kdvdriigldqvagmsetalpgafKTRKGMFRTvGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQL 695
Cdd:cd14908 536 ------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQL 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 696 RCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnSIPK----GFMDGKQACVLMIKALELDSNLYR------------- 758
Cdd:cd14908 591 RYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKDLVKGVlspamvsmknipe 669
|
730
....*....|...
gi 972988096 759 ----IGQSKVFFR 767
Cdd:cd14908 670 dtmqLGKSKVFMR 682
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
95-767 |
2.09e-133 |
|
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: 434.04 E-value: 2.09e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKkdtsITGElekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVE---KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNytflSNGFVPIPAAQDDEM------FQETVEA 328
Cdd:cd01386 154 ASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 329 MAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSI------------LTPR 396
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 397 IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEifevN----------S 466
Cdd:cd01386 310 GQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGFQ----NpahsgsqrgaT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 467 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPN------------NPPGVLALLDEE 534
Cdd:cd01386 385 FEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdeDRRGLLWLLDEE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 535 CWFPKATDKSFVEKLCTEQG--SHPKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNIATLLHQSSD 608
Cdd:cd01386 465 ALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 609 KFvselwkdvdriigldqvagmsetalpgAFKTRKGMFRTVgqlyKEQLAKLMATLRNTNPNFVRCIIPNHE------KK 682
Cdd:cd01386 545 ET---------------------------AAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkderST 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 683 AGKLDPHLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGF-----MDGKQACVLMIKALE 751
Cdd:cd01386 594 SSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELD 673
|
730
....*....|....*.
gi 972988096 752 LDSNLYRIGQSKVFFR 767
Cdd:cd01386 674 LEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
95-765 |
8.81e-130 |
|
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: 422.47 E-value: 8.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAvvaSSHKGKKDTSItgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI----QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKErntDQASMPDntAA----------QKVCHLMGINVTDFTRSILTPRIKVGRDV 403
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 404 VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAsFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 483
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 484 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFqKPK 563
Cdd:cd14876 388 IDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 564 QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRK 643
Cdd:cd14876 464 KVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------KIAK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 644 GMFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQR 723
Cdd:cd14876 528 GSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQ 605
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 972988096 724 YEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVF 765
Cdd:cd14876 606 FKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
95-763 |
3.76e-122 |
|
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: 403.21 E-value: 3.76e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAIADTAYRSMLQDREDQSILC 172
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 173 TGESGAGKTENTKKVIQYLaVVASSHKGKKDTSITG---ELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVT 249
Cdd:cd14906 81 SGESGSGKTEASKTILQYL-INTSSSNQQQNNNNNNnnnSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 250 GYIV-GANIETYLLEKSR-AIRQARDERTFHIFYYMIAGAKEKMRSDLLLEG-FNNYTFL--------------SNGFVP 312
Cdd:cd14906 160 DGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 313 IPAAQD-DEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQAS--MPDNTAA-QKVCHLMGINVTDF 388
Cdd:cd14906 240 HNNKTEsIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 389 TRSILTPRIKVG---------RDVVQKAQTKEqadfaveALAKATYERLFRWILTRVNKALDK----------THRQGAS 449
Cdd:cd14906 320 KQALLNRNLKAGgrgsvycrpMEVAQSEQTRD-------ALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 450 FLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLA 529
Cdd:cd14906 393 FIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 530 LLDEECWFPKATDKSFVEKlCTEQgSHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDK 609
Cdd:cd14906 470 LLDDECIMPKGSEQSLLEK-YNKQ-YHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 610 FVSELWKdvdriigldqvagMSETALPGAFKTRKGMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPH 689
Cdd:cd14906 548 LKKSLFQ-------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNV 613
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972988096 690 LVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSK 763
Cdd:cd14906 614 HVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
95-765 |
2.15e-121 |
|
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: 399.22 E-value: 2.15e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAIADTAYRSMLQDRE--DQSI 170
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 171 LCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 250
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 251 YIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGfvpiPAAQDDEMFQETVEAMA 330
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 331 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKV---CHLMGINVTDFTRSILTPRIKVGRD--VVQ 405
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVrtsALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 406 KAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 485
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 486 TMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQL 565
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 566 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgafktrkgm 645
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPV---------- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 646 fRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 725
Cdd:cd14880 544 -LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 972988096 726 ILTPN--SIPKGFMDGKQAcvlmikalELDSNLYRIGQSKVF 765
Cdd:cd14880 623 LLRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
95-767 |
9.71e-116 |
|
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: 383.01 E-value: 9.71e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYS-GLIYTYSGLFCVVINPYKNLPIYSEEIVEMY-KGKKRHEMPPHIYAIADTAYRSM-LQDREDQSIL 171
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 172 CTGESGAGKTENTKKVIQYLAVVASSHKGK-KDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VT 249
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNtSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 250 GYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDL----------LLEGFNnyTFLSNGfVPIPAAQDD 319
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgglktaqdykCLNGGN--TFVRRG-VDGKTLDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 320 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILtprIKV 399
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 400 GRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEK 478
Cdd:cd14875 314 KTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 479 LQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCTE-QGSHP 557
Cdd:cd14875 394 LQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKRT--GIFSMLDEECNFKGGTTERFTTNLWDQwANKSP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 558 KFQKPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriigLDQVAGMSEtalpg 637
Cdd:cd14875 471 YFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LSTEKGLAR----- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 638 afktRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVF 717
Cdd:cd14875 536 ----RK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 718 QEFRQRYEILTPNSIPKGFMDGK--QACVLMI----KALELDSNLYRIGQSKVFFR 767
Cdd:cd14875 609 EQFCRYFYLIMPRSTASLFKQEKysEAAKDFLayyqRLYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-767 |
2.75e-112 |
|
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: 372.68 E-value: 2.75e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH-----EMPPHIYAIADTAYRSMLQDREDQ 168
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 169 SILCTGESGAGKTENTKKVIQYLAVVASSHkgkkdtsiTGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 248
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS--------STDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 249 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFQETVE 327
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASkCYDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 328 AMAIMgFSEEEQLSILKVVSSVLQLGNIVFKKERN--TDQASMPDNTAA-QKVCHLMGINVTDFTRSILTPRIKVGRDVV 404
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 405 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALdKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 484
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 485 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKlCTEQGSHPKF--QKP 562
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSS-CKSKIKNNSFipGKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 563 KQLKdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLdqvagmsetalpgafktR 642
Cdd:cd14886 467 SQCN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-----------------M 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 643 KGMFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 722
Cdd:cd14886 526 KGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFH 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 972988096 723 RYEILT--PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14886 604 RNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
95-724 |
5.11e-109 |
|
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: 365.57 E-value: 5.11e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY----------KGKKRHEMPPHIYAIADTAYRSMLQ 163
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 164 DREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE---------LEKQLLQANPILEAFGNAKTVKNDN 234
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 235 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAG-----AKEKMRSDLLLEGFNNYTFLSN 308
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 309 GFVPI--PAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF-----KKERNT--DQASMPDNTAA----- 374
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 375 QKVCHLMGINvTDFTRSILTPR--------IKVGRDVVQKAQTKEqadfaveALAKATYERLFRWILTRVNKAL------ 440
Cdd:cd14899 321 TKAAELLGVS-TEALDHALTKRwlhasnetLVVGVDVAHARNTRN-------ALTMECYRLLFEWLVARVNNKLqrqasa 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 441 --------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQ 512
Cdd:cd14899 393 pwgadesdVDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 513 PCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTE---QGSHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLM 589
Cdd:cd14899 472 ACLELFE--HRPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 590 KNMDPLNDNIATLLHQSSDKFVSELWKDVDRiiglDQVAGMSETALPGAFKTRKGMFRT----VGQLYKEQLAKLMATLR 665
Cdd:cd14899 550 KNKDSFCESAAQLLAGSSNPLIQALAAGSND----EDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVR 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 972988096 666 NTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 724
Cdd:cd14899 626 ATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
95-767 |
3.73e-100 |
|
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: 340.09 E-value: 3.73e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYS--------GLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDRE 166
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 167 DQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 246
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 247 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLsngfvpipaaqddemfQET 325
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGDPESTDL----------------RRI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 326 VEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTA--------AQKVCHLM-------GINVTDFTR 390
Cdd:cd14887 221 TAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 391 SILTPRIK------------------VGRDV--VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHR----- 445
Cdd:cd14887 301 KHLKTVARllglppgvegeemlrlalVSRSVreTRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesd 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 446 --------QGASFLGILDIAGFEIFE---VNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQ 512
Cdd:cd14887 381 sdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 513 PCIELIERPNN----------------------PPGVLALLDEECWFPKATDKSFVEKLCTEQGSHP-------KFQKPK 563
Cdd:cd14887 461 LASTLTSSPSStspfsptpsfrsssafatspslPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNiinsakyKNITPA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 564 QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLhQSSDKFVSElwkdvdriIGLDQVAGMSetalpgAFKTRK 643
Cdd:cd14887 541 LSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKKNSGVR------AISSRR 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 644 gmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQR 723
Cdd:cd14887 606 ---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRR 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 972988096 724 YEILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 767
Cdd:cd14887 683 YETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
92-766 |
3.20e-98 |
|
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: 331.82 E-value: 3.20e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 92 LNEASVLHNLKERYYSGLIYTY---SGLfcVVINPYKNLPIYSEEIVEMYK-------GKKRHEMPPHIYAIADTAYRSM 161
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 162 LQDREDQSILCTGESGAGKTENTKKVI-QYLAVVASSHKGKKdtsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGK 240
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 241 FIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGF--VPIPAA 316
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 317 QDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF--KKERNTDQASMpDNTAA-QKVCHLMGINVTDFtRSIL 393
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 394 TPRIK-VGRDVV----QKAQTKEQADfaveALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIF---EVN 465
Cdd:cd14879 310 TYKTKlVRKELCtvflDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 466 SFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIELIERPnnPPGVLALLDEEC-WFPK 539
Cdd:cd14879 386 SLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILDDQTrRMPK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 540 ATDKSFVEKLCTEQGSHPKF---QKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLndniatllhqSSDkFVSelwk 616
Cdd:cd14879 458 KTDEQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN---- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 617 dvdriigldqvagmsetalpgafktrkgMFRTVGQLyKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 696
Cdd:cd14879 523 ----------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIR 573
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 697 CNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgFMDGKQACVLMIKALELDSNLYRIGQSKVFF 766
Cdd:cd14879 574 SLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
96-729 |
2.10e-96 |
|
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: 324.16 E-value: 2.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNlpIYSEEIVEMYKGKKRHeMPPHIYAIADTAYRSMLQdREDQSILCTGE 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAvvasshkgkKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvtGYIVGA 255
Cdd:cd14898 78 SGSGKTENAKLVIKYLV---------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 256 NIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLlegfNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGFS 335
Cdd:cd14898 147 KFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKYKMTCSAMKSLGIANFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 336 EEEQLSIlkvvsSVLQLGNIVFKKERNTDQASmpdNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADF 415
Cdd:cd14898 223 SIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 416 AVEALAKATYERLFRWILTRVNKALDKThrqGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 495
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 496 QREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLcteqgshpKFQKPKQLKDKADFCII- 574
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI--------KKYLNGFINTKARDKIKv 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 575 -HYAGKVDYKADEWLMKNMDplndniatllhqssdkfvselwKDVDRIIGLDQVAgmsetalpgafktRKGMFRTVGQLY 653
Cdd:cd14898 440 sHYAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN-------------DEGSKEDLVKYF 484
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 654 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 729
Cdd:cd14898 485 KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
95-767 |
4.07e-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: 317.53 E-value: 4.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 171
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 172 CTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITgelekqllQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 250
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFK--------HVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 251 YIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAA---QDDEMFQETV 326
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREdVSTAersLNREKLAVLK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 327 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINvTDFTRSILTPRIKVGR-DVVQ 405
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVS-TDELASALTTDIQYFKgDMII 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 406 KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 482
Cdd:cd14878 312 RRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 483 FNHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKSFVEKLCT 551
Cdd:cd14878 392 INEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPNLPKKLQS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 552 --EQGSHPKFQKPKQ-------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdri 621
Cdd:cd14878 459 llESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 622 igldqvagmsetalpgaFKTRkgmFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVL 701
Cdd:cd14878 532 -----------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVL 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 702 EGIRICRQGFPNRVVFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 767
Cdd:cd14878 592 EMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
95-767 |
1.52e-89 |
|
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: 306.56 E-value: 1.52e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEivemYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQ-YLAVVasshkgKKDTSITgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 253
Cdd:cd14937 77 ESGSGKTEASKLVIKyYLSGV------KEDNEIS----NTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd14937 147 SSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQlSILKVVSSVLQLGNIVFK---KERNTDQASMPDNT--AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 408
Cdd:cd14937 227 MHDMKD-DLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 409 TKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 488
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 489 ILEQEEYQREGIEWNFIDFGLDlQPCIELIeRPNNppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDK 568
Cdd:cd14937 385 EKETELYKAEDILIESVKYTTN-ESIIDLL-RGKT--SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 569 aDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagMSETAlpgafkTRKGMfrt 648
Cdd:cd14937 461 -NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSESL------GRKNL--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 649 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRVVFQEFRQRYEILT 728
Cdd:cd14937 521 ITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLD 599
|
650 660 670
....*....|....*....|....*....|....*....
gi 972988096 729 PNSIPKGFMDGKQACVLMIKAlELDSNLYRIGQSKVFFR 767
Cdd:cd14937 600 YSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
95-719 |
8.14e-80 |
|
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: 279.48 E-value: 8.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHE-------MPPHIYAIADTAYRSMLQDRE 166
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 167 DQSILCTGESGAGKTENTKKVIQYLavvassHKGKKDTSITgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 246
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF------HYIQTDSQMT-ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 247 D---------VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAG-AKEKMRSDLLLEGFNNYTFL---------- 306
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 307 ----------SNGFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKerntdqasmpdntaaqk 376
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 377 VCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-------- 448
Cdd:cd14884 297 AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediys 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 449 ---SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnnpp 525
Cdd:cd14884 377 ineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 526 gVLALLDE-----ECWFPKATDKSF-----------VEKLCTEQGSHPKFQK---PKQLKDKADFCIIHYAGKVDYKADE 586
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFryllnnerqqqLEGKVSYGFVLNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 587 WLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpGAFKTRKGMFRTVGQLYKEQLAKLMATLRN 666
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 972988096 667 TNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 719
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
96-753 |
1.93e-76 |
|
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: 267.75 E-value: 1.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYknlpiyseeiveMYKGKKRH-------EMPPHIYAIADTAYRSMLQDREDQ 168
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 169 SILCTGESGAGKTENTKKVIQYLAVVASshkGKKDTsitgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFdV 248
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG---GGPET----DAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 249 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETV 326
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 327 EAMAIMG--FseeeqLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSiLTPRIK-VGRDV 403
Cdd:cd14881 222 ACLGILGipF-----LDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 404 VQKAQTKEQADFAVEALAKATYERLFRWILTRVN--KALDKTHRQGAS--FLGILDIAGFEIFEVNSFEQLCINYTNEKL 479
Cdd:cd14881 295 VKSVCDANMSNMTRDALAKALYCRTVATIVRRANslKRLGSTLGTHATdgFIGILDMFGFEDPKPSQLEHLCINLCAETM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 480 QQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIELIErpNNPPGVLALLDEECwFPKATDKSFVEKLCTEQGSHPK 558
Cdd:cd14881 375 QHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNPR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 559 FQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdvdriigldqvagmsetalpgA 638
Cdd:cd14881 451 LFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF---------------------------G 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 639 FKTRKGMFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQ 718
Cdd:cd14881 503 FATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFK 575
|
650 660 670
....*....|....*....|....*....|....*..
gi 972988096 719 EFRQRYEILTPNSIPKGFMDGKQAC--VLMIKALELD 753
Cdd:cd14881 576 AFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQP 612
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
95-732 |
1.35e-72 |
|
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: 256.34 E-value: 1.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYkgkkrhemppHIYAIADTAYRSMLQDRED-QSILCT 173
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 174 GESGAGKTENTKKVIQYLAvvaSSHKGKKDTSITGELEKqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDvTGYIV 253
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 254 GANIE-TYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIM 332
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 333 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTD---QASMPDNTAAQK-VCHLMGINVTDFTrSILTPRIKVGRDVvqkaq 408
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSEDGTTI----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 409 TKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAsfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 488
Cdd:cd14874 294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 489 ILEQEEYQREGIEWNF-IDFGLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQlKD 567
Cdd:cd14874 372 HDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 568 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmsetalpgAFKTRKgMFR 647
Cdd:cd14874 449 RLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-------------------SSNTSD-MIV 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 648 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 727
Cdd:cd14874 509 SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
....*
gi 972988096 728 TPNSI 732
Cdd:cd14874 589 LPGDI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
96-720 |
1.10e-71 |
|
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: 255.02 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVasshkgkkDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 254
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTT--------DLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 255 ANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN-GFVPIPAAQDDEMFQETVEAMAIMG 333
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 334 FSEEEQLSILKVVSSVLQLGNIVFKKERNtdQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAqtkeqa 413
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 414 dfavEALAKATYERLFRWILTRVNKALDKThrQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQE 493
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 494 EYQREGIEW-NFIDFGlDLQPCIELIERpnnppgVLALLDEECWFPKATDKSFVEKLCTEQGSHPKF-QKPKQlkdkadF 571
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------F 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 572 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFV---SELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFR- 647
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrDGVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLSc 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 648 -----------------------------TVGQLYKeQLAKLMATLRNTNPN--FVRCIIPNHEKKAGKLDPHLVLDQLR 696
Cdd:cd14905 525 gsnnpnnvnnpnnnsgggggggnsgggsgSGGSTYT-TYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660
....*....|....*....|....*...
gi 972988096 697 CNGVLEGIRICRQGFP----NRVVFQEF 720
Cdd:cd14905 604 SLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
96-767 |
2.29e-70 |
|
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: 250.43 E-value: 2.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 175
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 176 SGAGKTENTKKVIQYLAVVAsshKGKKDTSitgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 255
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG---DGNRGAT------GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 256 NIETYLLEKSRAIRQARDERTFHIFYYMIAG--AKEKMRsDLLLEGFNNYTFL----SNGFVPIPAAQDD-----EMFQE 324
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLrippEVPPSKLKYRRDDpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 325 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKerNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 404
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 405 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHrqgaSFLG------ILDIAGFEIFEVNSFEQLCINYTNEK 478
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR----AVFGdkysisIHDMFGFECFHRNRLEQLMVNTLNEQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 479 LQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciELIERPNnppGVLALLDEECwfPKATDKSFVekLCTEQGS 555
Cdd:cd14882 386 MQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYI--MDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 556 HPKFQKPKQlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMsetal 635
Cdd:cd14882 456 HSQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM----- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 636 pgafKTRKGMFRTVGQlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 715
Cdd:cd14882 521 ----RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRI 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 972988096 716 VFQEFRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 767
Cdd:cd14882 594 PFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
98-725 |
3.73e-66 |
|
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: 240.26 E-value: 3.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 98 LHNLKERYYSGLIYTYSGLFCVVINPYKNLPIY----------SEEIVEMYKGKKRHEMPPHIYAIADTAYRSMLQDRED 167
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 168 QSILCTGESGAGKTENTKKVIQYLAVVASS----HKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 243
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 244 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKE--KMRSDLLL-EGFNNYTFLSNGFVPIPA-AQDD 319
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMnKCVNEFVMLKQADPLATNfALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 320 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF-------KKERNTDQASMPDNTA------AQ--KVCHLMGIN 384
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAKLLEVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 385 --VTD---FTRSILTpriKVGRDVVQ--KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQG----AS 449
Cdd:cd14893 324 pvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 450 FLGILDIAGFEIFE--VNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIELIER 520
Cdd:cd14893 401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFED 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 521 PnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKAD------------FCIIHYAGKVDYKADEWL 588
Cdd:cd14893 481 K--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 589 MKNMDPLNDNIATLLHQSSDKfvselwkdVDRIIGLDQVA------GMSETALPGAF--KTRKGMFR----------TVG 650
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAaassekAAKQTEERGSTssKFRKSASSaresknitdsAAT 630
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 651 QLYKEQLAKLMAtLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 725
Cdd:cd14893 631 DVYNQADALLHA-LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
117-251 |
6.74e-63 |
|
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: 212.20 E-value: 6.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 117 FCVVINPYKNLPIYSEEIV-EMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVA 195
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 972988096 196 SSHKGKKD-------TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 251
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 ... |
96-765 |
4.57e-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: 215.47 E-value: 4.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK-GKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 174
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 175 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQ---------------LLQANPILEAFGNAKTVKNDNSSRFG 239
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIhneentdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 240 KFIRINFDvTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDD 319
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 320 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNI-----VFKKE---------------------RNTDQASMPDNTA 373
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 374 AQKV-CHLMGINVTDFTRSILTPRIkVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHR--QGASF 450
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 451 LGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNppGVLAL 530
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 531 LDEECWFPKATDKSFVEKLCTEQGSH-PKFQKPKQLK-DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 608
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRnSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 609 KFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQ----LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKA- 683
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 684 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgfmDGKQACVLMIKALELDSNLYRIGQSK 763
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 972988096 764 VF 765
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
936-1833 |
1.44e-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: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 936 HLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1015
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEELRE-----ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1016 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARV 1095
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE-------AQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1096 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtlDSTAAQQELRSKREQEvniL 1175
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE---RLEDRRERLQQEIEEL---L 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1176 KKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnevkvllqgkgdSEHKRKKVEA 1255
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA------------QLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1256 QLQELQVKFNEGERvrteladKVTKLQVELDNVTGLLSQSDSKSSKLTKdfsALESQLQDT-QELLQEENRQKLSLSTKL 1334
Cdd:TIGR02168 496 RLQENLEGFSEGVK-------ALLKNQSGLSGILGVLSELISVDEGYEA---AIEAALGGRlQAVVVENLNAAKKAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1335 KQVEDEKNSFREQLEEEEeakhnlekqiATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLE--------------GL 1400
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKG----------TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldnAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1401 SQRHEEK-----VAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR 1475
Cdd:TIGR02168 636 ELAKKLRpgyriVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1476 EKETKALSLARALEEAMEQKAELERlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATE 1555
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEA-------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1556 DAKLRLEVNLQAMKAQFeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKN 1635
Cdd:TIGR02168 789 AQIEQLKEELKALREAL-DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1636 RDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN 1715
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1716 ssgKGALALEEKRRLEARIAqleeeleeeqGNTELINDRLKKANLQIDQINTdlnlershaqKNENARQQLERQNKELKV 1795
Cdd:TIGR02168 948 ---EYSLTLEEAEALENKIE----------DDEEEARRRLKRLENKIKELGP----------VNLAAIEEYEELKERYDF 1004
|
890 900 910
....*....|....*....|....*....|....*...
gi 972988096 1796 KLQEMEGTVKSKYKasitaLEAKIaqleEQLDNETKER 1833
Cdd:TIGR02168 1005 LTAQKEDLTEAKET-----LEEAI----EEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
873-1619 |
2.80e-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: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 873 EMETLQSQLMA---EKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQ 949
Cdd:TIGR02168 240 ELEELQEELKEaeeELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 950 ELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHE 1029
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1030 AMITDLEERLRREEKQRQELEKTRRKLEGDSTDLsdQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKI 1109
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1110 RELESQISELQEDLESERASRNKAEKQKRDLGEELEAlKTELEDTLDSTAAQQELRSKREQEVNI-----LKKTLEEEAK 1184
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLSGILGVLSELISVDEGYEAAIEAalggrLQAVVVENLN 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1185 THEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKV-----EAQLQE 1259
Cdd:TIGR02168 557 AAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddLDNALE 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1260 LQVKFNEGERVRTELADKVTK-----------------LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQE 1322
Cdd:TIGR02168 637 LAKKLRPGYRIVTLDGDLVRPggvitggsaktnssileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1323 ENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQ 1402
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1403 RHEEKVAAYDKLEKTKTRLQQELDDLLVDldhQRQSACNLEKKQKKFDQLLAEEKTISakyaEERDRAEAEAREKETKAL 1482
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRER---LESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIE 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1483 SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDaKLRLE 1562
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-RLSEE 948
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972988096 1563 VNLQAMKA-QFERDLQGRDEQSEEKKKQLVRQVREM---------EAELEDER-----KQRSMAVAARKKLE 1619
Cdd:TIGR02168 949 YSLTLEEAeALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieEYEELKERydfltAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1038-1882 |
4.73e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 134.03 E-value: 4.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1038 RLRREEKQRQeLEKTRRKLEgdstDLSDQIAELQAQIAELKMQlAKKEEELQAAlaRVEEEAAQKNMALKKIRELESQIS 1117
Cdd:TIGR02168 171 KERRKETERK-LERTRENLD----RLEDILNELERQLKSLERQ-AEKAERYKEL--KAELRELELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1118 ELQEDLESERASRNKAEKQKRDLGEELEALKTEL-EDTLDSTAAQQELrskreQEVNILKKTLEEEAKTHEAQIQEMRQK 1196
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKEL-----YALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1197 hsqaVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVkvllqgkgdsehkrkkveaqlQELQVKFNEGERVRTELAD 1276
Cdd:TIGR02168 318 ----LEELEAQLEELESKLDELAEELAELEEKLEELKEEL---------------------ESLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1277 KVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLkqVEDEKNSFREQLEEEEEAKH 1356
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1357 NLEKQIATLHAQvadmkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQR 1436
Cdd:TIGR02168 451 ELQEELERLEEA--------------LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1437 QSACNLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKA---ELERLNKQF--RTEMED 1511
Cdd:TIGR02168 517 GLSGILGVLS---ELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflPLDSIKGTEiqGNDREI 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1512 LMSSKDDVGkSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAK-LRLEVNLQAMK--------------AQFERDL 1576
Cdd:TIGR02168 594 LKNIEGFLG-VAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKkLRPGYRIVTLDgdlvrpggvitggsAKTNSSI 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1577 QGRD---EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDC 1653
Cdd:TIGR02168 673 LERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1654 MRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR 1733
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1734 IAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKAsIT 1813
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK-RS 911
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1814 ALEAKIAQLEEQLdNETKERQAACKQVRRT--EKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1882
Cdd:TIGR02168 912 ELRRELEELREKL-AQLELRLEGLEVRIDNlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
994-1854 |
3.23e-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: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 994 AKEKKLLEDRIA---EFttnlteEEEKSKSLAKLK------NKHEAMITDLEERLRREEKQRQELEK----TRRKLEGDS 1060
Cdd:TIGR02169 152 PVERRKIIDEIAgvaEF------DRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1061 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQED-----------LESERAS 1129
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekigeLEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1130 RNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKhsqaVEELAEQLE 1209
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE----LEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1210 QTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELdnvt 1289
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL---- 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1290 gllsqsdsksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQV 1369
Cdd:TIGR02169 458 ----------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTV 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1370 ADMKKKMEDSVGCLETAeeVKRKLQK---DLEGLSQR-----HEEKVAAYDKLEKTKTRlQQELDDLLVDLDHQRQSACN 1441
Cdd:TIGR02169 528 AQLGSVGERYATAIEVA--AGNRLNNvvvEDDAVAKEaiellKRRKAGRATFLPLNKMR-DERRDLSILSEDGVIGFAVD 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1442 LEKKQKKF---------DQLLAE----------------------------------EKTISAKYAEERDRAEAEAREKE 1478
Cdd:TIGR02169 605 LVEFDPKYepafkyvfgDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1479 tkalSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAK 1558
Cdd:TIGR02169 685 ----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1559 LRLEVNLQAMKAQFErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDE 1638
Cdd:TIGR02169 761 KELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1639 AIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIanssg 1718
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI----- 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1719 kgalaleekRRLEARIAQLEEELEEEQGNTELInDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKElkvKLQ 1798
Cdd:TIGR02169 913 ---------EKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNML---AIQ 979
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1799 EMEGTVKskykasitaleaKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQV 1854
Cdd:TIGR02169 980 EYEEVLK------------RLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
973-1557 |
3.87e-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: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 973 EAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1052
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1053 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNK 1132
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1133 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvnilkktlEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK 1212
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1213 RVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKfnEGERVRTELADKVTKLQVELDNVTGLL 1292
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR--GLAGAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1293 SQ----SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQ 1368
Cdd:COG1196 548 LQnivvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1369 VADmkkKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAcnlekkQKK 1448
Cdd:COG1196 628 VAA---RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL------EEA 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1449 FDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskDDVGKSVHELEK 1528
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL----EELERELERLER 774
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 972988096 1529 SKRAL--------------EQQVEEMKTQLEELEDELQATEDA 1557
Cdd:COG1196 775 EIEALgpvnllaieeyeelEERYDFLSEQREDLEEARETLEEA 817
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
101-708 |
5.47e-29 |
|
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: 126.40 E-value: 5.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 101 LKERYYSGLIYTYSGLFCV-VINPYKNL------PIYSEEIVEMYKGKKRHE--MPPHIYAIAD---------------- 155
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 156 ----TAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAVVASS--HKGKKDT-SITG-------------------- 208
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPalSKGSEETcKVSGstrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 209 --------------------------------------------------------------ELEKQL------------ 214
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehlEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 215 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------RDERTFHI 279
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 280 FYYMIAGAK-----EKMRSDLLLEGFN--NYTFLSN------GFVPIPAA--QDDEMFQETVEAMAIMGFSEEEQLSILK 344
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDGIDcsALTYLGRsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 345 VVSSVLQLGNIVFKKERNTDQASMPDN---TAAQKVCHLMGI-NVTDFTRSILTPRIKV--GRDVVQKAQTKEQADFAVE 418
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 419 ALAKATYERLFRWILTRVNKAL----------------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLqql 482
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 483 fnhtmfileqeeYQREGiewNFIDFGLDLQPciELIERPN---------NPPGVLALLDEECWFPKAT----------DK 543
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRP--HLTARDSekdvlfiyeHPLGVFASLEELTILHQSEnmnaqqeekrNK 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 544 SFVEKLCTEQGShpKFQKPKQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVS 612
Cdd:cd14894 626 LFVRNIYDRNSS--RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFC 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 613 ELWKDVDRiIGLD-----QVAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMatlrntnPNFVRCIIPNHEKKAGKLD 687
Cdd:cd14894 704 RMLNESSQ-LGWSpntnrSMLGSAESRLSGT-KSFVGQFRSHVNVLTSQDDKNM-------PFYFHCIRPNAKKQPSLVN 774
|
810 820
....*....|....*....|.
gi 972988096 688 PHLVLDQLRCNGVLEGIRICR 708
Cdd:cd14894 775 NDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
962-1713 |
9.84e-28 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 122.87 E-value: 9.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 962 RQKLQLEKVTTEaKLKKLEEEQIILEDQncKLAKEKKLLEDRIAEFTTNLTEEEEkskSLAKLknkhEAMITDLEERL-R 1040
Cdd:TIGR02169 200 LERLRREREKAE-RYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEE---ELEKL----TEEISELEKRLeE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1041 REEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQknmalkkIRELESQISELQ 1120
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1121 EDLESERasrnkaeKQKRDLGEELEALKTELEDtldstaaqqelrskreqevniLKKTLEEEAKTHeaqiQEMRQKHSQA 1200
Cdd:TIGR02169 343 REIEEER-------KRRDKLTEEYAELKEELED---------------------LRAELEEVDKEF----AETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1201 VEELAEqleqtkrvkanlekakqtLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1280
Cdd:TIGR02169 391 REKLEK------------------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1281 LQVELdnvtgllsqsdsksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEK 1360
Cdd:TIGR02169 453 QEWKL--------------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1361 QIATLHAQVADMKKKMEDSVGCLETAeeVKRKLQK---DLEGLSQR-----HEEKVAAYDKLEKTKTRlQQELDDLLVDL 1432
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERYATAIEVA--AGNRLNNvvvEDDAVAKEaiellKRRKAGRATFLPLNKMR-DERRDLSILSE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1433 DHQRQSACNLEKKQKKF---------DQLLAE----------------------------------EKTISAKYAEERDR 1469
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYepafkyvfgDTLVVEdieaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1470 AEAEAREKEtkalSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELED 1549
Cdd:TIGR02169 676 LQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1550 ELQATEDAKLRLEVNLQAMKAQFErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHI 1629
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1630 DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL 1709
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
....
gi 972988096 1710 ADEI 1713
Cdd:TIGR02169 909 EAQI 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1702 |
2.74e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 115.17 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 859 KVREKQLAAENRLTEMETLqsqlMAEKLQLQEQLQAETElcaEAEELRArLTAKKQELE--EICHDLEARVEEEEERCQH 936
Cdd:TIGR02169 174 KALEELEEVEENIERLDLI----IDEKRQQLERLRRERE---KAERYQA-LLKEKREYEgyELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 937 LQAEKKKMQQNIQELEEQLEEEESARQKLQlekvTTEAKLKKL-EEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1015
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLE----ELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1016 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARV 1095
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1096 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNIL 1175
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1176 KKTLEE-----EAKTHEAQIQEMRQKHSQAVEELAE--------QLEQTKRVKANLEKAkqtLENERGELANEVKVllqg 1242
Cdd:TIGR02169 482 EKELSKlqrelAEAEAQARASEERVRGGRAVEEVLKasiqgvhgTVAQLGSVGERYATA---IEVAAGNRLNNVVV---- 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1243 KGDSEHKR-----KKVEA------QLQELQVKFNEGERVRTELADKVTKLQVELDNV-----------TGLLSQSDSKSS 1300
Cdd:TIGR02169 555 EDDAVAKEaiellKRRKAgratflPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARR 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1301 KLTK-DFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEeeeakhnLEKQIATLHAQVADMKKKMEDS 1379
Cdd:TIGR02169 635 LMGKyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1380 VGCLETAEEVKRKLQKDLEGLSQRHEekvAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTI 1459
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEE---KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1460 SAKYAEER--------DRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKR 1531
Cdd:TIGR02169 785 EARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1532 ALEQQVEEMKTQLEELEDELQatedaklrlevnlqamkaqferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMA 1611
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1612 VAARKKLEMDLKDLEAHIdSANKNRDEAIKQLRKLQAQMKDCMRELDD-----TRASR--EEILAQAKENEKKLKSMEAE 1684
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnMLAIQeyEEVLKRLDELKEKRAKLEEE 1001
|
890
....*....|....*...
gi 972988096 1685 MIQLQEELAAAERAKRQA 1702
Cdd:TIGR02169 1002 RKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1205-1926 |
8.91e-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: 8.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1205 AEQLEQTKRVKANLEKAKQTLE-NERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQV 1283
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1284 ELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEeeeeakhNLEKQIA 1363
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------SLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1364 TLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSACNLE 1443
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1444 KKqkKFDQLLAEEKTISAKYAEERDRAEAEareKETKALSLARALEEAMEQKAELERLNKQFRTeMEDLMSSKDDVGKSV 1523
Cdd:TIGR02168 435 LK--ELQAELEELEEELEELQEELERLEEA---LEELREELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1524 HELEKSKRALEQQVEEMKTQLE-----ELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRD------EQSEEKKKQLVR 1592
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISvdegyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1593 QVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANkNRDEAIKQLRKLQAQMKdcMRELDDTRASREEILAQA- 1671
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKKLRPGYR--IVTLDGDLVRPGGVITGGs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1672 --------------KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQL 1737
Cdd:TIGR02168 666 aktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1738 EEELeeeqgntELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKyKASITALEA 1817
Cdd:TIGR02168 746 EERI-------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1818 KIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRR 1897
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
730 740
....*....|....*....|....*....
gi 972988096 1898 KLQRELedatetadamnREVSSLKNKLRR 1926
Cdd:TIGR02168 898 ELSEEL-----------RELESKRSELRR 915
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1085-1913 |
2.96e-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: 111.70 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1085 EEELQAALARVEEeaaqknmALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeleALKTELEDTlDSTAAQQEL 1164
Cdd:TIGR02169 169 DRKKEKALEELEE-------VEENIERLDLIIDEKRQQLERLRREREKAERYQ--------ALLKEKREY-EGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1165 RSKREQEVNILKK--TLEEEAKTHEAQIQEMRQKHSQAVEELAEQleqTKRVKANLEKAKQTLENERGELANEVKVLLQG 1242
Cdd:TIGR02169 233 EALERQKEAIERQlaSLEEELEKLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRVKEKIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1243 KGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdSKSSKLTKDFSALESQLQDTQELLQE 1322
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT-------EEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1323 ENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK-------MEDSVGCLETAEEVKRKLQK 1395
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeeKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1396 DLEGLSQRHEEKVAAYDKLEKTKTRLQQElddllvdldhqrqsacnlekkqkkfdqLLAEEKTISAKYAEERDRAEAEar 1475
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRE---------------------------LAEAEAQARASEERVRGGRAVE-- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1476 eketkaLSLARALEEAMEQKAELERLNKQFRTEMEDLMSSK--------DDVGKSVHELEKSK---RALEQQVEEMKTQL 1544
Cdd:TIGR02169 514 ------EVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRlnnvvvedDAVAKEAIELLKRRkagRATFLPLNKMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1545 EELEdelQATEDAKLRLEVNLQAMKAQFERDLQG--RDE---QSEEKKKQLVRQVR--EMEAELED-----------ERK 1606
Cdd:TIGR02169 588 RDLS---ILSEDGVIGFAVDLVEFDPKYEPAFKYvfGDTlvvEDIEAARRLMGKYRmvTLEGELFEksgamtggsraPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1607 QRSMAVAARKKLEM---DLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1683
Cdd:TIGR02169 665 GILFSRSEPAELQRlreRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1684 EMIQLQEELAAAErakrqaqQERDELADEIANSSGKGALALEEKRRLEARIAQleEELEEEQGNTELINDRLKKANLQID 1763
Cdd:TIGR02169 745 DLSSLEQEIENVK-------SELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLR 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1764 QINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTV------KSKYKASITALEAKIAQLEEQLDNETKERQAAC 1837
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1838 KQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQrANASRRKLQRELEDATETADAM 1913
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 ... |
1305-1928 |
2.74e-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: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1305 DFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLE 1384
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1385 TAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELddllvdldhqrqsaCNLEKKQKKFDQLLAEEKTISAKYA 1464
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEK--------------VTTEAKIKKLEEDILLLEDQNSKLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1465 EERDRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1544
Cdd:pfam01576 152 KERKLLEERISEFTSN-------LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1545 EELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLK- 1623
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEa 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1624 ---DLEAHIDSANKNRDEAIKQLRKLqAQMKDCMREldDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKR 1700
Cdd:pfam01576 304 lktELEDTLDTTAAQQELRSKREQEV-TELKKALEE--ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1701 QAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNE 1780
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1781 NARQQLERQNKELKVKLQEmEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRN 1860
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1861 AEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGD 1928
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFD 607
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1383-1926 |
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 972988096 1383 LETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAK 1462
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1463 YAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1542
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1543 QLEELEDELQATEDAKLRLEVNLQAmkaqferdLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDL 1622
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEE--------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1623 KDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKL--KSMEAEMIQLQEELAAAERAKR 1700
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVliGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1701 QAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGN-TELINDRLKKANLQIDQINTDLNLERSHAQKN 1779
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAaVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1780 ENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQldnetKERQAACKQVRRTEKKLKDVLLQVDDERR 1859
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE-----AELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1860 NAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET----ADAMNREVSSLKNKLRR 1926
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEA 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1040-1615 |
1.42e-21 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 102.43 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1040 RREEKQRQELEKTRRKLEG-DSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEA---AQKNMALKKIRELESQ 1115
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1116 ISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTaaqqELRSKREQEVNILKKTLEEEakthEAQIQEMRQ 1195
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDR----DEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1196 KHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA 1275
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1276 DKVTKLQVELDNVTGllsqsdsKSSKLTKDFSALESQLQDTQELLQE----ENRQKLSLSTKLKQVEDEknsfREQLEEe 1351
Cdd:PRK02224 412 DFLEELREERDELRE-------REAELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVETIEED----RERVEE- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1352 eeakhnLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKdLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVD 1431
Cdd:PRK02224 480 ------LEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER-REDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1432 LDHQRQSAcnlEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKAL--SLARALEEAMEQKAELERLNKQFRTEM 1509
Cdd:PRK02224 553 AEEKREAA---AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiaDAEDEIERLREKREALAELNDERRERL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1510 EDLMSSKDDVGKSVHEleKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER--DLQGRDEQSEEKK 1587
Cdd:PRK02224 630 AEKRERKRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEleELRERREALENRV 707
|
570 580 590
....*....|....*....|....*....|....
gi 972988096 1588 KQL------VRQVREMEAELEDERKQRSMAVAAR 1615
Cdd:PRK02224 708 EALealydeAEELESMYGDLRAELRQRNVETLER 741
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1201-1801 |
1.80e-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: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1201 VEELAEQLEQTKRVKAnLEKAKQTLENErgELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1280
Cdd:COG1196 202 LEPLERQAEKAERYRE-LKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1281 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEK 1360
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1361 QIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAC 1440
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1441 NLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELErlnkqfrtEMEDLMSSKDDVG 1520
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL--------EAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1521 KSVHELEKSKRaLEQQVEEMKTQLEELEDELQATEDAKLRLEVNlqamkaqfERDLQGRDEQSEEKKKQLVRQVREMEAE 1600
Cdd:COG1196 511 KAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALAAALQNIVV--------EDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1601 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKS 1680
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1681 MEAEmiQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANL 1760
Cdd:COG1196 662 LTGG--SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 972988096 1761 QIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEME 1801
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1720 |
2.81e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.14 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 862 EKQLAAENRLTEMETlqsqlmAEKLQLQEQLQAETELCAEAEELRARLTAKKQEleeichdlEARVEEEEERCQHLQAEK 941
Cdd:PTZ00121 1096 AFGKAEEAKKTETGK------AEEARKAEEAKKKAEDARKAEEARKAEDARKAE--------EARKAEDAKRVEIARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 942 KKMQQNIQELEEQLEEEESARQKLQLEKVTteaKLKKLEEEQIILEDQncKLAKEKKLLEDRIAEfttnlteEEEKSKSL 1021
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAE---ELRKAEDARKAEAAR--KAEEERKAEEARKAE-------DAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1022 AKLKnkheamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIaelKMQLAKKEEELQAALARVEEEAAQ 1101
Cdd:PTZ00121 1230 KKAE----------EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKAEEKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1102 KNMALKKIRELESQISELQEDLESER----------ASRNKAEKQKRD---LGEELEALKTELEDTLDSTAAQQELRSKR 1168
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKkaeeakkkadAAKKKAEEAKKAaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1169 EQEVNILKKTLEEEAKTHEAqiqemrQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGelANEVKVLLQGKGDSEH 1248
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEA------KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1249 KRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDfsalESQLQDTQELLQEENRQKl 1328
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA----AEAKKKADEAKKAEEAKK- 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1329 slSTKLKQVEDEKNSFR----EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRH 1404
Cdd:PTZ00121 1524 --ADEAKKAEEAKKADEakkaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1405 EE----KVAAYDKLEKTKTRlQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKE-- 1478
Cdd:PTZ00121 1602 EEekkmKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEea 1680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1479 TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKS-------VHELEKSKRALEQQVEEMKTQLEELEDEL 1551
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAeeenkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1552 QATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKklEMDLKDLEAHIDS 1631
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADS 1838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1632 ANKNRDEAikqlrklqaqmkdcmrelDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELAD 1711
Cdd:PTZ00121 1839 KNMQLEEA------------------DAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER 1900
|
....*....
gi 972988096 1712 EIANSSGKG 1720
Cdd:PTZ00121 1901 EIPNNNMAG 1909
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
859-1423 |
4.87e-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: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 859 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQ 938
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 939 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKS 1018
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1019 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1098
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1099 AAQKNMALKKIRELESQISELQEDLESERASRN---------KAEKQKRDLGEELEALKTEL--EDTLDSTAAQQELRSK 1167
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligVEAAYEAALEAALAAALQNIvvEDDEVAAAAIEYLKAA 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1168 REQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSE 1247
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1248 HKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDfsALESQLQDTQELLQEENRQK 1327
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER--ELAEAEEERLEEELEEEALE 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1328 LSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDsvgcLET----AEEvkrklqkDLEGLSQR 1403
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA----LGPvnllAIE-------EYEELEER 796
|
570 580
....*....|....*....|
gi 972988096 1404 HEEKVAAYDKLEKTKTRLQQ 1423
Cdd:COG1196 797 YDFLSEQREDLEEARETLEE 816
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1594 |
8.48e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.06 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 859 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQ 938
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 939 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKS 1018
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1019 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA---ELKMQLAKKEEELQAALarv 1095
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGSVGERYATAI--- 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1096 eeEAAQKNMALKKIRELESQISELQEDLESERASR------NKAEKQKRDLGEELE-------------------ALKTE 1150
Cdd:TIGR02169 542 --EVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRatflplNKMRDERRDLSILSEdgvigfavdlvefdpkyepAFKYV 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1151 LEDTLdstaAQQELRSKREQEVNILKKTLEEEAKTHEAQI----QEMRQKHSQAVEELAEQLEQTKRVKAnLEKAKQTLE 1226
Cdd:TIGR02169 620 FGDTL----VVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggsRAPRGGILFSRSEPAELQRLRERLEG-LKRELSSLQ 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1227 NERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDF 1306
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1307 SALESQLQDTQELLQEEnrqklslstKLKQVEDEKNSfreqleeeeeakhnLEKQIATLHAQVADMKKKMEDSVGCLETA 1386
Cdd:TIGR02169 775 HKLEEALNDLEARLSHS---------RIPEIQAELSK--------------LEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1387 EEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKtisakyaEE 1466
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE-------RK 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1467 RDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkDDVGKSVHELEKSKRALE-------QQVEE 1539
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRALEpvnmlaiQEYEE 983
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1540 MKTQLEELEDELqatedAKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLVRQV 1594
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 ... |
977-1869 |
2.40e-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: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 977 KKLEEEQIILEDQNCKLAKEKKLLE--DRIAEFTTNLTEEEEKSKSLAKLKNKheamitdleERLRREEKQRQELEKTRR 1054
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEetENLAELIIDLEELKLQELKLKEQAKK---------ALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1055 KLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAE 1134
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1135 KQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvnilKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRV 1214
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE----LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1215 KANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQ 1294
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1295 SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKK 1374
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1375 KMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLA 1454
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1455 EEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDvgKSVHELEKSKRALE 1534
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAE--SELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1535 QQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAA 1614
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1615 RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQ-----MKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQ 1689
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAElleeeQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1690 EELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDL 1769
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1770 NLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKD 1849
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
890 900
....*....|....*....|
gi 972988096 1850 VLLQVDDERRNAEQYKDQAD 1869
Cdd:pfam02463 1021 EFLELFVSINKGWNKVFFYL 1040
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1083-1713 |
4.89e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 94.36 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1083 KKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtLDSTAAQQ 1162
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1163 ELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKAnLEKAKQTLENERGELANEVKVLLQG 1242
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKE----IEELEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1243 KGDSEHKRKKVEAQLQELQVKFNEGErvrtELADKVTKLQVELDNVtgllsqsdSKSSKLTKDFSALESQLQDTQELLQE 1322
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEEL--------EERHELYEEAKAKKEELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1323 ENRQKLSlsTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGC-----LETAEEVKRKLQKDL 1397
Cdd:PRK03918 384 LTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCgreltEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1398 EGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVdldhqrqsacnLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREK 1477
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESE-----------LIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1478 ETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDA 1557
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1558 KLRLEVNLQAMKaqferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARK-----KLEMDLKDLEAHIDSA 1632
Cdd:PRK03918 611 EKELEREEKELK-----KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEEL 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1633 NKNRDEAIKQLRKLQaqmkdcmRELDDTRASREEIlaqakeneKKLKSMEAEMIQLQEELAAAE-RAKRQAQQERDELAD 1711
Cdd:PRK03918 686 EKRREEIKKTLEKLK-------EELEEREKAKKEL--------EKLEKALERVEELREKVKKYKaLLKERALSKVGEIAS 750
|
..
gi 972988096 1712 EI 1713
Cdd:PRK03918 751 EI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1000-1579 |
9.02e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.57 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1000 LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST---DLSDQIAELQAQIAE 1076
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1077 LkmqlakkEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQ--------------KRDLGE 1142
Cdd:PRK02224 291 L-------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeslredaddleerAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1143 ELEALKTELEDtldstaAQQELRSKREQevnilkktleeeaktheaqiqemrqkhsqaVEELAEQLEQtkrvkanLEKAK 1222
Cdd:PRK02224 364 EAAELESELEE------AREAVEDRREE------------------------------IEELEEEIEE-------LRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1223 QTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKL 1302
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1303 TKDFSALESQlqdtqellQEENRQKLSLSTKLKQVEDEKNSFREQleeeeeaKHNLEKQIATLHAQVADMKKKME---DS 1379
Cdd:PRK02224 481 EAELEDLEEE--------VEEVEERLERAEDLVEAEDRIERLEER-------REDLEELIAERRETIEEKRERAEelrER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1380 VGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYD-KLEKTKTRLQQELDDllvdldhqRQSACNLEKKQKKFDQLLAEEKT 1458
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNsKLAELKERIESLERI--------RTLLAAIADAEDEIERLREKREA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1459 ISAKYAEERDR-AEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDvgksvheLEKSKRALEQQV 1537
Cdd:PRK02224 618 LAELNDERRERlAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDD-------LQAEIGAVENEL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 972988096 1538 EEmktqLEELEDELQATEDAKLRLEV------NLQAMKAQFERDLQGR 1579
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 ... |
859-1720 |
1.47e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.11 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 859 KVREKQLAAENRLTEMETLQSQLMAEKLQ-LQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 937
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQaKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 938 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1017
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1018 SKSLAKLKNKHEAmitDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1097
Cdd:pfam02463 337 IEELEKELKELEI---KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1098 EAAQKNMALKKIRELESQISELQEDLESERA-----------------SRNKAEKQKRDLGEELEALKTELEDTLDSTAA 1160
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQGklteekeelekqelkllKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1161 QQELRSKREQEVNILKKTLEEEAKTHEA-QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1239
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGgRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1240 LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQEL 1319
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1320 LQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDsvgcletaEEVKRKLQKDLEG 1399
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL--------KKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1400 LSQRHEEKVAAYDKLEKTKTRLQQELDDllvdldhqrqsacNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKET 1479
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEE-------------KSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1480 KALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKL 1559
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1560 RLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVaaRKKLEMDLKDLEAHIDSANKNRDEA 1639
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE--EAEILLKYEEEPEELLLEEADEKEK 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1640 IKQLRKLQAQMKDCM-RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSG 1718
Cdd:pfam02463 951 EENNKEEEEERNKRLlLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
..
gi 972988096 1719 KG 1720
Cdd:pfam02463 1031 KG 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1226 |
3.11e-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: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 861 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEIC---HDLEARVEEEEERCQHL 937
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 938 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1017
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1018 SKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1097
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1098 EAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEEL-EALKTELEDTLDSTAAQQELRSKREQEVNILK 1176
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 972988096 1177 KTLEEEAKTHEAQIQEMrqkhsqavEELAEQLEQTKRVKANLEKAKQTLE 1226
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEY--------EELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1592-1892 |
4.79e-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: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1592 RQVREMEAELEdeRKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAqmkdcmrELDDTRASREEILAQA 1671
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1672 KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELI 1751
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1752 NDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTvKSKYKASITALEAKIAQLEEQLDNETK 1831
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1832 ERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRA 1892
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1109-1924 |
1.74e-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: 89.41 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1109 IRELESQISELQEDLESeraSRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA 1188
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1189 QiqemRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN--ERGELANEVKVLLQGKGDSEHKRK---KVEAQLQEL--Q 1261
Cdd:pfam15921 157 A----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilVDFEEASGKKIYEHDSMSTMHFRSlgsAISKILRELdtE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1262 VKFNEG---------ERVRTELADKVTKL-QVELDNVTGLLSQSDSKSSKLTKDFSALESQ---LQDTQELLQEENRQKL 1328
Cdd:pfam15921 233 ISYLKGrifpvedqlEALKSESQNKIELLlQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1329 SLStkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVAdmkkkmedsvgcLETAEEVKRKLQKDleglsQRHEEKV 1408
Cdd:pfam15921 313 SMY--MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV------------LANSELTEARTERD-----QFSQESG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1409 AAYDKLEKTKTRLqqelddllvdldHQRQSACNLEKKQKK--FDQLLAEEKTISAKYAEERDRaEAEAREKETKALSLAR 1486
Cdd:pfam15921 374 NLDDQLQKLLADL------------HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDR-NMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1487 ALEEAMEQK-AELERLNKQFR---TEMEDLMSSKDDVGKSVHELEKSKRALE---QQVEEMKTQLEELEDELQAT--EDA 1557
Cdd:pfam15921 441 ECQGQMERQmAAIQGKNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIEATnaEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1558 KLRLEVNLQAmkaqfeRDLQGRDEQSEekkkqlvrQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRD 1637
Cdd:pfam15921 521 KLRSRVDLKL------QELQHLKNEGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1638 EAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSS 1717
Cdd:pfam15921 587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1718 GKGALALEEKRRLEARIaqleeeleeeQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENArqqlerQNKELKVKL 1797
Cdd:pfam15921 667 NELNSLSEDYEVLKRNF----------RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS------DGHAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1798 QeMEGTVKSKyKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVD-----------DERRNAEQYKD 1866
Cdd:pfam15921 731 G-MQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNkmagelevlrsQERRLKEKVAN 808
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1867 QA---DKASTRLKQLKRQLeeaeeEAQRANASRRKLQRELeDATETADAMNREVSSLKNKL 1924
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 ... |
967-1572 |
3.93e-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: 87.77 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 967 LEKVTTEAKLKKleEEQIILEDQNCKLAKEKKLLEDRIAEFttnLTEEEEKSKSLAKLKNKHeamitdleerlrreekqr 1046
Cdd:TIGR04523 105 LSKINSEIKNDK--EQKNKLEVELNKLEKQKKENKKNIDKF---LTEIKKKEKELEKLNNKY------------------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1047 QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEeeaaqknmalkKIRELESQISELQEDLESE 1126
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ-----------KNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1127 RASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV---NILKKTLEEEAKTHEAQIQEMRQKHSQavee 1203
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQ---- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1204 laeqlEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKkveaqlqELQVKFNEGERVRTELADKVTKLQV 1283
Cdd:TIGR04523 307 -----DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-------ELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1284 eldnvtgLLSQSDSKSS---KLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEK 1360
Cdd:TIGR04523 375 -------LKKENQSYKQeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1361 QIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELD--DLLVDLDHQRQS 1438
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKdlTKKISSLKEKIE 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1439 ACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSKDD 1518
Cdd:TIGR04523 528 KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKE-------IEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1519 VGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQF 1572
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1537-1912 |
5.41e-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: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1537 VEEMKTQLEELEDELQATEDAKlrlevNLQAMKAQFERDLQG-RDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAAR 1615
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYR-----ELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1616 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1695
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1696 ERAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQLEEELEEEQgntELINDRLKKANLQIDQINTDLNLERSH 1775
Cdd:COG1196 350 EEELEEAEAELAEAE--------------EALLEAEAELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1776 AQKNENARQQLERQNKELKVKLQEMEGTvkskyKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVD 1855
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1856 DERRNAEQYKDQADKASTRLKQ-LKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1912
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
860-1551 |
7.51e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.04 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 860 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHD---LEARVEEEEERCQH 936
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREineISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 937 LQAEKKKMQQniqeleeqleeEESARQKLQLEKVTTEAKLKKLEEEqiiledqncklakeKKLLEDRIAEFTTNLTEEEE 1016
Cdd:PRK03918 226 LEKEVKELEE-----------LKEEIEELEKELESLEGSKRKLEEK--------------IRELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1017 KSKSLAKLKNKHEAMITdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVE 1096
Cdd:PRK03918 281 KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1097 EEAAQKNMALKKIRELEsqiselqedleserasrnkaEKQKRDLGEELEALKTELEdtldstaaqqelrskreqEVNILK 1176
Cdd:PRK03918 359 ERHELYEEAKAKKEELE--------------------RLKKRLTGLTPEKLEKELE------------------ELEKAK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1177 KTLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKANLEKAKQTL-ENERGELANEVKVLLqgkgdsehkrKKVEA 1255
Cdd:PRK03918 401 EEIEEEISKITARIGELKKE----IKELKKAIEELKKAKGKCPVCGRELtEEHRKELLEEYTAEL----------KRIEK 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1256 QLQELQVKFNEGERVRTELaDKVTKLQVELDNVTGLLSQSDSKSSKLTK-DFSALESQLQDTQELLQEENRQKLSLSTKL 1334
Cdd:PRK03918 467 ELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1335 KQVEdEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKkkmedsvgcLETAEEVKRKLqKDLEGLSQRHEEKVAAYDKL 1414
Cdd:PRK03918 546 KELE-KLEELKKKLAELEKKLDELEEELAELLKELEELG---------FESVEELEERL-KELEPFYNEYLELKDAEKEL 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1415 EKTKTRLQQELDDLLVDLDhqrqsacNLEKKQKKFDQLLAEEKTISAKYAEErdraeaEAREKETKALSLARALEEAMEQ 1494
Cdd:PRK03918 615 EREEKELKKLEEELDKAFE-------ELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELAGLRAE 681
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1495 KAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEqQVEEMKTQLEELEDEL 1551
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1018-1709 |
1.13e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 86.89 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1018 SKSLAKLKNKHEAMITDLE--ERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE-----EELQA 1090
Cdd:COG4913 231 VEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLA----ELEYLRAALRLWFAQRRLELLEAEleelrAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1091 ALARVEEEAAQKNMALKKIRELESQIS--------ELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQ 1162
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1163 ELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKV---L 1239
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFvgeL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1240 LQGKGDSEHKRKKVEAQL----------QELQVKFNE-------GERVRTEladKVTKLQVELDNVTgllSQSDSKSSKL 1302
Cdd:COG4913 467 IEVRPEEERWRGAIERVLggfaltllvpPEHYAAALRwvnrlhlRGRLVYE---RVRTGLPDPERPR---LDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1303 TKDFSALESQLQdtQELLQEENRQKlslstklkqVEDEknsfrEQLeeeeeakHNLEKQIaTLHAQVadmkkKMEDSVGC 1382
Cdd:COG4913 541 DFKPHPFRAWLE--AELGRRFDYVC---------VDSP-----EEL-------RRHPRAI-TRAGQV-----KGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1383 LETAEEVKRKLQkdlegLSQRHEEKVAAydkLEKTKTRLQQElddllvdldhqrqsacnLEKKQKKFDQLLAEEKTISAK 1462
Cdd:COG4913 592 KDDRRRIRSRYV-----LGFDNRAKLAA---LEAELAELEEE-----------------LAEAEERLEALEAELDALQER 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1463 YAEERDRAEAEAREKETKalSLARALEEAMEQKAELERLNKQFRT---EMEDLMSSKDDVGKSVHELEKSKRALEQQVEE 1539
Cdd:COG4913 647 REALQRLAEYSWDEIDVA--SAEREIAELEAELERLDASSDDLAAleeQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1540 MKTQLEELEDELQ-ATEDAKLRLEVNLQAMKAQferdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQ-RSMAVAARKK 1617
Cdd:COG4913 725 AEEELDELQDRLEaAEDLARLELRALLEERFAA-----ALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNRE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1618 LEMDLKDLEAHIDSAnknrDEAIKQLRKLqaqmkdcmrelddtrasREEILAQAKENEKKL--KSMEAEMIQLQEELaaa 1695
Cdd:COG4913 800 WPAETADLDADLESL----PEYLALLDRL-----------------EEDGLPEYEERFKELlnENSIEFVADLLSKL--- 855
|
730
....*....|....
gi 972988096 1696 ERAKRQAQQERDEL 1709
Cdd:COG4913 856 RRAIREIKERIDPL 869
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
884-1626 |
2.05e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.79 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 884 EKLQLQEQLQAET-----ELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNiQELEEQLEEE 958
Cdd:TIGR00618 173 FPLDQYTQLALMEfakkkSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS-HAYLTQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 959 ESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLedRIAEfttnlteeeeKSKSLAKLKNKHEAMITDLEER 1038
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAA----------HIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1039 LRREEKQRQElektRRKLEGDSTDLSDQIAELQaqiaelkmQLAKKEEELqaalARVEEEAAQKNMALKKIRELESQISE 1118
Cdd:TIGR00618 320 MRSRAKLLMK----RAAHVKQQSSIEEQRRLLQ--------TLHSQEIHI----RDAHEVATSIREISCQQHTLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1119 LQEDLESERASRNKAEKQKRDLGEEleALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKH- 1197
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQRE--QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHl 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1198 ---SQAVEELaEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGErvrtel 1274
Cdd:TIGR00618 462 qesAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGE------ 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1275 aDKVTKLQVELDNVTGllsQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEA 1354
Cdd:TIGR00618 535 -QTYAQLETSEEDVYH---QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1355 KHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDH 1434
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1435 QRQSAC-NLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAEL--ERLNKQFRTEMED 1511
Cdd:TIGR00618 691 QLTYWKeMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1512 LMS--SKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdeqseEKKKQ 1589
Cdd:TIGR00618 771 TAAlqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL--------EEKSA 842
|
730 740 750
....*....|....*....|....*....|....*..
gi 972988096 1590 LVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLE 1626
Cdd:TIGR00618 843 TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1445 |
6.31e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 6.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 890 EQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERcqhlQAEKKKMQQNIQELEEQLEEEESARQKLQLEK 969
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK----KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 970 VTTEAKlKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNL-----TEEEEKSKSLAKLKNKHEAMITDLEERLRREEK 1044
Cdd:PTZ00121 1484 KADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdeakkAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1045 QRQELEKTRrklEGDSTDLSDQIAELQAQIAELK----MQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQ 1120
Cdd:PTZ00121 1563 KKKAEEAKK---AEEDKNMALRKAEEAKKAEEARieevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1121 EDLESErasRNKAEKQKRDlgEELEALKTELEdtldstaAQQELRSKREQEVniLKKTLEEEAKTHEAQIQEMRQKhsQA 1200
Cdd:PTZ00121 1640 KKEAEE---KKKAEELKKA--EEENKIKAAEE-------AKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEA--KK 1703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1201 VEELAEQLEQTKRVKANLEKAkqtlENERGELANEVKvllqgKGDSEHKRKKVEAQLQE------LQVKFNEGERVRTEL 1274
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKA----EEENKIKAEEAK-----KEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIR 1774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1275 ADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQeeNRQKLSLSTKLKQVEDEKNSFREQ---LEEE 1351
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVI--NDSKEMEDSAIKEVADSKNMQLEEadaFEKH 1852
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1352 EEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDkleKTKTRLQQELDDLLVD 1431
Cdd:PTZ00121 1853 KFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNND---IIDDKLDKDEYIKRDA 1929
|
570
....*....|....
gi 972988096 1432 LDhQRQSACNLEKK 1445
Cdd:PTZ00121 1930 EE-TREEIIKISKK 1942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1032-1798 |
6.85e-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: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1032 ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQ----IAELQA--------------QIAELKMQLAKKE---EELQA 1090
Cdd:pfam15921 112 VIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQlqntVHELEAakclkedmledsntQIEQLRKMMLSHEgvlQEIRS 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1091 ALARVEEEAAQK-----NMALKKIRELESQISELQEDLESERASrnkAEKQKRDLGEELEALKTELEDTLDSTAAQQELR 1165
Cdd:pfam15921 192 ILVDFEEASGKKiyehdSMSTMHFRSLGSAISKILRELDTEISY---LKGRIFPVEDQLEALKSESQNKIELLLQQHQDR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1166 SKR---EQEVNIlkKTLEEEAKTHEAQ----------IQEM-RQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGE 1231
Cdd:pfam15921 269 IEQlisEHEVEI--TGLTEKASSARSQansiqsqleiIQEQaRNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1232 LANEVKVllqgkgdsehkrkkVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALES 1311
Cdd:pfam15921 347 LEKQLVL--------------ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1312 QLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKR 1391
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1392 KLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQkkfdqllaeektisakyaeerdrae 1471
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQ------------------------- 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1472 aeareKETKALSLaraleeameQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEdEL 1551
Cdd:pfam15921 548 -----TECEALKL---------QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK-IL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1552 QATEDAKLrlevnlqamkaqfeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDS 1631
Cdd:pfam15921 613 KDKKDAKI--------------RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1632 ANKN----RDEAIKQLRKLQAQMKDCMRELDDTRASreeilaqakenekkLKSMEAE-------MIQLQEELaAAERAKR 1700
Cdd:pfam15921 679 LKRNfrnkSEEMETTTNKLKMQLKSAQSELEQTRNT--------------LKSMEGSdghamkvAMGMQKQI-TAKRGQI 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1701 QAQQERDELADE-IANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIndRLKKANLQIDQINTDLNLERSHAQKN 1779
Cdd:pfam15921 744 DALQSKIQFLEEaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL--RSQERRLKEKVANMEVALDKASLQFA 821
|
810 820
....*....|....*....|
gi 972988096 1780 EnARQQLERQNKE-LKVKLQ 1798
Cdd:pfam15921 822 E-CQDIIQRQEQEsVRLKLQ 840
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
993-1671 |
1.87e-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: 82.86 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 993 LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelektrRKLegdsTDLSDQIAELQA 1072
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM------RQL----SDLESTVSQLRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1073 QIAELKMQLAKKEEELQAAL----ARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQK-----RDLGEE 1143
Cdd:pfam15921 332 ELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNkrlwdRDTGNS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1144 --LEALKTELEDtldstaaqqelRSKREQEVNILKKTLEEEAKTH-EAQIQEMRQKHS--QAVEELAEQLEQTKRV---- 1214
Cdd:pfam15921 412 itIDHLRRELDD-----------RNMEVQRLEALLKAMKSECQGQmERQMAAIQGKNEslEKVSSLTAQLESTKEMlrkv 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1215 -------KANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRteladkvtKLQVELDN 1287
Cdd:pfam15921 481 veeltakKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR--------NVQTECEA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1288 VTGLLSQSDsksskltKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1367
Cdd:pfam15921 553 LKLQMAEKD-------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1368 QVADMKKKMEDSVGC----LETAEEVKRKLQK----------DLEGLSQRHEEKVAAY----DKLEKTKTRLQQELDDLL 1429
Cdd:pfam15921 626 RVSDLELEKVKLVNAgserLRAVKDIKQERDQllnevktsrnELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQ 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1430 VDLDHQRQSACNLEKKQKKFDQL-LAEEKTISAKyaeerdRAEAEARekETKALSLARALEEAMEQKAELERLNKQFRTE 1508
Cdd:pfam15921 706 SELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK------RGQIDAL--QSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1509 MEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERD---LQGRDEQSEE 1585
Cdd:pfam15921 778 LSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDvkeLQGPGYTSNS 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1586 KKKQLVRQVREMEAELEDERKQRSMAvaarkklemdlKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRE 1665
Cdd:pfam15921 858 SMKPRLLQPASFTRTHSNVPSSQSTA-----------SFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKA 926
|
....*.
gi 972988096 1666 EILAQA 1671
Cdd:pfam15921 927 EDKGRA 932
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
974-1854 |
2.16e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 82.79 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 974 AKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEeeksksLAKLKNKHEAMITDLEERLRREEKQRQELEKTR 1053
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ------LNDLYHNHQRTVREKERELVDCQRELEKLNKER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1054 RKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAalarveeeaaqknmalkkiRELESQISELQEDLESERASRNKA 1133
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS-------------------LATRLELDGFERGPFSERQIKNFH 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1134 EKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ------AVEELAEQ 1207
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSSDRILEL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1208 LEQTKRVKANLEKAKQTLENErgELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDN 1287
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTE--TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1288 VtgllSQSDSKSSKLTKDFSAlESQLQDTQEllqeenrqklSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1367
Cdd:TIGR00606 555 K----SRHSDELTSLLGYFPN-KKQLEDWLH----------SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1368 QVADMKKKMEDSVGC------LETAEEVKRKLQKDL--------------EGLSQRHEEKVAAYDKLEKTKTRLQQELDD 1427
Cdd:TIGR00606 620 QLSSYEDKLFDVCGSqdeesdLERLKEEIEKSSKQRamlagatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1428 LLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARaleEAMEQKAELERLNKQFRT 1507
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR---DIQRLKNDIEEQETLLGT 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1508 EMEDLMSSKD---DVGksvhelekSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERD-----LQGR 1579
Cdd:TIGR00606 777 IMPEEESAKVcltDVT--------IMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskIELN 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1580 DEQSEEKKKQlVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMreldd 1659
Cdd:TIGR00606 849 RKLIQDQQEQ-IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ----- 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1660 traSREEILAQAKENEKKLKSMEAEMI--QLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIaQL 1737
Cdd:TIGR00606 923 ---QEKEELISSKETSNKKAQDKVNDIkeKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI-NE 998
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1738 EEELEEEQGNTELINDRLKKANLQIDQINTDLN-LERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALE 1816
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKeVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQK 1078
|
890 900 910
....*....|....*....|....*....|....*...
gi 972988096 1817 akiaQLEEQLDNETKERQAacKQVRRTEKKLKDVLLQV 1854
Cdd:TIGR00606 1079 ----GYEKEIKHFKKELRE--PQFRDAEEKYREMMIVM 1110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1201-1925 |
3.28e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.04 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1201 VEELAEQLEQTKRVKANLEKAkQTLENERGELanEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1280
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERY-QALLKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1281 LQVELDNVTGLLSQ-SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLE 1359
Cdd:TIGR02169 270 IEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1360 KQIATLHAQVADMKKKMEDSVgclETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKT---RLQQELDDLLVDLDHQR 1436
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLR---AELEEVDKEFAETRDELKDYREKLEKLKREINELKReldRLQEELQRLSEELADLN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1437 QSACNLEKKQKKFDqllaeektisakyaEERDRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSK 1516
Cdd:TIGR02169 427 AAIAGIEAKINELE--------------EEKEDKALEIKKQEWK-------LEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1517 DDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGR-------DEQSEEKKKQ 1589
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRlnnvvveDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1590 LVRQVREMEAELEDERKQRSMAVAARKKLE-------MDLKDLEAHIDSANKN--RD----EAIKQLRKL--QAQMKDCM 1654
Cdd:TIGR02169 566 LLKRRKAGRATFLPLNKMRDERRDLSILSEdgvigfaVDLVEFDPKYEPAFKYvfGDtlvvEDIEAARRLmgKYRMVTLE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1655 RELDD--------TRASREEILAQAKENEKkLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEE 1726
Cdd:TIGR02169 646 GELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS-------RK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1727 KRRLEARIaqleeeleeeqgntELINDRLKKANLQIDQINTDLnleRSHAQKNENARQQLERQNKELkvklQEMEgTVKS 1806
Cdd:TIGR02169 718 IGEIEKEI--------------EQLEQEEEKLKERLEELEEDL---SSLEQEIENVKSELKELEARI----EELE-EDLH 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1807 KYKASITALEAKIA-----QLEEQLDNETKERQAACKQVRRTEKKLKDVLL---QVDDERRNAEQY----KDQADKASTR 1874
Cdd:TIGR02169 776 KLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQELQEQridlKEQIKSIEKE 855
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1875 LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLR 1925
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1310-1926 |
4.14e-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: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1310 ESQLQDTQE-------LLQEENRQKLSLSTKLKQVEDEKNsFREQLEEEEEA-----KHNLEKQIATLHAQVADMKKKME 1377
Cdd:TIGR02168 178 ERKLERTREnldrledILNELERQLKSLERQAEKAERYKE-LKAELRELELAllvlrLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1378 DsvgcletAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 1457
Cdd:TIGR02168 257 E-------LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1458 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkddvgksVHELEKSKRALEQQV 1537
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-------VAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1538 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKK 1617
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELK---ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1618 LEMDLKDLEAHIDSAnKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQ--LQEELAAA 1695
Cdd:TIGR02168 480 AERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQavVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1696 ERAkrqaqqerdelADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQI------------- 1762
Cdd:TIGR02168 559 KKA-----------IAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlv 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1763 -DQINTDLNLERSHAQKNENARQQLERQNKE-LKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQV 1840
Cdd:TIGR02168 628 vDDLDNALELAKKLRPGYRIVTLDGDLVRPGgVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1841 RRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSL 1920
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
....*.
gi 972988096 1921 KNKLRR 1926
Cdd:TIGR02168 788 EAQIEQ 793
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
860-1685 |
1.06e-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: 80.48 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 860 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELrarLTAKKQELEEICHDLEARVEEEEERCQHLQA 939
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKV---FQGTDEQLNDLYHNHQRTVREKERELVDCQR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 940 EKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEE--EEK 1017
Cdd:TIGR00606 327 ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIErqEDE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1018 SKSLAKLKNkheamitDLEERLRREEKQRQELEKTR----RKLEGDSTDLSDQIAELQAQIAELKM------QLAKKEEE 1087
Cdd:TIGR00606 407 AKTAAQLCA-------DLQSKERLKQEQADEIRDEKkglgRTIELKKEILEKKQEELKFVIKELQQlegssdRILELDQE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1088 LQAALARVEEEAAQKNMALKKIRELESQiselQEDLESERASRNKAEKQKrDLGEELEALKTELEDTLDSTAAQQELRSK 1167
Cdd:TIGR00606 480 LRKAERELSKAEKNSLTETLKKEVKSLQ----NEKADLDRKLRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1168 REQEVNIL---------KKTLEEEAKTHEAQIQEMRQKHSQAVEELAeQLEQTKRVKANLEKAKQTLENERGELANEVKV 1238
Cdd:TIGR00606 555 KSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA-SLEQNKNHINNELESKEEQLSSYEDKLFDVCG 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1239 LLQGKGDSEHKRKKVE---AQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQD 1315
Cdd:TIGR00606 634 SQDEESDLERLKEEIEkssKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKS 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1316 TQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEE------V 1389
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtI 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1390 KRKLQKDLEGLSQRHEEKVAAYD--KLEKTKTRLQQELDDLLVDLDHQRQSACNLEK----KQKKFDQL------LAEEK 1457
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKliqdQQEQIQHLksktneLKSEK 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1458 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVH-ELEKSKRALEQQ 1536
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1537 VEEMKTQLEELEDelqATEDAKLRLEVNLQAMKAQFerdlqgrdEQSEEKKKQLVRQVREMEAELEDERKQRSMAV--AA 1614
Cdd:TIGR00606 954 HGYMKDIENKIQD---GKDDYLKQKETELNTVNAQL--------EECEKHQEKINEDMRLMRQDIDTQKIQERWLQdnLT 1022
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1615 RKKLEMDLKDLEAHIDSANKNRDEaiKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1685
Cdd:TIGR00606 1023 LRKRENELKEVEEELKQHLKEMGQ--MQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
842-1147 |
1.23e-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: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 842 QVSRQEEEMMAKEEELVKVREKQLAAEN-------RLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQ 914
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 915 ELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLA 994
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 995 KEKK-------LLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQI 1067
Cdd:TIGR02168 845 EQIEelsedieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1068 AELQAQIAELKMQLAKKEEELqAALARVEEEAAQKNMALK---------KIRELESQISEL-------QEDLESERASRN 1131
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERL-SEEYSLTLEEAEALENKIeddeeearrRLKRLENKIKELgpvnlaaIEEYEELKERYD 1003
|
330
....*....|....*.
gi 972988096 1132 KAEKQKRDLGEELEAL 1147
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETL 1019
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1009-1733 |
1.46e-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: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1009 TNLTEEEEKSKSL-AKLKNKHEAmITDLEERLRREEKQRQELEKTRR-KLEGDSTDLSDQIAELQAQIAELKMQLAKKEE 1086
Cdd:pfam12128 244 TKLQQEFNTLESAeLRLSHLHFG-YKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1087 ELQAA--------LARVEEEAAQKNMALKKIRELESQ-------------ISELQEDLESERASRNKAE----KQKRD-L 1140
Cdd:pfam12128 323 ELEALedqhgaflDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdVTAKYNRRRSKIKEQNNRDiagiKDKLAkI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1141 GEELEALKTELEDTLDstAAQQELRSKREQEVNILKktleEEAKTHEAQIQEM--RQKHSQAVEELAEQLEQTKrvkANL 1218
Cdd:pfam12128 403 REARDRQLAVAEDDLQ--ALESELREQLEAGKLEFN----EEEYRLKSRLGELklRLNQATATPELLLQLENFD---ERI 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1219 EKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSK 1298
Cdd:pfam12128 474 ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGK 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1299 --SSKLTK----DFSALESQLQDTQEL----LQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQ 1368
Cdd:pfam12128 554 viSPELLHrtdlDPEVWDGSVGGELNLygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1369 VADMKKKMEDSVGCLETAEEVKRKLqkdleglsqrHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSacnLEKKQKK 1448
Cdd:pfam12128 634 LEKASREETFARTALKNARLDLRRL----------FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1449 FDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMedlmsskddvgksvheleK 1528
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS-GAKAELKALETWYKRDL------------------A 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1529 SKRALEQQVEEMKTQLEELEDELQatedaklRLEVNLQAMkAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDerkqr 1608
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIE-------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISE----- 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1609 smavaarkkLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDtRASREEILAQAKENEKKLKSMEAEMIQL 1688
Cdd:pfam12128 826 ---------LQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC-EMSKLATLKEDANSEQAQGSIGERLAQL 895
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 972988096 1689 QEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR 1733
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDH 940
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
824-1396 |
2.13e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 824 KLRNWQWWRLFTKVKPLLQVSRQEEEMMAKE---EELVKVREKQLAAENRLTEMETLQSQLmaeKLQLQEQLQAEtELCA 900
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEArkaDELKKAEEKKKADEAKKAEEKKKADEA---KKKAEEAKKAD-EAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 901 EAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLE 980
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 981 EEQIILEDQNCKLAKEKKLLEdriaefttnLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelEKTRRKLEgds 1060
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADE---------AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA--EEAKKKAE--- 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1061 tdlsdqiAELQAQIAELKMQLAKKEEELQaalaRVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRdl 1140
Cdd:PTZ00121 1468 -------EAKKADEAKKKAEEAKKADEAK----KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK-- 1534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1141 gEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKA---- 1216
Cdd:PTZ00121 1535 -KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeak 1613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1217 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADK-----VTKLQVELDNVTGL 1291
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeAKKAEEDEKKAAEA 1693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1292 LSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSfREQLEEEEEAKHNLEKQIATLHAQVAD 1371
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK-AEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
570 580
....*....|....*....|....*
gi 972988096 1372 MKKKMEDSVGCLETAEEVKRKLQKD 1396
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
857-1416 |
3.15e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 857 LVKVREKQLAA-ENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQ 935
Cdd:PRK03918 194 LIKEKEKELEEvLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK----LEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 936 HLQAEKKKMQQNIQELEEQLEEEESARqKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1015
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1016 EKSKSLAKLKNKHEA--MITDLEERLRREEKQR-----QELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEEL 1088
Cdd:PRK03918 349 ELEKRLEELEERHELyeEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELK----KEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1089 QAALARVE-------------EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKteLEDTL 1155
Cdd:PRK03918 425 KKAIEELKkakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1156 DstaaqqELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ--AVEELAEQLEQTKRVKANLEKAKQTLENERGELA 1233
Cdd:PRK03918 503 E------QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1234 NEVKVLlqGKGDSEHKRKKVEaQLQELQVKFNEGERVRTELADKVTKLQVELDNvtglLSQSDSKSSKLTKDFSALESQL 1313
Cdd:PRK03918 577 KELEEL--GFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEELRKEL 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1314 QDTQELLQEENRQKlsLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKmedsvgcletAEEVKrKL 1393
Cdd:PRK03918 650 EELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA----------KKELE-KL 716
|
570 580
....*....|....*....|...
gi 972988096 1394 QKDLEGLsQRHEEKVAAYDKLEK 1416
Cdd:PRK03918 717 EKALERV-EELREKVKKYKALLK 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
863-1596 |
4.50e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 863 KQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAE----AEELRARLTAKKQELEEICHDLEARVEeeeercqhlq 938
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkkAEEKKKADEAKKAEEKKKADEAKKKAE---------- 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 939 aEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILE--DQNCKLAKEKKLLEDRIAEFTTNLTEEEE 1016
Cdd:PTZ00121 1313 -EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1017 KSKslaKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlAKKEEELQAALARVE 1096
Cdd:PTZ00121 1392 KAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK---KKAEEAKKAEEAKKK 1465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1097 EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILK 1176
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1177 KTLEEEAKTHEAQIQEMRQKHSQAVEElAEQLEQTKRVKANLEKAKQTLENERGELANEVKvllqgKGDSEHKRKKVEAQ 1256
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK-----KMKAEEAKKAEEAK 1619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1257 LQELQVKFNEGERVRTELADKVTKLQVEldnvtgllsqsdsKSSKLTKDFSalESQLQDTQELLQEENRQKlsLSTKLKQ 1336
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKK-------------KAEELKKAEE--ENKIKAAEEAKKAEEDKK--KAEEAKK 1682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1337 VEDEKNSFREQLEEEEEAKHNLEKqiatLHAQVADMKKKMEDsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEK 1416
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEE----LKKKEAEEKKKAEE----LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1417 TKTRLQQElddllvdldhQRQSACNLEKKQKKFDQLLAEEktisAKYAEERDRAEAEAREKETKAlSLARALEEAMEQKA 1496
Cdd:PTZ00121 1755 EKKKIAHL----------KKEEEKKAEEIRKEKEAVIEEE----LDEEDEKRRMEVDKKIKDIFD-NFANIIEGGKEGNL 1819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1497 ELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEE-------MKTQLEELEDELQATEDAKLRLEVNLQAMK 1569
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEdgnkeadFNKEKDLKEDDEEEIEEADEIEKIDKDDIE 1899
|
730 740 750
....*....|....*....|....*....|....*
gi 972988096 1570 AQF-ERDLQGRDEQS-------EEKKKQLVRQVRE 1596
Cdd:PTZ00121 1900 REIpNNNMAGKNNDIiddkldkDEYIKRDAEETRE 1934
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1037-1865 |
4.90e-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: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1037 ERLRREEKQRQELEKTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKnmalKKIRELE 1113
Cdd:COG3096 282 ELSERALELRRELFGARRQL----AEEQYRLVEMARELEELSARESDLEQDYQAAsdhLNLVQTALRQQ----EKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1114 SQISELQEDLESERASRNKAEKQKRDLGEELEA-------LKTELED---TLDS--TAA---QQELRSKRE-QEVNILKK 1177
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVqqTRAiqyQQAVQALEKaRALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1178 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN-----ERGELANEVKVLLQGKGDSEH---K 1249
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYRSQQAlaqR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1250 RKKVEAQLQELQVKFNEGERVRTELADkvtklqveldnvtglLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1329
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEE---------------FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1330 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVadmkkkmedsvGC-LETAEEVKRKLQKDLEGLSQRHEEKv 1408
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS-----------GEaLADSQEVTAAMQQLLEREREATVER- 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1409 aayDKLEKTKTRLQQELDDLlvdldHQRQSACNLEKKQKKfDQ----LLAE---EKTISakyaeerDRAEAEAREKETKA 1481
Cdd:COG3096 647 ---DELAARKQALESQIERL-----SQPGGAEDPRLLALA-ERlggvLLSEiydDVTLE-------DAPYFSALYGPARH 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1482 LSLARALEEAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEK------SKRAL---------------- 1533
Cdd:COG3096 711 AIVVPDLSAVKEQLAGLEDC-------PEDLYliegdpDSFDDSVFDAEELEDavvvklSDRQWrysrfpevplfgraar 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1534 EQQVEEMKTQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED---- 1603
Cdd:COG3096 784 EKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEAELAALRQRRSELERELAQhraq 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1604 ERKQRSMAVAARKKLEMdlkdLEAHIDSANKNRDEAikqlrkLQAQMKDCMRELDDTRASREEI------LAQAKENEKK 1677
Cdd:COG3096 859 EQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELDAAQEAQAFIqqhgkaLAQLEPLVAV 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1678 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN----SSGKGALALEEKR----RLEARIAQLEEELEEEqgnte 1749
Cdd:COG3096 929 LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRrphfSYEDAVGLLGENSdlneKLRARLEQAEEARREA----- 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1750 liNDRLKKANLQIDQINTDL-NLERSHAQKNENArQQLERQNKELKVKL-QEMEGTV---KSKYKASITALEAKIAQLEE 1824
Cdd:COG3096 1004 --REQLRQAQAQYSQYNQVLaSLKSSRDAKQQTL-QELEQELEELGVQAdAEAEERArirRDELHEELSQNRSRRSQLEK 1080
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 972988096 1825 QLDNETKERQAACKQVRRTEKKLKdvllqvdDERRNAEQYK 1865
Cdd:COG3096 1081 QLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAK 1114
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1111-1923 |
1.94e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1111 ELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA-- 1188
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDar 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1189 QIQEMRQKHSQAVEELAEQLEQTKRVKANlEKAKQTLENERGELANEVKVLLQGKgDSEHKRKKVEAQLQELQVKFNEGE 1268
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARKAEDARKAEEA-RKAEDAKKAEAARKAEEVRKAEELR-KAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1269 RVRTEL-ADKVTKLQ-VELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKlslSTKLKQVEdEKNSFRE 1346
Cdd:PTZ00121 1219 KAEDAKkAEAVKKAEeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAE-EKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1347 QLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVgclETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELD 1426
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK---KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1427 DLLVDLDHQRQSACNLEKKQKkfdqllAEEktisAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFR 1506
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKK------ADE----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1507 TEME-DLMSSKDDVGKSVHELEKsKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEE 1585
Cdd:PTZ00121 1442 EAKKaDEAKKKAEEAKKAEEAKK-KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1586 KKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQmkdcmrELDDTRASRE 1665
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE------EAKKAEEARI 1594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1666 EILAQAKENEKKLKSmeaemiqlqEELAAAERAKRQAQQERDELADEIANSSGKGALAlEEKRRLEariaqleeeleeeq 1745
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKA---------EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA-EEKKKAE-------------- 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1746 gntelindRLKKANlqidqintdlnlERSHAQKNENARQQLERQNKELKVKLQEMEgtvkSKYKASITALEAKIAQLEEQ 1825
Cdd:PTZ00121 1651 --------ELKKAE------------EENKIKAAEEAKKAEEDKKKAEEAKKAEED----EKKAAEALKKEAEEAKKAEE 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1826 LDNETKERQAACKQVRRTEKKLKdvlLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELED 1905
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENK---IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
810
....*....|....*...
gi 972988096 1906 ATETADAMNREVSSLKNK 1923
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1164-1733 |
3.03e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1164 LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnEVKVLlqgk 1243
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETL---- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1244 gdsehkrkkvEAQLQELQVKFNEGERVRTELADKVTKLQVEL----DNVTGLLSQSDsksskltkdfsaLESQLQDTQEL 1319
Cdd:PRK02224 257 ----------EAEIEDLRETIAETEREREELAEEVRDLRERLeeleEERDDLLAEAG------------LDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1320 LQEE-NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLE 1398
Cdd:PRK02224 315 RREElEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1399 GLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAkyaeerdraeaearEKE 1478
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEC--------------GQP 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1479 TKALSLARALEEAMEQKAELERLNKQFRTEMEDLmSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDak 1558
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE-- 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1559 lRLEvNLQAMKAQFERDLQGRDEQSEEKKKQlVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDE 1638
Cdd:PRK02224 538 -RAE-ELRERAAELEAEAEEKREAAAEAEEE-AEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1639 aikqlRKLQAQMKDCMRELDDTRASREEILAqAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSG 1718
Cdd:PRK02224 615 -----REALAELNDERRERLAEKRERKRELE-AEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
570
....*....|....*
gi 972988096 1719 KgalaLEEKRRLEAR 1733
Cdd:PRK02224 689 E----LEELEELRER 699
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1002-1243 |
3.98e-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: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1002 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1081
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1082 AKKEEELQAALArveeeAAQKNMALKKIRELESQiselQEDLESERASR--NKAEKQKRDLGEELEALKTELEDTLDSTA 1159
Cdd:COG4942 100 EAQKEELAELLR-----ALYRLGRQPPLALLLSP----EDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1160 AQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1239
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....
gi 972988096 1240 LQGK 1243
Cdd:COG4942 251 LKGK 254
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
963-1712 |
4.52e-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: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 963 QKLQLEKVTTEAKLK----KLEEEQIILEDQNcKLAKEKKLLEDRIaefTTNLTEEEEKSKSLAKLKNKHEAMITDLEER 1038
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1039 LRREEKQRQELEKTRRKLEGDSTDLSDQIAelqaqiaelKMQLAKKEEELQAALARVEEEAaqknmalkKIRELESQISE 1118
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIE---------KMILAFEELRVQAENARLEMHF--------KLKEDHEKIQH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1119 LQEDLESERasrNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQevnilkktLEEEAKTHEAQIQEMRQKHS 1198
Cdd:pfam05483 227 LEEEYKKEI---NDKEKQVSLLLIQITEKENKMKDL---TFLLEESRDKANQ--------LEEKTKLQDENLKELIEKKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1199 QAVEELAEqleqtkrVKANLEKAKQTLENERGELANEVKVLLQgkgdsehKRKKVEAQLQELQVKFNEGERVRTELADKV 1278
Cdd:pfam05483 293 HLTKELED-------IKMSLQRSMSTQKALEEDLQIATKTICQ-------LTEEKEAQMEELNKAKAAHSFVVTEFEATT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1279 TKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVE---DEKNSFREQLEEEEEAK 1355
Cdd:pfam05483 359 CSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEkllDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1356 HNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQ 1435
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1436 RQSACNLEKKQKKfdqLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS 1515
Cdd:pfam05483 519 QEDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1516 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1595
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLE 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1596 EMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENE 1675
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
730 740 750
....*....|....*....|....*....|....*..
gi 972988096 1676 KKLKSmeaemiQLQEELAAAERAKRQAQQERDELADE 1712
Cdd:pfam05483 756 LSLKK------QLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1383-1926 |
6.36e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1383 LETAEEvKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACN---------LEKKQKKFDQLL 1453
Cdd:COG4913 244 LEDARE-QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRaelarleaeLERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1454 AEEKTISAKYAE-----------ERDRAEAEAREKETKALSLARALEeAMEQKAELERlnKQFRTEMEDLMSSKDDVGKS 1522
Cdd:COG4913 323 EELDELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLA-ALGLPLPASA--EEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1523 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ-----------SEEKKKQ-- 1589
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelievrPEEERWRga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1590 ------------LV-----RQVRE------MEAELEDERKQRSMAVAARKKLE-------MDLKD------LEAHIdsaN 1633
Cdd:COG4913 480 iervlggfaltlLVppehyAAALRwvnrlhLRGRLVYERVRTGLPDPERPRLDpdslagkLDFKPhpfrawLEAEL---G 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1634 KNRD----EAIKQLRK------LQAQMKD--CMRELDDTRASREE-ILAQakENEKKLKSMEAEMIQLQEELAAAERAKR 1700
Cdd:COG4913 557 RRFDyvcvDSPEELRRhpraitRAGQVKGngTRHEKDDRRRIRSRyVLGF--DNRAKLAALEAELAELEEELAEAEERLE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1701 QAQQERDeladeianssgkgalALEEKRRLEARIAQleeeleeeqgntelindrlkkanLQIDQINTDLnLERSHAQKnE 1780
Cdd:COG4913 635 ALEAELD---------------ALQERREALQRLAE-----------------------YSWDEIDVAS-AEREIAEL-E 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1781 NARQQLERQNKELkvklqemegtvkskykasitaleakiAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRN 1860
Cdd:COG4913 675 AELERLDASSDDL--------------------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1861 AEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETAdamNREVSSLKNKLRR 1926
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL---RARLNRAEEELER 791
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1386-1963 |
1.48e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1386 AEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAE 1465
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1466 ERDRAEAEAREKETKALSLARALEEAmeQKAELERLNKQFR-TEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1544
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAA--RKAEEERKAEEARkAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKF 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1545 EELEDELQATEDAKLRLEvnlQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERK----------QRSMAVAA 1614
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAE---EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadeakkkaeeAKKKADAA 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1615 RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMK---------DCMRELDDTRASREEILAQAKENEKK---LKSME 1682
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeeakkkaDAAKKKAEEKKKADEAKKKAEEDKKKadeLKKAA 1414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1683 A------EMIQLQEELAAAERAKRQAQQERDelADEIANSSGKGALALEEKRRLE-ARIAQLEEELEEEQGNTELINDRL 1755
Cdd:PTZ00121 1415 AakkkadEAKKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEeAKKADEAKKKAEEAKKADEAKKKA 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1756 KKANLQIDQINTDLNLERS--HAQKNENARQQLERQNKELKVKLQEMEGTVKSKykasiTALEAKIAQLEEQLDNETKER 1833
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-----KADELKKAEELKKAEEKKKAE 1567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1834 QAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQleeaeeEAQRANASRRKLQRELEDATETADAM 1913
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA------EEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1914 NREVSSLKNKLRRGDLPFVVPR-RMARKGAGDGSDEEVDGKADGAEAKPAE 1963
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAaEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
862-1322 |
1.53e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 862 EKQLAAENRLTEMETLQSQlmAEKLQLQEQLQAE----TELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 937
Cdd:PRK02224 228 QREQARETRDEADEVLEEH--EERREELETLEAEiedlRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 938 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1017
Cdd:PRK02224 306 DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1018 SKSLaklknkhEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1097
Cdd:PRK02224 386 IEEL-------EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECG 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1098 EAAQKNMALKKIRELESQISELQEDLESERASRNKAEKqKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKK 1177
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1178 TLEEEAKTHEAQIQEMRQKHSQAvEELAEQLEQTKRVKANLEKAKQTLENERGELAN--EVKVLLQGKGDSEHKRKKVEA 1255
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAA-AEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKRE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1256 QLQELQVKFNE-----GERVRtELADKVTKLQVE------------LDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQE 1318
Cdd:PRK02224 617 ALAELNDERRErlaekRERKR-ELEAEFDEARIEearedkeraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
....
gi 972988096 1319 LLQE 1322
Cdd:PRK02224 696 LRER 699
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1044-1871 |
1.56e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.08 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1044 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDL 1123
Cdd:TIGR00618 124 KKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1124 ESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQevnilkktleeeaKTHEAQIQEMRQKHSQAVEE 1203
Cdd:TIGR00618 204 QLLTLCTPCMPDTYHERKQVLEKELKHLRE------ALQQTQQSHAY-------------LTQKREAQEEQLKKQQLLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1204 LAEQLEQTKRVKANLEKAkqtleNERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRteladkvtklqv 1283
Cdd:TIGR00618 265 LRARIEELRAQEAVLEET-----QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL------------ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1284 eldnvtgllsqsdSKSSKLTKDFSALESQLQDTQELLQEENRqklslstkLKQVEDEKNSFREQLEEeeeaKHNLEKQIA 1363
Cdd:TIGR00618 328 -------------MKRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQ----QHTLTQHIH 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1364 TLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLE 1443
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1444 KKQKKFDQLLAEEKtisakyaeerDRAEAEAREKETKALSLARALEEAmEQKAELERLNKQFRTEMEDLMSSKDDVGK-- 1521
Cdd:TIGR00618 463 ESAQSLKEREQQLQ----------TKEQIHLQETRKKAVVLARLLELQ-EEPCPLCGSCIHPNPARQDIDNPGPLTRRmq 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1522 ----SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQgrdeqseekkkQLVRQVREM 1597
Cdd:TIGR00618 532 rgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN-----------ITVRLQDLT 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1598 EAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCM-RELDDTRASREEILAQAKENEK 1676
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQeRVREHALSIRVLPKELLASRQL 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1677 KLKSMEAEMIQL---QEELAAAERAKRQAQQ---ERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNtEL 1750
Cdd:TIGR00618 681 ALQKMQSEKEQLtywKEMLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLK-AR 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1751 INDRLKKANLQIDQINTDLNLERShAQKNENARQQLERQNKELKVKLQEMEGTVKSkYKASITALEAKIAQLEEQLDNET 1830
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHL-AAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFLSRL 837
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 972988096 1831 KERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKA 1871
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1015-1501 |
2.42e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1015 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR 1094
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1095 VEEEAAQKNMAL--KKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV 1172
Cdd:COG4717 132 QELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1173 NILKKTLEEEAKTHEAQIQEMRQKhsQAVEELAEQLEQTKR----------VKANLEKAKQTLENERGELANEVKVLLQG 1242
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENE--LEAAALEERLKEARLllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1243 KGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQlqdTQELLQE 1322
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL---EEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1323 ENRQKLSLSTKLKQVEDEKnSFREQLeEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGcletaeevkrklQKDLEGLSQ 1402
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEE-ELRAAL-EQAEEYQELKEELEELEEQLEELLGELEELLE------------ALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1403 RHEEKVAAYDKLEKTKTRLQQElddllvdldhqrQSACNLEKKQKKFDQLLAEektisAKYAEERDRAEAEAREKETKAL 1482
Cdd:COG4717 433 ELEELEEELEELEEELEELREE------------LAELEAELEQLEEDGELAE-----LLQELEELKAELRELAEEWAAL 495
|
490
....*....|....*....
gi 972988096 1483 SLARALEEAMEQKAELERL 1501
Cdd:COG4717 496 KLALELLEEAREEYREERL 514
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1069-1799 |
3.99e-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: 71.59 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1069 ELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERasrNKAEKQKRDLGEELEALK 1148
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK---DKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1149 TEledtldstaaqQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQTLENE 1228
Cdd:TIGR04523 114 ND-----------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1229 RGELANEVKvllqgkgDSEHKRKKVEAQLQELQVKFNEgervRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSA 1308
Cdd:TIGR04523 182 KLNIQKNID-------KIKNKLLKLELLLSNLKKKIQK----NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1309 LESQLQDTQELLQEENRQklsLSTKLKQVEDEKNSFReqleeeeeakhNLEKQIATLHAQVADMKKKMEDSV-----GCL 1383
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQ---LSEKQKELEQNNKKIK-----------ELEKQLNQLKSEISDLNNQKEQDWnkelkSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1384 ETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEK-KQKKFDQLLAEEKTISAk 1462
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQIND- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1463 yaeerdrAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1542
Cdd:TIGR04523 396 -------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1543 QLEELEDELQATEdaklrlevnlqamkaqferdlqgrdEQSEEKKKQLVRQVREMEaELEDERKQrsmavaarkkLEMDL 1622
Cdd:TIGR04523 469 QLKVLSRSINKIK-------------------------QNLEQKQKELKSKEKELK-KLNEEKKE----------LEEKV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1623 KDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMREL--DDTRASREEILAQAKENEKKLKsmeaemiQLQEELAAAERAKR 1700
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIE-------ELKQTQKSLKKKQE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1701 QAQQERDELADEIANSSGKgalaLEEKrrlEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNE 1780
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKE----IEEK---EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
730
....*....|....*....
gi 972988096 1781 NARQQLERQNKELKVKLQE 1799
Cdd:TIGR04523 659 NKWPEIIKKIKESKTKIDD 677
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1480-1936 |
4.19e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1480 KALSL-ARALeeAMEQkaeLERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAlEQQVEEMKTQ---LEELEDELQATE 1555
Cdd:COG4913 192 KALRLlHKTQ--SFKP---IGDLDDFVREYMLEEPDTFEAADALVEHFDDLERA-HEALEDAREQielLEPIRELAERYA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1556 DAKLRLEVN------LQAMKAQFERDL-QGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMD-LKDLEA 1627
Cdd:COG4913 266 AARERLAELeylraaLRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1628 HIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEmiqLQEELAAAERAKRQAQQERD 1707
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1708 ELADEIANSSGKGALALEEKRRLEARIAQLEEELEEE---------------------------QGNT------------ 1748
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelievrpeeerwrgaiervlggFALTllvppehyaaal 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1749 ELINDRLKKANLQIDQINTDL-NLERSHAQKN--------------ENARQQLERQNKELKVK-LQEM---------EGT 1803
Cdd:COG4913 503 RWVNRLHLRGRLVYERVRTGLpDPERPRLDPDslagkldfkphpfrAWLEAELGRRFDYVCVDsPEELrrhpraitrAGQ 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1804 VKSKY---------------------KASITALEAKIAQLEEQLdNETKERQAACKQVRRTEKKLKDVLLQVDD------ 1856
Cdd:COG4913 583 VKGNGtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEyswdei 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1857 -------ERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGDL 1929
Cdd:COG4913 662 dvasaerEIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
....*..
gi 972988096 1930 PFVVPRR 1936
Cdd:COG4913 742 LARLELR 748
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1034-1208 |
4.40e-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: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1034 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMAlKKIRELE 1113
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1114 SqiseLQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldstaaqQELRSKREQEVNILKKTLEEEAKTHEAQIQEM 1193
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 972988096 1194 RQKHSQAVEELAEQL 1208
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
857-1618 |
6.62e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 71.23 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 857 LVKVREKQLAAE-----NRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEE 931
Cdd:TIGR00606 346 LVEQGRLQLQADrhqehIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 932 ERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKL--EEEQIILEDQNCKLAKEKKLLEDRIAEFTT 1009
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIleLDQELRKAERELSKAEKNSLTETLKKEVKS 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1010 NLTEEEEKSKSLAKL------KNKHEAMITDLE----------ERLRREEKQ--------------RQELEKTRRKLEGD 1059
Cdd:TIGR00606 506 LQNEKADLDRKLRKLdqemeqLNHHTTTRTQMEmltkdkmdkdEQIRKIKSRhsdeltsllgyfpnKKQLEDWLHSKSKE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1060 STDLSDQIAELQAQIAEL---KMQLAKKEEELQAALARVEEeaaqKNMALKKIRELESQISELQEDLESERASRN----- 1131
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLeqnKNHINNELESKEEQLSSYED----KLFDVCGSQDEESDLERLKEEIEKSSKQRAmlaga 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1132 --------------------------KAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1185
Cdd:TIGR00606 662 tavysqfitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1186 HEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERgELANEVKVLLQGKGDSEHKRKKVEAQLQELQVkfN 1265
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERFQMELKDVERKIAQQAAKLQG--S 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1266 EGERVRTELADKVTKLQVELDNVTgllsqsdsksskltkdfsaleSQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1345
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVV---------------------SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIG 877
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1346 EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKtrlqqel 1425
Cdd:TIGR00606 878 TNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD---SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK------- 947
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1426 ddllvdldhqrqsacnlekkqKKFDQLLAEEKTISAKYAEERDRaeaEAREKETKALSLARALEEAMEQKaelERLNKQF 1505
Cdd:TIGR00606 948 ---------------------EKVKNIHGYMKDIENKIQDGKDD---YLKQKETELNTVNAQLEECEKHQ---EKINEDM 1000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1506 RTEMEDLMSSK--DDVGKSVHELEKSKRALEQQVEEMKTQLEEL-EDELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQ 1582
Cdd:TIGR00606 1001 RLMRQDIDTQKiqERWLQDNLTLRKRENELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRN-HVLALGRQKG 1079
|
810 820 830
....*....|....*....|....*....|....*.
gi 972988096 1583 SEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKL 1618
Cdd:TIGR00606 1080 YEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTEL 1115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1045-1301 |
6.64e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1045 QRQELEKTRRKLEgdstDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEEAAQKNmalKKIRELESQISELQEDLe 1124
Cdd:COG4942 18 QADAAAEAEAELE----QLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALA---RRIRALEQELAALEAEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1125 serasrNKAEKQKRDLGEELEALKTELEDTLDstAAQQelRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEEL 1204
Cdd:COG4942 86 ------AELEKEIAELRAELEAQKEELAELLR--ALYR--LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1205 AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVE 1284
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*..
gi 972988096 1285 LDNVTGLLSQSDSKSSK 1301
Cdd:COG4942 236 AAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1329-1924 |
7.49e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.82 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1329 SLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKV 1408
Cdd:TIGR04523 44 TIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1409 AAYDKLEKTK--------------TRLQQELDDLLVDLDHQRQSACNLEKKQKKF-DQLLAEEKTIsakyaeerDRAEAE 1473
Cdd:TIGR04523 124 VELNKLEKQKkenkknidkflteiKKKEKELEKLNNKYNDLKKQKEELENELNLLeKEKLNIQKNI--------DKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1474 AREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQ---QVEEMKTQLEELEDE 1550
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQlkdEQNKIKKQLSEKQKE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1551 LQATEDAKLRLEVNLQAMKAQFErDLqgRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHID 1630
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEIS-DL--NNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1631 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELaaaerakRQAQQERDELA 1710
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI-------KKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1711 DEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1790
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1791 KELKVKLQEMEGTVKSkYKASITALEAKIAQLEEQLDNetKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADK 1870
Cdd:TIGR04523 506 KELEEKVKDLTKKISS-LKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1871 ASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1924
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1481-1724 |
9.23e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 9.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1481 ALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLR 1560
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1561 LEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAvAARKKLEMDLKDLEAHIDSANKNRDEAI 1640
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1641 KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1720
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
....
gi 972988096 1721 ALAL 1724
Cdd:COG4942 254 KLPW 257
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
873-1471 |
1.30e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.33 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 873 EMETLQSQLMA-EKL-QLQEQLQAETELCAEAEELRARLTA-----KKQELEEICHDLEARVEEEEERCQHLQAEKKKMQ 945
Cdd:COG4913 243 ALEDAREQIELlEPIrELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 946 QNIQELEEQLEEEESAR-QKLQLEKVTTEAKLKKLEEEQIILEDQ----NCKLAKEKKLLEDRIAEFTTNLTEEEEKSKS 1020
Cdd:COG4913 323 EELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1021 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAE-LQAQIAELK-----MQLAKKEEELQAALAR 1094
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPfvgelIEVRPEEERWRGAIER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1095 ----------VEEEAAQKnmALKKIRELesqisELQEDLESERASRNKAEKQKRDLGEelEALKTELEdtLDSTAAQQEL 1164
Cdd:COG4913 483 vlggfaltllVPPEHYAA--ALRWVNRL-----HLRGRLVYERVRTGLPDPERPRLDP--DSLAGKLD--FKPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1165 RSKREQEVNILKKTLEEEAKTHEAQIQEMRQ-KHSQAVEELAEQleqtKRVKANL------EKAKQTLENERGELANEVK 1237
Cdd:COG4913 552 EAELGRRFDYVCVDSPEELRRHPRAITRAGQvKGNGTRHEKDDR----RRIRSRYvlgfdnRAKLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1238 VLLQGKGDSEHKRKKVEAQLQELQ--VKFNEGERVRTELADKVTKLQVELDNvtglLSQSDSksskltkDFSALESQLQD 1315
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELER----LDASSD-------DLAALEEQLEE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1316 TQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADmkkKMEDSVGCLETAEEVKRKLQK 1395
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVERELRENLEE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1396 DLEGLSQRHEEkvaAYDKLEKTKTRLQQELDDLLV------------DLDHQRQSACNLEKKQKKFDQLLAEEKT----- 1458
Cdd:COG4913 774 RIDALRARLNR---AEEELERAMRAFNREWPAETAdldadleslpeyLALLDRLEEDGLPEYEERFKELLNENSIefvad 850
|
650
....*....|...
gi 972988096 1459 ISAKYAEERDRAE 1471
Cdd:COG4913 851 LLSKLRRAIREIK 863
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1538-1926 |
1.39e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1538 EEMKTQLEELEDELQATEDAKLRLEVN-LQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELEDERKQRsmavAARK 1616
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNgLESELAELDEEI----ERYEEQREQARETRDEADEVLEEHEERR----EELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1617 KLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE 1696
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1697 RAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHA 1776
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1777 QKNENARQQLERQNKELKVKLQEMEGTVK---------------------------SKYKASITALEAKIAQLEEQLDnE 1829
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVE-E 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1830 TKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET 1909
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
410
....*....|....*..
gi 972988096 1910 ADAMNREVSSLKNKLRR 1926
Cdd:PRK02224 574 VAELNSKLAELKERIES 590
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1442-1927 |
2.76e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1442 LEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskdDVGK 1521
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1522 SVHELEKSKRALEQQVEEMKTQLEELED---ELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREME 1598
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1599 AELEDERKQRSMAVAARKKLEMDLKDLEA-HIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN--- 1674
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENeLEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1675 ----EKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQgNTEL 1750
Cdd:COG4717 286 lallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1751 INDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKA-SITALEAKIAQLEEQLDNE 1829
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1830 TKERQAACKQVRRTEKKLKDVLLQvdderrnaeqykDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATET 1909
Cdd:COG4717 445 EEELEELREELAELEAELEQLEED------------GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
490
....*....|....*....
gi 972988096 1910 -ADAMNREVSSLKNKLRRG 1927
Cdd:COG4717 513 rLPPVLERASEYFSRLTDG 531
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1216-1702 |
4.17e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1216 ANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQS 1295
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1296 DsksskLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEdeknsfreqleeeeeakhNLEKQIATLHAQVADMKKK 1375
Cdd:COG4717 129 P-----LYQELEALEAELAELPERLEELEERLEELRELEEELE------------------ELEAELAELQEELEELLEQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1376 MEdsvgcLETAEEVKRkLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQrqsacNLEKKQKKFDQLLAE 1455
Cdd:COG4717 186 LS-----LATEEELQD-LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-----ALEERLKEARLLLLI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1456 EKTISAKYAEERDRAEAEAREKETKALSLA----------RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE 1525
Cdd:COG4717 255 AAALLALLGLGGSLLSLILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1526 LEKSKRALEQQVEEMKTQLEELEDELQ--ATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKkQLVRQVREMEAELED 1603
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1604 ERK--QRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCM--RELDDTRASREEILAQAKENEKKLK 1679
Cdd:COG4717 414 LLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEWA 493
|
490 500
....*....|....*....|...
gi 972988096 1680 SMEAEMIQLQEELAAAERAKRQA 1702
Cdd:COG4717 494 ALKLALELLEEAREEYREERLPP 516
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1110-1918 |
4.22e-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: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1110 RELESQISELQEDLESERASRNKAEK--QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAkthE 1187
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE---L 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1188 AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER-GELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNE 1266
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1267 GERVRTELADkvtklqveldNVTGLLSQSDSKSSKLTKDFSALESQLQDTQEllqeenrqklslstKLKQVEDEKNSfre 1346
Cdd:COG4913 378 SAEEFAALRA----------EAAALLEALEEELEALEEALAEAEAALRDLRR--------------ELRELEAEIAS--- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1347 qleeeeeakhnLEKQIATLHAQVADMKKKMEDSVGCLET-----AE--EVK---RKLQKDLEGL----------SQRHEE 1406
Cdd:COG4913 431 -----------LERRKSNIPARLLALRDALAEALGLDEAelpfvGEliEVRpeeERWRGAIERVlggfaltllvPPEHYA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1407 KVAAYDKLEKTKTRLQqelddllvdldhqrqsacnlekkqkkfdqllaeektisakYAEERDRAEAEAREKETKAlSLAR 1486
Cdd:COG4913 500 AALRWVNRLHLRGRLV----------------------------------------YERVRTGLPDPERPRLDPD-SLAG 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1487 aleeameqkaELERLNKQFRTEMEDLMSSKDDVGK--SVHELEKSKRALeqqveemktqleeledelqaTEDAKLRLEvn 1564
Cdd:COG4913 539 ----------KLDFKPHPFRAWLEAELGRRFDYVCvdSPEELRRHPRAI--------------------TRAGQVKGN-- 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1565 lqamKAQFERDLQGRDEQ-------SEEKKKQLVRQVREMEAELEDerkqrsmAVAARKKLEMDLKDLEAhidsanknRD 1637
Cdd:COG4913 587 ----GTRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAE-------AEERLEALEAELDALQE--------RR 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1638 EAIKQLRKLQAQMKDcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANss 1717
Cdd:COG4913 648 EALQRLAEYSWDEID-VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-- 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1718 gkgalALEEKRRLEARIAQLEEELEEEQgnTELINDRLKKANLQidqintdlNLERSHAQKNENARQQLERQNKELKVKL 1797
Cdd:COG4913 725 -----AEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGD--------AVERELRENLEERIDALRARLNRAEEEL 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1798 QEMEGTVKSKYKASITALEAKIAQLEE------QLDNE---TKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQykdqa 1868
Cdd:COG4913 790 ERAMRAFNREWPAETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREIKE----- 864
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 972988096 1869 dkastRLKQLKRQLEEAE---------EEAQRANASRRKLQRELEDATETADAMNREVS 1918
Cdd:COG4913 865 -----RIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1273-1916 |
5.92e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.94 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1273 ELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNsfreqlEEEE 1352
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN------GELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1353 EAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQ---ELDDLL 1429
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSkikEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1430 VDLDHQRQSAcnleKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEA--------------MEQK 1495
Cdd:pfam12128 392 IAGIKDKLAK----IREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1496 AELERLNK------QFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQA---TEDAKLRLEVNL- 1565
Cdd:pfam12128 468 NFDERIERareeqeAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagTLLHFLRKEAPDw 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1566 -QAMKAQFERDLQGR-DEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQL 1643
Cdd:pfam12128 548 eQSIGKVISPELLHRtDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1644 RKLQAQMKDCMRELDDTRASreeiLAQAKENEKKLKS-MEAEMIQLQEelaAAERAKRQAQQERDELADEIANSSGKGAL 1722
Cdd:pfam12128 628 VQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1723 ALEEKRR--LEARIAQLEEELeeeqgntELINDRlkkaNLQIDQINTDLNLERSHAQKNENArqqLERQNK-ELKVKlqE 1799
Cdd:pfam12128 701 WLEEQKEqkREARTEKQAYWQ-------VVEGAL----DAQLALLKAAIAARRSGAKAELKA---LETWYKrDLASL--G 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1800 MEGTVKSKYKASITALEAKIAQLE---------EQLDNET--KERQAACKQVRRTEKKLKDvlLQVDDERRNAEqykdqa 1868
Cdd:pfam12128 765 VDPDVIAKLKREIRTLERKIERIAvrrqevlryFDWYQETwlQRRPRLATQLSNIERAISE--LQQQLARLIAD------ 836
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 972988096 1869 dkASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNRE 1916
Cdd:pfam12128 837 --TKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSE 882
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1453-1926 |
8.68e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1453 LAEEKTISAKYAEERDRAEA----------EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKS 1522
Cdd:PRK02224 215 LAELDEEIERYEEQREQAREtrdeadevleEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1523 VHEL-------EKSKRALEQQVEEMKTQLEELEDELqatEDAKLRLevnlQAMKAQFERdLQGRDEQSEEKKKQLVRQVR 1595
Cdd:PRK02224 295 RDDLlaeagldDADAEAVEARREELEDRDEELRDRL---EECRVAA----QAHNEEAES-LREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1596 EMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENE 1675
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1676 KKLKSMEA-EMIQLQEELAAAERAKrQAQQERDELADEIANssgkgalALEEKRRLEARIAQLEEELEEEQGnTELINDR 1754
Cdd:PRK02224 447 ALLEAGKCpECGQPVEGSPHVETIE-EDRERVEELEAELED-------LEEEVEEVEERLERAEDLVEAEDR-IERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1755 LKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKAsITALEAKIAQLEEQLDNETK--- 1831
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE-VAELNSKLAELKERIESLERirt 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1832 ---ERQAACKQVRRTEKKLKDvLLQVDDERRnaeqykDQADKASTRLKQLKRQ-----LEEAEEEAQRANASRRKLQREL 1903
Cdd:PRK02224 597 llaAIADAEDEIERLREKREA-LAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKL 669
|
490 500
....*....|....*....|...
gi 972988096 1904 EDATETADAMNREVSSLKNKLRR 1926
Cdd:PRK02224 670 DELREERDDLQAEIGAVENELEE 692
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1446-1849 |
9.18e-11 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 66.46 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1446 QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE 1525
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1526 LEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKaqferdlqgrdeqseEKKKQLVRQVREMEAELEDER 1605
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1606 KQRSMAVAARKKLEMDLKDLEAHIDsankNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1685
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1686 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGA---LALEEKRrleariAQLEEELEEEQGNTELINDRLKKANLQI 1762
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAdasLALREGR------ARWAQERETLQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1763 DQINTDLNLERSHAQK-----------NENARQQLERQNKELKVKLQEMEGTvKSKYKASITALEAKIAQLEEQLDNET- 1830
Cdd:pfam07888 328 QRLEERLQEERMEREKlevelgrekdcNRVQLSESRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVAd 406
|
410 420
....*....|....*....|
gi 972988096 1831 -KERQAACKQVRRTEKKLKD 1849
Cdd:pfam07888 407 aKWSEAALTSTERPDSPLSD 426
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
962-1514 |
9.54e-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: 66.97 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 962 RQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKL------------LEDRIAEF---TTNLTEE-EEKSKSLAKLK 1025
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknksLESQISELkkqNNQLKDNiEKKQQEINEKT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1026 ---NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlaKKEEELQAALARVEEEAAQK 1102
Cdd:TIGR04523 246 teiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1103 NMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTL--- 1179
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqnq 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1180 EEEAKTHEAQIQEMRQKH---SQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1256
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1257 LQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKlslstKLKQ 1336
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL-----KKEN 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1337 VEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEK 1416
Cdd:TIGR04523 559 LEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1417 TKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKA 1496
Cdd:TIGR04523 639 KKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKEIEK 718
|
570
....*....|....*...
gi 972988096 1497 ELERLnKQFRTEMEDLMS 1514
Cdd:TIGR04523 719 ELKKL-DEFSKELENIIK 735
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1019-1854 |
1.41e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1019 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDL--SDQIAELQAQIAELKMQLAKKEEELQAALARVE 1096
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqQEKIERYQADLEELEERLEEQNEVVEEADEQQE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1097 EEAAQKNMALKKIRELESQISELQE--DLESERASRNKAEKQkrdLGEELEALKTELEDTLDSTAA-QQELRSKREQEVN 1173
Cdd:PRK04863 380 ENEARAEAAEEEVDELKSQLADYQQalDVQQTRAIQYQQAVQ---ALERAKQLCGLPDLTADNAEDwLEEFQAKEQEATE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1174 ILkktLEEEAKTHEAqiQEMRQKHSQAVEELAEQLEQTKRVKANlEKAKQTLenerGELANEVKVLLQGKGdsehkrkkV 1253
Cdd:PRK04863 457 EL---LSLEQKLSVA--QAAHSQFEQAYQLVRKIAGEVSRSEAW-DVARELL----RRLREQRHLAEQLQQ--------L 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1254 EAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdsksskltkDFSALESQLQDTQELLQEENRQKLSLSTK 1333
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDED---------------ELEQLQEELEARLESLSESVSEARERRMA 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1334 LKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKvaayDK 1413
Cdd:PRK04863 584 LRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEE----------FEDSQDVTEYMQQLLERERELTVER----DE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1414 LEKTKTRLQQElddllVDLDHQRQSAcNLEKKQKKFDQ----LLAEektISAKYAEErDRAEAEAREKETKALSLARALE 1489
Cdd:PRK04863 650 LAARKQALDEE-----IERLSQPGGS-EDPRLNALAERfggvLLSE---IYDDVSLE-DAPYFSALYGPARHAIVVPDLS 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1490 EAMEQKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEKS----------------------KRALEQQVEEMK 1541
Cdd:PRK04863 720 DAAEQLAGLEDC-------PEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLR 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1542 TQLEELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED----ERKQRSMA 1611
Cdd:PRK04863 793 AEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqEQQQRSQL 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1612 VAARKKLEMdlkdLEAHIDSANKNRDEA-IKQLRKLQAQMKDCmreLDDTR--ASREEILAQAKENEKKLKSMEAEMIQL 1688
Cdd:PRK04863 868 EQAKEGLSA----LNRLLPRLNLLADETlADRVEEIREQLDEA---EEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQL 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1689 QEELAAAERAKRQAQQERDELADEIANssgKGALALEEKRRLEAriaqleeeleEEQGNTELINDRLKKANLQIDQINTD 1768
Cdd:PRK04863 941 KQDYQQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMLA----------KNSDLNEKLRQRLEQAEQERTRAREQ 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1769 LNLERS-HAQKNE------NARQQLERQNKELKVKLQEM-----EG------TVKSKYKASITALEAKIAQLEEQLDNET 1830
Cdd:PRK04863 1008 LRQAQAqLAQYNQvlaslkSSYDAKRQMLQELKQELQDLgvpadSGaeerarARRDELHARLSANRSRRNQLEKQLTFCE 1087
|
890 900
....*....|....*....|....
gi 972988096 1831 KERQAACKQVRRTEKKLKDVLLQV 1854
Cdd:PRK04863 1088 AEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1333-1929 |
1.71e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1333 KLKQVEDEKNSFREQLEEEEEAKHNLEKQIATlhaqvadMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEkvaayd 1412
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKE-------KEKELEEVLREINEISSELPELREELEKLEKEVKE------ 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1413 kLEKTKTRLqqelddllvdldhqrqsacnlEKKQKKFDQLLAEEKTISAKYAEERDRAEaEAREKETKALSLARALEEAM 1492
Cdd:PRK03918 233 -LEELKEEI---------------------EELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1493 EQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQV---EEMKTQLEELEDELQATEDAKLRLEVNLQAmk 1569
Cdd:PRK03918 290 EKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL-- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1570 aqFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsmavaARKKLEMDLKDLEAHI---DSANKNRDEAIKQLRKL 1646
Cdd:PRK03918 364 --YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-------AKEEIEEEISKITARIgelKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1647 QAQMKDCMRELDDTRasREEILAqakENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERD---------ELADEIANSS 1717
Cdd:PRK03918 435 KGKCPVCGRELTEEH--RKELLE---EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliklkELAEQLKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1718 GK-GALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN----KE 1792
Cdd:PRK03918 510 EKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEE 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1793 LKVKLQEMEGTVK-----SKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDE---------- 1857
Cdd:PRK03918 590 LEERLKELEPFYNeylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeyeelreeyl 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1858 ---------RRNAEQYKDQADKASTRLKQLKRQLeeaeeeaqranASRRKLQRELED---ATETADAMNREVSSLKNKLR 1925
Cdd:PRK03918 670 elsrelaglRAELEELEKRREEIKKTLEKLKEEL-----------EEREKAKKELEKlekALERVEELREKVKKYKALLK 738
|
....
gi 972988096 1926 RGDL 1929
Cdd:PRK03918 739 ERAL 742
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1039-1908 |
2.19e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.13 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1039 LRREEKQRQELEKTRRKLEGDSTDLSdqiaELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKN---MALKKIREL 1112
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLV----EMARELAELNEAESDLEQDYQAAsdhLNLVQTALRQQEkieRYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1113 ESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE---------EEA 1183
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglpdltaDNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1184 KTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL-----ENERGELANEVKVLLQgkgdsEHKRKKVEA-QL 1257
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVrkiagEVSRSEAWDVARELLR-----RLREQRHLAeQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1258 QELQVKFNEGERvRTELADKVTKLQVELDNVTGLLSQSDSksskltkDFSALESQLQDTQELLQEENRQKLSLSTKLKQV 1337
Cdd:PRK04863 516 QQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1338 EDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKvaayDKLEKT 1417
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLAAQDALARLREQSGEE----------FEDSQDVTEYMQQLLERERELTVER----DELAAR 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1418 KTRLQQELDDLlvdldHQRQSAcNLEKKQKKFDQ----LLAEektISAKYAEErDRAEAEAREKETKALSLARALEEAME 1493
Cdd:PRK04863 654 KQALDEEIERL-----SQPGGS-EDPRLNALAERfggvLLSE---IYDDVSLE-DAPYFSALYGPARHAIVVPDLSDAAE 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1494 QKAELERLnkqfrteMEDLM------SSKDDVGKSVHELEKS----------------------KRALEQQVEEMKTQLE 1545
Cdd:PRK04863 724 QLAGLEDC-------PEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAERE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1546 ELEDELqatedAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED----ERKQRSMAVAAR 1615
Cdd:PRK04863 797 ELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqEQQQRSQLEQAK 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1616 KKLEMdlkdLEAHIDSANKNRDEA-IKQLRKLQAQMKDCmreLDDTR--ASREEILAQAKENEKKLKSMEAEMIQLQEEL 1692
Cdd:PRK04863 872 EGLSA----LNRLLPRLNLLADETlADRVEEIREQLDEA---EEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDY 944
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1693 AAAERAKRQAQQERDELADEIANssgKGALALEEKRRLEAriaqleeeleEEQGNTELINDRLKKANLQIDQintdlnle 1772
Cdd:PRK04863 945 QQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMLA----------KNSDLNEKLRQRLEQAEQERTR-------- 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1773 rshaqknenARQQLERQNKELKVKLQemegtVKSKYKASITALEAKIAQLEEQLDNET-KERQAACKQVRRTEKKLKDVL 1851
Cdd:PRK04863 1004 ---------AREQLRQAQAQLAQYNQ-----VLASLKSSYDAKRQMLQELKQELQDLGvPADSGAEERARARRDELHARL 1069
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1852 LQvDDERRNaeqykdqadkastrlkQLKRQLEEAEEEAQRANASRRKLQRELEDATE 1908
Cdd:PRK04863 1070 SA-NRSRRN----------------QLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1689-1934 |
3.52e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1689 QEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTD 1768
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1769 LNLERSHAQKNENARQQLERQNK-ELKVKLQEMEGTVKSK--YKASITALEAKIAQLEEQLDNETKERQaackQVRRTEK 1845
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRA----ELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1846 KLKDVLLQVDDERRNAEQYKDQADKAstrLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKLR 1925
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
....*....
gi 972988096 1926 RGDLPFVVP 1934
Cdd:COG4942 252 KGKLPWPVS 260
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1251-1923 |
3.53e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1251 KKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDtqellqeENRQKLSL 1330
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN-------DKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1331 STKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAA 1410
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1411 YDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLaralEE 1490
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL----EQ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1491 AMEQKAELERLNKQFRTEMEDLMSSKD-DVGKSVHElekskraleqQVEEMKTQLEELEDELQATEDAKLRLEVNLqamk 1569
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEqDWNKELKS----------ELKNQEKKLEEIQNQISQNNKIISQLNEQI---- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1570 AQFERDLQGRDEQSEEKKKQLvrqvREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSA---NKNRDEAIKQL--- 1643
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQREL----EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklNQQKDEQIKKLqqe 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1644 -RKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGAL 1722
Cdd:TIGR04523 421 kELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1723 ALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNlERSHAQKNENARQQLERQNKELkvklqemeg 1802
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN-KDDFELKKENLEKEIDEKNKEI--------- 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1803 tvkSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKdvllqvdderrnaeqykdqadkastrlkQLKRQL 1882
Cdd:TIGR04523 571 ---EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS----------------------------SLEKEL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 972988096 1883 EEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1923
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
857-1373 |
5.31e-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: 64.74 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 857 LVKVREKqlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTakkQELEEICHDLEARVEEEEERCQH 936
Cdd:pfam05483 246 LIQITEK----ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEED 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 937 LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeqiILEDQNCKLAKEkkllEDRIAEFTTNLTEEEE 1016
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKN----EDQLKIITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1017 KSKSLAKLKNKHEAMITDLEERLRREEK---QRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL----------AK 1083
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseehyLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1084 KEEELQAALARVE----EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALK---TELEDTLD 1156
Cdd:pfam05483 472 EVEDLKTELEKEKlkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekeMNLRDELE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1157 STaaQQELRSKREQEVNILKKTlEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEV 1236
Cdd:pfam05483 552 SV--REEFIQKGDEVKCKLDKS-EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1237 KVLlqgkGDSEHKRKKVEAQLQELQVKFNE---------------GERVRTEL------ADKVTKLQVELD-----NVTG 1290
Cdd:pfam05483 629 KQL----NAYEIKVNKLELELASAKQKFEEiidnyqkeiedkkisEEKLLEEVekakaiADEAVKLQKEIDkrcqhKIAE 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1291 LLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVA 1370
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
...
gi 972988096 1371 DMK 1373
Cdd:pfam05483 785 DKK 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1217-1871 |
8.20e-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: 63.89 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1217 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSD 1296
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1297 SKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK- 1375
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1376 --MEDSVGCLETAEEVKRKLQKDLEGL----SQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKF 1449
Cdd:TIGR04523 197 lkLELLLSNLKKKIQKNKSLESQISELkkqnNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1450 DQllAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVG---KSVHEL 1526
Cdd:TIGR04523 277 EQ--NNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkKELTNS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1527 EKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFE------RDLQGRDEQSEEKKKQLVRQVREMEAE 1600
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQnqeklnQQKDEQIKKLQQEKELLEKEIERLKET 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1601 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKS 1680
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1681 MEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalaleekrrleariaqleeeleeeqgntelINDRLKKANL 1760
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNK-----------------------------------DDFELKKENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1761 QIDQINTDLNLERSHAQKNEnarqqLERQNKELKVKLQEmegtvkskYKASITALEAKIAQLEEQLDNETKERQAACKQV 1840
Cdd:TIGR04523 560 EKEIDEKNKEIEELKQTQKS-----LKKKQEEKQELIDQ--------KEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
650 660 670
....*....|....*....|....*....|.
gi 972988096 1841 RRTEKKLKDVLLQVDDERRNAEQYKDQADKA 1871
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
27-72 |
8.63e-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: 8.63e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 972988096 27 AAKKLVWVPSDKSGFEPASLKEEVGEEAIVELvENGKKVKVNKDDI 72
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
862-1457 |
1.31e-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: 63.59 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 862 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEK 941
Cdd:pfam05483 201 ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 942 KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKlledriaeftTNLTEEEEKSKSL 1021
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE----------AQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1022 AKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSDQIAELQaQIAELKMQLAKKEEELQAALARVEEEAAQ 1101
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSELE-EMTKFKNNKEVELEELKKILAEDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1102 KNMALKKIRELESQISELQEDLESErasrnkaEKQKRDLGEELEALKTELEDTLDS-----TAAQQELRSKREQEVNILK 1176
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELIFLLQAR-------EKEIHDLEIQLTAIKTSEEHYLKEvedlkTELEKEKLKNIELTAHCDK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1177 KTLEEEAKTHEAQIQEMRQKHSQavEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1256
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQ--EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1257 LQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQ------DTQELLQEENRQKLS- 1329
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayeikvNKLELELASAKQKFEe 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1330 -LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKL----QKDLEGLSQRH 1404
Cdd:pfam05483 655 iIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIieerDSELGLYKNKE 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 972988096 1405 EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 1457
Cdd:pfam05483 735 QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
935-1263 |
1.51e-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: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 935 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKleEEQIILEDQNCKLAKEKKLleDRIaefttnltEE 1014
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMEREREL--ERI--------RQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1015 EEKSKSLAKLKNKHEAM----ITDLE----ERLRREEKQRQELEKTRRKlegdSTDLSDQIAELQAQIAELKMQLAKKEE 1086
Cdd:pfam17380 356 EERKRELERIRQEEIAMeisrMRELErlqmERQQKNERVRQELEAARKV----KILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1087 ELQAALARVEEEAAQKnmaLKKIRELE----SQISELQEDLESERASRNKAEKQKRD--LGEEL--EALKTELEDTLDST 1158
Cdd:pfam17380 432 ARQREVRRLEEERARE---MERVRLEEqerqQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQrrKILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1159 AAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEkakqTLENERgELANEVKv 1238
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE----AMERER-EMMRQIV- 582
|
330 340
....*....|....*....|....*
gi 972988096 1239 llqgkgDSEHKRKKVEAQLQELQVK 1263
Cdd:pfam17380 583 ------ESEKARAEYEATTPITTIK 601
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
862-1229 |
2.62e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 862 EKQLAAENRLTEMETLQSQLMAEKLQ---LQEQLQAETELCAEAEELRARLTAKKQELEEICHDL----EARVEEEEERC 934
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 935 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTtEAKLKKLEEEQIILEDQN--CKLAKEKKLLEDRIAEFTTNLT 1012
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLLLLIAAalLALLGLGGSLLSLILTIAGVLF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1013 EEEE----KSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST-------DLSDQIAELQAQIAEL---- 1077
Cdd:COG4717 281 LVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlspeellELLDRIEELQELLREAeele 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1078 -KMQLAKKEEELQAALARV----EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDlgEELEALKTELE 1152
Cdd:COG4717 361 eELQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1153 DTLDSTAAQQELRSKREQEVNILKKTLEEEAktheaQIQEMRQKHSQAVEELAEQLEQTKRVK---ANLEKAKQTLENER 1229
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 ... |
1063-1701 |
2.64e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.53 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1063 LSDQIAELQAQIAELKMQLAKKEEELQAALARVE---EEAAQKNMALKKirELESQISELQEdleserasrnkaekQKRD 1139
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKtfwSPELKKERALRK--EEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1140 LGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAvEELAEQLEQTKRVKANLE 1219
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEH-ERQAKELFLLRKTLEEME 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1220 ----KAKQTLeNERGELANEVKVLLQGKG--------DSEHKRKKVEAQLQ------ELQVKFNEGERVRTELADKvTKL 1281
Cdd:pfam10174 144 lrieTQKQTL-GARDESIKKLLEMLQSKGlpkksgeeDWERTRRIAEAEMQlghlevLLDQKEKENIHLREELHRR-NQL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1282 QVELDNVTGL---LSQSDSKSSKLTKDFSALESQLQ--DTQELLQEENRQKlslstKLKQVEDEKNSFR------EQLEE 1350
Cdd:pfam10174 222 QPDPAKTKALqtvIEMKDTKISSLERNIRDLEDEVQmlKTNGLLHTEDREE-----EIKQMEVYKSHSKfmknkiDQLKQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1351 EEEAKHN----LEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELD 1426
Cdd:pfam10174 297 ELSKKESellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1427 DLLVDLDHQRQSACNLEKK----QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLArALEEAMEQKAE-LERL 1501
Cdd:pfam10174 377 TLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERiIERL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1502 NKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ------ATEDAKLR-LEVNLQAMKAQFER 1574
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASslassgLKKDSKLKsLEIAVEQKKEECSK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1575 dLQGRD------EQSEEKKKQLVRQVREMEAELEDERKQRSMAVA-------ARKKLEMDLKDLEAHIDSANKNRDEAIK 1641
Cdd:pfam10174 536 -LENQLkkahnaEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAeverllgILREVENEKNDKDKKIAELESLTLRQMK 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1642 QLRKLQAQMKDCMRELddtRASREEILAQAKENEKKLKSMEAEmIQLQEELAAAERAKRQ 1701
Cdd:pfam10174 615 EQNKKVANIKHGQQEM---KKKGAQLLEEARRREDNLADNSQQ-LQLEELMGALEKTRQE 670
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1021-1634 |
2.65e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 62.45 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1021 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAA 1100
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1101 QKNMALKKIRELESQISELQEDLES--ERASRNKAEKQKRDLgeELEALKTELEDTLDstaaQQELRSKREQEVNILKKT 1178
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISClkNELSELRRQIQRAEL--ELQSTNSELEELQE----RLDLLKAKASEAEQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1179 LE---EEAKTHEAQIQEMRQKHSQAVEELAEqleqTKRVKANLEKAKqTLENERGELANEVKVLLQGKGDSEhkrkKVEA 1255
Cdd:pfam05557 158 LEkqqSSLAEAEQRIKELEFEIQSQEQDSEI----VKNSKSELARIP-ELEKELERLREHNKHLNENIENKL----LLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1256 QLQELQVKFNEGERVRTELADkvtkLQVELdnvtgllsqsdsksSKLTKDFSALESQLQDTQELLqeenRQKLSLSTKLK 1335
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAAT----LELEK--------------EKLEQELQSWVKLAQDTGLNL----RSPEDLSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1336 QVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHE---EKVAAYD 1412
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyrAILESYD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1413 K-LEKTKTRLQqelddllvdldhqrqsacnLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALeEA 1491
Cdd:pfam05557 367 KeLTMSNYSPQ-------------------LLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL-QA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1492 MEQKAELErlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELedELQATEDAK----LRLEVNLQA 1567
Cdd:pfam05557 427 LRQQESLA--------DPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR--CLQGDYDPKktkvLHLSMNPAA 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1568 MKAQFERDLQgrdEQSEEKKKQLVRQVREMEAELEDerkQRSMAVAARKKLEMDLKDLEAHIDSANK 1634
Cdd:pfam05557 497 EAYQQRKNQL---EKLQAEIERLKRLLKKLEDDLEQ---VLRLPETTSTMNFKEVLDLRKELESAEL 557
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1066-1226 |
2.89e-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: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1066 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeELE 1145
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1146 ALKTELEdtldSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL 1225
Cdd:COG1579 93 ALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
.
gi 972988096 1226 E 1226
Cdd:COG1579 169 A 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
898-1128 |
4.36e-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: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 898 LCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLK 977
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQ----LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 978 KLEEEQIILEDQnckLAKEKKLLEDRIAEFTTNLTEEE-------EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELE 1050
Cdd:COG4942 87 ELEKEIAELRAE---LEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1051 KTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERA 1128
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1534-1736 |
5.50e-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: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1534 EQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVA 1613
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1614 ARKKLEMDLKDLEAHIDSanKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1693
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 972988096 1694 AAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1736
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1056-1284 |
7.45e-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: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1056 LEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR--VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKA 1133
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1134 EKQkrdLGEELEALKTELEDTLDSTAAQQelRSKREQEVNILKKTLEEE---AKTHEAQIQEMRQKHSQAVEELAEQLEQ 1210
Cdd:COG3206 246 RAQ---LGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1211 TKRVkanLEKAKQTLENERGELANEVKVLlqgkgdsehkrKKVEAQLQELQVKFNEGERVRTELADKVTKLQVE 1284
Cdd:COG3206 321 ELEA---LQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1631-1874 |
7.65e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1631 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1710
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1711 DEIANSSGKGALALeekRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQN 1790
Cdd:COG4942 97 AELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1791 KELKVKLQEMEgtvksKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADK 1870
Cdd:COG4942 174 AELEALLAELE-----EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 972988096 1871 ASTR 1874
Cdd:COG4942 249 AALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1132-1849 |
8.75e-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: 60.89 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1132 KAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQE---MRQKHSQAVEELAEQL 1208
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnaTRHLCNLLKETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1209 EQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGER-VRTELADKVTKlqveldn 1287
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEeYKKEINDKEKQ------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1288 VTGLLSQSDSKSSKLtKDFSalesqlqdtqeLLQEENRQKLSlstklkQVEDEKNSFREQLEEEEEAKHNLEKQIAtlha 1367
Cdd:pfam05483 242 VSLLLIQITEKENKM-KDLT-----------FLLEESRDKAN------QLEEKTKLQDENLKELIEKKDHLTKELE---- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1368 qvaDMKKKMEDSVGCLETAEEvkrKLQKDLEGLSQRHEEKVAAYDKLEKTKTrlqqeldDLLVDLDHQRQSACNLEK--- 1444
Cdd:pfam05483 300 ---DIKMSLQRSMSTQKALEE---DLQIATKTICQLTEEKEAQMEELNKAKA-------AHSFVVTEFEATTCSLEEllr 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1445 -KQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARaLEEAMEQKAELERLNKQFRTEMEDLMSSKDDV---- 1519
Cdd:pfam05483 367 tEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE-LKKILAEDEKLLDEKKQFEKIAEELKGKEQELifll 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1520 ---GKSVHELE-------KSKRALEQQVEEMKTQLEELE---DELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEK 1586
Cdd:pfam05483 446 qarEKEIHDLEiqltaikTSEEHYLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1587 KKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREE 1666
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1667 ILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEEleeeqg 1746
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEK------ 679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1747 nTELINDRLKKANLQID-----QINTDLNLERSHAQKNENARQQLERQNKELKVKLQEmEGTVKSKYKASITALEAKIAQ 1821
Cdd:pfam05483 680 -AKAIADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE-QSSAKAALEIELSNIKAELLS 757
|
730 740
....*....|....*....|....*...
gi 972988096 1822 LEEQLDNETKERQAACKQVRRTEKKLKD 1849
Cdd:pfam05483 758 LKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1021-1179 |
1.01e-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: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1021 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL--AKKEEELQAALARVEEE 1098
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1099 AAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtldstAAQQELRSKREQEVNILKKT 1178
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE------AELEELEAEREELAAKIPPE 175
|
.
gi 972988096 1179 L 1179
Cdd:COG1579 176 L 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1473-1920 |
1.05e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1473 EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ 1552
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1553 ATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKdLEAHID 1630
Cdd:PRK03918 225 KLEKEVKELEelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1631 SANKNRDEAIKQLRKLQAQMKDCMRELDDtrasREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK----------- 1699
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKakkeelerlkk 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1700 RQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTElindRLKKANLQIDQINTDLNLERSHAQKN 1779
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAKGKCPVCGRELTEEHRKELLE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1780 EnARQQLERQNKELKvKLQEMEgtvkSKYKASITALEAKIAQLEEQLdnetKERQAAcKQVRRTEKKLKDVLLQ-VDDER 1858
Cdd:PRK03918 456 E-YTAELKRIEKELK-EIEEKE----RKLRKELRELEKVLKKESELI----KLKELA-EQLKELEEKLKKYNLEeLEKKA 524
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972988096 1859 RNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRanasRRKLQRELEDATETADAMNREVSSL 1920
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEEL 582
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1086-1553 |
1.10e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1086 EELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKR--DLGEELEALKTELEDT---LDSTAA 1160
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1161 QQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLl 1240
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1241 qgkgDSEHKRKKVEAQLQELQVKFNeGERVRTELADKVTKLQVELDNVTGLLSQSDS----KSSKLTKDFSALESQLQDT 1316
Cdd:COG4717 233 ----ENELEAAALEERLKEARLLLL-IAAALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1317 QELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAkhnlEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKD 1396
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDR----IEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1397 LEGLSQRHEEKvAAYDKLEKTKTRLQQelddllvdldhqrqsacnlekkqkkfdQLLAEEKTISAKYA-EERDRAEAEAR 1475
Cdd:COG4717 384 EEELRAALEQA-EEYQELKEELEELEE---------------------------QLEELLGELEELLEaLDEEELEEELE 435
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1476 EKETKALSLARALEEAMEQKAELErlnkqfrTEMEDLMSSkddvgksvHELEKskraLEQQVEEMKTQLEELEDELQA 1553
Cdd:COG4717 436 ELEEELEELEEELEELREELAELE-------AELEQLEED--------GELAE----LLQELEELKAELRELAEEWAA 494
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1065-1256 |
1.13e-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: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1065 DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLEserASRNKAEKQKRDLGEEL 1144
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1145 EALK---------------TELEDTLDSTAAQQELRSKREQEVNILKKtLEEEAKTHEAQIQEMRQKHSQAVEELAEQLE 1209
Cdd:COG3883 93 RALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 972988096 1210 QTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1256
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1395-1792 |
1.78e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1395 KDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDqLLAEEKTISAKYAEERDRAEA-E 1473
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEElE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1474 AREKETKAL--SLARALEEAMEQKAELERLNKQF----RTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 1547
Cdd:COG4717 153 ERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1548 EDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQ-------------LVRQVREMEAELEDERKQRSMAVAA 1614
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1615 RKKLE-MDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASReEILAQAKENEKKLKSMEAEMIQLQEELA 1693
Cdd:COG4717 313 LEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1694 AAERAKRQAQQERDELADEIANSSG--KGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNL 1771
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|.
gi 972988096 1772 ERSHAQKnENARQQLERQNKE 1792
Cdd:COG4717 472 AELLQEL-EELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1326-1560 |
1.96e-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: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1326 QKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHE 1405
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1406 EKVAAYDKLEKTktrLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLA 1485
Cdd:COG4942 101 AQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1486 RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLR 1560
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
887-1103 |
2.69e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 887 QLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEES--ARQK 964
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAelEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 965 LQLEKVTTEA-KLKKLEEEQIILEDQNCK--------LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDL 1035
Cdd:COG4942 104 EELAELLRALyRLGRQPPLALLLSPEDFLdavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1036 EERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKN 1103
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1446-1908 |
2.71e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1446 QKKFDQLLAEEKTISAkyaEERDRAEAEAREKETKALSLARALEEAMEQKAELERlnKQFRTEMEDLMSSKDDVGKSVHE 1525
Cdd:TIGR00606 172 KQKFDEIFSATRYIKA---LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR--DQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1526 LEKSKRALeQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDER 1605
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1606 KQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLK--SMEA 1683
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVieRQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1684 EMIQLQEELAAAERAKRQAQQERDELADEIansSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKanlqiD 1763
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEK---KGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL-----D 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1764 QINTDLNLERSHAQKNENARQQLERQnkelkVKLQEMEGTVKSKYKASITALEAKIAQLE--EQLDNETKERQAACKQVR 1841
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKKEV-----KSLQNEKADLDRKLRKLDQEMEQLNHHTTtrTQMEMLTKDKMDKDEQIR 552
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1842 RTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATE 1908
Cdd:TIGR00606 553 KIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1029-1233 |
2.72e-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: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1029 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1108
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1109 IRELESQISELQEDLESE-------RASR-NKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE 1180
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldRLSAlSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 972988096 1181 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA 1233
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
960-1226 |
3.02e-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: 58.16 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 960 SARQKLQLEKVTTEAKLK-------KLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMI 1032
Cdd:pfam19220 41 RELPQAKSRLLELEALLAqeraaygKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1033 TDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIREL 1112
Cdd:pfam19220 121 EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1113 ESQ-------ISELQEDLESERASRNKAEKQkrdLGEELEALKTELE------DTLDSTAA--QQELRSKREQEVNILKK 1177
Cdd:pfam19220 201 ETQldatrarLRALEGQLAAEQAERERAEAQ---LEEAVEAHRAERAslrmklEALTARAAatEQLLAEARNQLRDRDEA 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 972988096 1178 TLEEEAKTHEAQIqEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQTLE 1226
Cdd:pfam19220 278 IRAAERRLKEASI-ERDTLERR-LAGLEADLERRTQQFQEMQRARAELE 324
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
861-1528 |
3.20e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 58.68 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 861 REKQLAAENRlTEMETLQSQLMA---EKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 937
Cdd:pfam10174 43 KERALRKEEA-ARISVLKEQYRVtqeENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 938 QAEKKK--------------MQQNIQELEEQLEEEESARQKLqLEKVTTEAKLKKLEEE------------------QII 985
Cdd:pfam10174 122 QSEHERqakelfllrktleeMELRIETQKQTLGARDESIKKL-LEMLQSKGLPKKSGEEdwertrriaeaemqlghlEVL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 986 LEDQNCKLAKEKKLLEDRiaeftTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSD 1065
Cdd:pfam10174 201 LDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1066 QIAELQA----------QIAELKMQLAKKEEELQAALARVEE------------EAAQKNMALKKIRE--LESQISELQE 1121
Cdd:pfam10174 273 EIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETltnqnsdckqhiEVLKESLTAKEQRAaiLQTEVDALRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1122 DLESERASRNKAEKQKRDLGEELEALKTELEDTLDstaaqqeLRSKREQEVNILKKTLE---EEAKTHEAQIQEMRqkhs 1198
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKD-------MLDVKERKINVLQKKIEnlqEQLRDKDKQLAGLK---- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1199 QAVEELAEQLEQTKRVKANLEKA----KQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTEL 1274
Cdd:pfam10174 422 ERVKSLQTDSSNTDTALTTLEEAlsekERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1275 ADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQElLQEENRQKLSLSTKLKQVEDEKNSFREQ------- 1347
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQEVARYKEEsgkaqae 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1348 -------LEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKlqKDLEGLSQRHEEKVAAYDKlektktR 1420
Cdd:pfam10174 581 verllgiLREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK--KGAQLLEEARRREDNLADN------S 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1421 LQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALsLArALEEAMEQKAELER 1500
Cdd:pfam10174 653 QQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL-LA-AISEKDANIALLEL 730
|
730 740
....*....|....*....|....*...
gi 972988096 1501 LNKQFRTEMEDLMSSKDDVGKSVHELEK 1528
Cdd:pfam10174 731 SSSKKKKTQEEVMALKREKDRLVHQLKQ 758
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
859-1125 |
3.58e-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: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 859 KVREKQLAAE-NRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEarvEEEEERCQHL 937
Cdd:pfam17380 364 RIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRL 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 938 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNcklakeKKLLEDRIAEFTTNLTEEEEK 1017
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR------RKILEKELEERKQAMIEEERK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1018 SKSLAKLKNKHEAMITDLEERLRREEKQRQELE-KTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQaalaRVE 1096
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKA----RAE 590
|
250 260 270
....*....|....*....|....*....|
gi 972988096 1097 EEAAQKNMALKKIreLESQISELQ-EDLES 1125
Cdd:pfam17380 591 YEATTPITTIKPI--YRPRISEYQpPDVES 618
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1525-1926 |
3.65e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1525 ELEKSKRALE----QQVEEMKTQLEELEDELQATEDAKLRLevnlqamkaqfeRDLQGRDEQSEEKKKQLVRQVREMEAE 1600
Cdd:COG4717 50 RLEKEADELFkpqgRKPELNLKELKELEEELKEAEEKEEEY------------AELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1601 LE--DERKQRSMAVAARKKLEMDLKDLEAHIDSAnknrDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAK-ENEKK 1677
Cdd:COG4717 118 LEklEKLLQLLPLYQELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1678 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR-----IAQLEEELEEEQGNTELIN 1752
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1753 DRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKY------KASITALEAKIAQLEEQL 1826
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlppdlsPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1827 DNETKERQAACKQVRRTEKK--LKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQR--ANASRRKLQRE 1902
Cdd:COG4717 354 REAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEE 433
|
410 420
....*....|....*....|....
gi 972988096 1903 LEDATETADAMNREVSSLKNKLRR 1926
Cdd:COG4717 434 LEELEEELEELEEELEELREELAE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1188-1410 |
4.76e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1188 AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFneg 1267
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1268 ERVRTELADKVTKLQV--ELDNVTGLLSQSDSksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1345
Cdd:COG4942 100 EAQKEELAELLRALYRlgRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1346 EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAA 1410
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
865-1515 |
7.61e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.93 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 865 LAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICH------DLEARVEEEEERCQHLQ 938
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHlhfgykSDETLIASRQEERQETS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 939 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTT-EAKLKKLEEEQIILEDQNCKLAK-----------EKKLLEDRIAE 1006
Cdd:pfam12128 286 AELNQLLRTLDDQWKEKRDELNGELSAADAAVAKdRSELEALEDQHGAFLDADIETAAadqeqlpswqsELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1007 FTTN---LTEEEEKSKSLAKLKNKHEamITDLEERL--RREEKQRQELEKT----------RRKLEGDSTDLSDQ----- 1066
Cdd:pfam12128 366 LTGKhqdVTAKYNRRRSKIKEQNNRD--IAGIKDKLakIREARDRQLAVAEddlqaleselREQLEAGKLEFNEEeyrlk 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1067 --IAELQAQIA------ELKMQLAKKEEELQAA-----LARVEEEAAQKNMALKKIR----------------ELESQIS 1117
Cdd:pfam12128 444 srLGELKLRLNqatatpELLLQLENFDERIERAreeqeAANAEVERLQSELRQARKRrdqasealrqasrrleERQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1118 ELQEDLESERAS-----RNKAEKQKRDLGEELEA---LKTELEDTLDSTAAQQE-------LRSKREQ--EVNILKKTLE 1180
Cdd:pfam12128 524 ELELQLFPQAGTllhflRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGElnlygvkLDLKRIDvpEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1181 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER---GELANEVKVLLQGKGDS--EHKRKKVEa 1255
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARldlRRLFDEKQSEKDKKNKAlaERKDSANE- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1256 QLQEL--QVKFNEG------ERVRTELADKVTKLQVELDNVTGLLsqsDSKSSKLTKDFSALESQLQDTQELLQEENRQK 1327
Cdd:pfam12128 683 RLNSLeaQLKQLDKkhqawlEEQKEQKREARTEKQAYWQVVEGAL---DAQLALLKAAIAARRSGAKAELKALETWYKRD 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1328 LslstKLKQVEDEKNSfreqleeeeeakhNLEKQIATLHAQVADMKKKMEDS----VGCLETAEEVKRKLQKDLEGLSQR 1403
Cdd:pfam12128 760 L----ASLGVDPDVIA-------------KLKREIRTLERKIERIAVRRQEVlryfDWYQETWLQRRPRLATQLSNIERA 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1404 HEEkvaaydkLEKTKTRLQQELDDLLVDLDHQRQSacnLEKKQKKFDQLLAEEKTISAKYAEER-----DRAEAEAREKE 1478
Cdd:pfam12128 823 ISE-------LQQQLARLIADTKLRRAKLEMERKA---SEKQQVRLSENLRGLRCEMSKLATLKedansEQAQGSIGERL 892
|
730 740 750
....*....|....*....|....*....|....*..
gi 972988096 1479 TKALSLARALEEAMEQkaeLERLNKQFRTEMEDLMSS 1515
Cdd:pfam12128 893 AQLEDLKLKRDYLSES---VKKYVEHFKNVIADHSGS 926
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
876-1706 |
1.04e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 876 TLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLeARVEEEEErcqhlQAEK-KKMQQNIQELEEQ 954
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL-NLVQTALR-----QQEKiERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 955 LEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQnckLAKEKKLLE--DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMI 1032
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQ---LADYQQALDvqQTRAIQYQQAVQALERAKQLCGLPDLTADNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1033 TDLEERLRREEKQR-QELEKTRRKLegdstDLSDQIAELQAQIAELKMQLAKKEEELQA------ALARVEEE---AAQK 1102
Cdd:PRK04863 441 EDWLEEFQAKEQEAtEELLSLEQKL-----SVAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvareLLRRLREQrhlAEQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1103 NMALKKIRELEsQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDStaAQQELRSKREQevnilKKTLEEE 1182
Cdd:PRK04863 516 QQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES--LSESVSEARER-----RMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1183 AKTHEAQIQEMRQKHSQ------AVEELAEQLEQTKRVKANLEKA-KQTLENERGelanevkvLLQGKGDSEHKRKKVEA 1255
Cdd:PRK04863 588 LEQLQARIQRLAARAPAwlaaqdALARLREQSGEEFEDSQDVTEYmQQLLERERE--------LTVERDELAARKQALDE 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1256 QLQEL-QVKFNEGERVRTeLADKVTKLQVEL--DNVT--------GLLSQsdSKSSKLTKDFSALESQLQDTQELLQEen 1324
Cdd:PRK04863 660 EIERLsQPGGSEDPRLNA-LAERFGGVLLSEiyDDVSledapyfsALYGP--ARHAIVVPDLSDAAEQLAGLEDCPED-- 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1325 rqklslstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATlhaqvADMKKKMEDSVGCLETAEEVKRklqkdLEGLSQRH 1404
Cdd:PRK04863 735 ---------LYLIEGDPDSFDDSVFSVEELEKAVVVKIAD-----RQWRYSRFPEVPLFGRAAREKR-----IEQLRAER 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1405 EEKVAAYDKLEKTKTRLQQelddllvdlDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSL 1484
Cdd:PRK04863 796 EELAERYATLSFDVQKLQR---------LHQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQ 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1485 ARALEEAMEQKAEL---------ERLNKQFRTEMEDLMSSKDDV------GKSVHELEKSKRAL---EQQVEEMKTQLEE 1546
Cdd:PRK04863 867 LEQAKEGLSALNRLlprlnlladETLADRVEEIREQLDEAEEAKrfvqqhGNALAQLEPIVSVLqsdPEQFEQLKQDYQQ 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1547 LEDELQATeDAKLRLEVNLQAMKAQFE-RDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDL 1625
Cdd:PRK04863 947 AQQTQRDA-KQQAFALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASL 1025
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1626 EAHIDSANKNRDEAIKQLRKLQAQMKDCMRELddTRASREEILAQAKEN-------EKKLKSMEAEMIQLQEELAAAERA 1698
Cdd:PRK04863 1026 KSSYDAKRQMLQELKQELQDLGVPADSGAEER--ARARRDELHARLSANrsrrnqlEKQLTFCEAEMDNLTKKLRKLERD 1103
|
....*...
gi 972988096 1699 KRQAQQER 1706
Cdd:PRK04863 1104 YHEMREQV 1111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
890-1347 |
1.40e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 890 EQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEeeesaRQKLQLEK 969
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQLLPLYQE-----LEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 970 VTTEAKLKKLEEEQIILEDqnckLAKEKKLLEDRIAEFTTNLTEEEE-----KSKSLAKLKNKHEAMITDLEERLRREEK 1044
Cdd:COG4717 142 AELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEqlslaTEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1045 QRQELEKTRRKLEGDSTDLsdQIAELQAQIAELKMQL-----------------AKKEEELQAALARVEEEAAQKNMALK 1107
Cdd:COG4717 218 AQEELEELEEELEQLENEL--EAAALEERLKEARLLLliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1108 KIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQevnilkktLEEEAKTHE 1187
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--------LEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1188 AQIQE---MRQKHSQAVEELAEQLEQTKRVKaNLEKAKQTLENERGELANEVKVLLQGKGDSEhkrkkVEAQLQELQVKF 1264
Cdd:COG4717 368 LEQEIaalLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1265 NEGERVRTELADKVTKLQVELDNVTGllsqsdskssklTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF 1344
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEE------------DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
...
gi 972988096 1345 REQ 1347
Cdd:COG4717 510 REE 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1669-1882 |
1.46e-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: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1669 AQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDeladeIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNT 1748
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1749 ELINDRLKKANLQIDQINTDLNLershaqknenarQQLERQNKELKVKLQEMEGTVKSKYKAsITALEAKIAQLEEQLDN 1828
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVI------------QQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQ 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1829 ETKERQAAckqvrrTEKKLKDVLLQVDDERRNAEQYKDQAD---KASTRLKQLKRQL 1882
Cdd:COG3206 310 EAQRILAS------LEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREV 360
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1088-1313 |
1.50e-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: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1088 LQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSK 1167
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1168 REQEVNILKKTLEEEAKTHE-----------------AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERG 1230
Cdd:COG4942 95 LRAELEAQKEELAELLRALYrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1231 ELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSklTKDFSALE 1310
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP--AAGFAALK 252
|
...
gi 972988096 1311 SQL 1313
Cdd:COG4942 253 GKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1581-1807 |
1.58e-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: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1581 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDT 1660
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1661 RASREEILAQAkenEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEE 1740
Cdd:COG4942 103 KEELAELLRAL---YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1741 LEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSK 1807
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
971-1222 |
1.89e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 971 TTEAKLKKLEEEQIILEDQncklAKEKKLLEDRIAEFTTNLTE-EEEKSKSLAKLKNKHEAMITDLEERLRREEK----- 1044
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKE----LEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEERLKELEPfyney 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1045 -----QRQELEKTRRKLEGDSTDLSDQIAELqaqiAELKMQLAKKEEELQAALARVEEEAAQKnmALKKIRELESQISEL 1119
Cdd:PRK03918 605 lelkdAEKELEREEKELKKLEEELDKAFEEL----AETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGL 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1120 QEDLESERASRNKAEKQKRDLGEELEAL---KTELEDTLDSTAAQQELRSKreqeVNILKKTLEEEAktheaqIQEMRQK 1196
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEERekaKKELEKLEKALERVEELREK----VKKYKALLKERA------LSKVGEI 748
|
250 260
....*....|....*....|....*.
gi 972988096 1197 HSQAVEELAEQLEQTKRVKANLEKAK 1222
Cdd:PRK03918 749 ASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1015-1137 |
2.33e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.99 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1015 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakkEEELQAALAR 1094
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 972988096 1095 VEEEAAQknmALKKIRELESQISELQ--EDLESERASRNKAEKQK 1137
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYASVkaHELIEARKRLNKANEKK 623
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
902-1290 |
2.38e-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: 55.67 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 902 AEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQqniqeleEQLEEEESARQKLQLEKVTTEAKLKKLEE 981
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE-------RQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 982 EQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST 1061
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1062 DLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKqkrdLG 1141
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG----LG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1142 EELEALKTELEDTldstaaQQELRSKREQ--EVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEqtkRVKANLE 1219
Cdd:pfam07888 258 EELSSMAAQRDRT------QAELHQARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIE---KLSAELQ 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1220 KAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQE----LQVKFNEGERVRT---ELADKVTKLQVELDNVTG 1290
Cdd:pfam07888 329 RLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQElkasLRVAQKEKEQLQAekqELLEYIRQLEQRLETVAD 406
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1525-1723 |
2.50e-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: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1525 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQ---FERDLQGRDEQSEEKKKQLVRQVREME--- 1598
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREELGERARALYrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1599 ---------------AELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRAS 1663
Cdd:COG3883 100 gsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1664 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1723
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1144-1605 |
2.66e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1144 LEALKTELEDTLDstAAQQELRSKREQEVNILKKTLEEEakthEAQIQEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQ 1223
Cdd:COG4717 40 LAFIRAMLLERLE--KEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEE-YAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1224 TLENERGELANEVKV--LLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA---DKVTKLQVELDNVTGLLSQSDSK 1298
Cdd:COG4717 113 ELREELEKLEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEeleAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1299 S-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKnsFREQLEEEEEAKHNLEKQIATLHAQVADMKKKME 1377
Cdd:COG4717 193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL--EAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1378 DSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 1457
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1458 TISAKYAEERDRAEAEAREKETKAL-------------SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKsvH 1524
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALlaeagvedeeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--E 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1525 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEE-KKKQLVRQV-REMEAE 1600
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELKAELRELAEEwAALKLALELlEEAREE 508
|
....*
gi 972988096 1601 LEDER 1605
Cdd:COG4717 509 YREER 513
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
961-1173 |
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 972988096 961 ARQKLQlekvTTEAKLKKLEEEQIILEdqnckLAKEKKLLEDRIAEFTTNLT-------EEEEKSKSLAKLKNKHEAMIT 1033
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAearaelaEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1034 DLEE--RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAkkeEELQAALARVEEEAAQknmALKKIRE 1111
Cdd:COG3206 258 ELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972988096 1112 LESQISELQEDLESErasrNKAEKQKRDLGEELEALKTELEDTLdstAAQQELRSKREQEVN 1173
Cdd:COG3206 332 LQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVG 386
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1655-1879 |
3.40e-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: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1655 RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEE--LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA 1732
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1733 RIAQLEEELEEEQGNTELINDRLkkanlQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASI 1812
Cdd:COG3206 248 QLGSGPDALPELLQSPVIQQLRA-----QLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1813 TALEAKIAQLEEQLDNETKERQaackQVRRTEKKLKDvlLQvdderRNAEQYKDQADKASTRLKQLK 1879
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLA----ELPELEAELRR--LE-----REVEVARELYESLLQRLEEAR 378
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1326-1891 |
3.49e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1326 QKLSLSTKLKQVEDEKN----SFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAE-------EVKRKLQ 1394
Cdd:pfam05557 3 ELIESKARLSQLQNEKKqmelEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEealreqaELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1395 KDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERD------ 1468
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQnlekqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1469 --RAEAEAREKE--------TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQvE 1538
Cdd:pfam05557 163 ssLAEAEQRIKElefeiqsqEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-E 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1539 EMKTQLEELEDELQATEdAKLRLEVNLQAMKAQFER---DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRsmavaar 1615
Cdd:pfam05557 242 KYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1616 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSME--AEMIQLQE 1690
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1691 ELAAAERAkrqaqqeRDELADEIANSSGKGALALEekRRLEARIAQLEEELeeeQGNTELINDRLKKANlqidqinTDLN 1770
Cdd:pfam05557 394 AHNEEMEA-------QLSVAEEELGGYKQQAQTLE--RELQALRQQESLAD---PSYSKEEVDSLRRKL-------ETLE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1771 LERshaqknenarQQLERQNKELKVKL--QEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLK 1848
Cdd:pfam05557 455 LER----------QRLREQKNELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLE 524
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 972988096 1849 DVLLQVDderRNAEQYKDQADKastRLKQLKRQLEEAEEEAQR 1891
Cdd:pfam05557 525 DDLEQVL---RLPETTSTMNFK---EVLDLRKELESAELKNQR 561
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
966-1348 |
3.72e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 55.35 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 966 QLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQ 1045
Cdd:COG5185 225 AKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1046 RQELEKTRRKLEgdstdlsdqiaelQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkiRELESQISELQEDLES 1125
Cdd:COG5185 305 IDIKKATESLEE-------------QLAAAEAEQELEESKRETETGIQNLTAEIEQGQ------ESLTENLEAIKEEIEN 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1126 ERASRNKAEKQkrdlgEELEALKTELEDTLDSTaaQQELRSKREQEVNILkKTLEEEAKTHEAQIQEMRQKHSQAVEELA 1205
Cdd:COG5185 366 IVGEVELSKSS-----EELDSFKDTIESTKESL--DEIPQNQRGYAQEIL-ATLEDTLKAADRQIEELQRQIEQATSSNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1206 EQleqtkrvkanlEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKveaqlQELQVKFNEGERVRTELADKV----TKL 1281
Cdd:COG5185 438 EV-----------SKLLNELISELNKVMREADEESQSRLEEAYDEIN-----RSVRSKKEDLNEELTQIESRVstlkATL 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972988096 1282 QVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLK-----QVEDEKNSFREQL 1348
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNaktdgQAANLRTAVIDEL 573
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1409-1921 |
4.81e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.91 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1409 AAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTIsakyAEERDRAEAEAREKETKALSLARAL 1488
Cdd:PRK01156 166 RNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSIT----LKEIERLSIEYNNAMDDYNNLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1489 EEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKR-----------------ALEQQVEEMKTQLEELEDEL 1551
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1552 QATEDAKLRLEVnLQAMKAQFERDLQGRDE---------QSEEKKKQLVRQVREMEAELEDERKQR-------------- 1608
Cdd:PRK01156 322 NKYHAIIKKLSV-LQKDYNDYIKKKSRYDDlnnqileleGYEMDYNSYLKSIESLKKKIEEYSKNIermsafiseilkiq 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1609 ----SMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKD---------CMRELDDTRASReeilaQAKENE 1675
Cdd:PRK01156 401 eidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcpvCGTTLGEEKSNH-----IINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1676 KKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRL 1755
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1756 KKANLQI-DQINTDLNleRSHAQKN----ENARQQLERQNKELK---VKLQEMEGT---VKSKYKASITALEAKIAQLEE 1824
Cdd:PRK01156 556 KSLKLEDlDSKRTSWL--NALAVISlidiETNRSRSNEIKKQLNdleSRLQEIEIGfpdDKSYIDKSIREIENEANNLNN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1825 QLdNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELE 1904
Cdd:PRK01156 634 KY-NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
570
....*....|....*..
gi 972988096 1905 DATETADAMNREVSSLK 1921
Cdd:PRK01156 713 ELSDRINDINETLESMK 729
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1631-1848 |
5.29e-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: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1631 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1710
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1711 DEIANSSGKGAL--ALEEKRRLEARIAQLEEELEEEQGNTELINDrLKKANLQIDQINTDLnlershaqknENARQQLER 1788
Cdd:COG3883 93 RALYRSGGSVSYldVLLGSESFSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAEL----------EAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1789 QNKELKVKLQEMEgTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLK 1848
Cdd:COG3883 162 LKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
935-1133 |
5.38e-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: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 935 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEqiiLEDQNCKLAKEKKLLEDRIAEF------- 1007
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGERARALyrsggsv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1008 --------TTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKM 1079
Cdd:COG3883 103 syldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1080 QLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKA 1133
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1029-1163 |
5.47e-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: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1029 EAMITDLEERLRRE--EKQRQELEKTRRKLEGDSTDLSD------------QIAELQAQIAELKMQLAKKEEELQAALAR 1094
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972988096 1095 VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQkrdlgEELEALKTEL---EDTLDSTAAQQE 1163
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1110-1921 |
5.74e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.96 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1110 RELESQISELQEDLESERASRNKAEKQKRDLGEELEALkteledtldsTAAQQELrskrEQEVNILKKTLeeeAKTHEA- 1188
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVEMARELEEL----------SARESDL----EQDYQAASDHL---NLVQTAl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1189 QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGD-----SEHKRKKVEAQlQELQVK 1263
Cdd:COG3096 344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqalDVQQTRAIQYQ-QAVQAL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1264 fnEGERVRTELADkvtklqVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELlQEENRQKLSLSTKLK-QVEDEK- 1341
Cdd:COG3096 423 --EKARALCGLPD------LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAA-RRQFEKAYELVCKIAgEVERSQa 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1342 -NSFREQLEEEEEAKHNLEkQIATLHAQVADmkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTR 1420
Cdd:COG3096 494 wQTARELLRRYRSQQALAQ-RLQQLRAQLAE-----------LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1421 LQQELDDLLVDLDHQRQSACNLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLA--RALEEAMEQKAEL 1498
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQL---EQLRARIKELAARAPAWLAAQDALERLREQSGEALAdsQEVTAAMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1499 ERLNKQfrtemedlmsSKDdvgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQATEDAKLRLEVNLQ----- 1566
Cdd:COG3096 639 EREATV----------ERD-------ELAARKQALESQIERLSqpggaedPRLLALAERLGGVLLSEIYDDVTLEdapyf 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1567 ------AMKAQFERDLQGrdeqseekkkqlvrqVREMEAELED--------ERKQRSMAVAARKKLEMDLKDL------- 1625
Cdd:COG3096 702 salygpARHAIVVPDLSA---------------VKEQLAGLEDcpedlyliEGDPDSFDDSVFDAEELEDAVVvklsdrq 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1626 -----------------EAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKklksmEAEMiql 1688
Cdd:COG3096 767 wrysrfpevplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDP-----EAEL--- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1689 qeelaaaerakRQAQQERDELADEIANssgkgalaleekrrLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQintd 1768
Cdd:COG3096 839 -----------AALRQRRSELERELAQ--------------HRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE---- 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1769 lnlerSHAQKNENARQQLErqnkelkvKLQEMEGTVKSKYKAsITALEAKIAQL------EEQLDNETKERQAACKQVRR 1842
Cdd:COG3096 890 -----TLADRLEELREELD--------AAQEAQAFIQQHGKA-LAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRRLKQ 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1843 TEKKLKDVLlqvddERRNAEQYKD---QADKASTRLKQLKRQLEeaeeeaqRANASRRKLQRELEDATETADAMNREVSS 1919
Cdd:COG3096 956 QIFALSEVV-----QRRPHFSYEDavgLLGENSDLNEKLRARLE-------QAEEARREAREQLRQAQAQYSQYNQVLAS 1023
|
..
gi 972988096 1920 LK 1921
Cdd:COG3096 1024 LK 1025
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
877-1613 |
5.79e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.96 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 877 LQSQLMAEKLQLQEQLQAETELCAE-AEELRARLTAKKQELEEICHDLEARVEEEEE-RCQHLQAekKKMQQNIQELEEQ 954
Cdd:COG3096 413 IQYQQAVQALEKARALCGLPDLTPEnAEDYLAAFRAKEQQATEEVLELEQKLSVADAaRRQFEKA--YELVCKIAGEVER 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 955 LEEEESAR--------QKLQLEKVTT-EAKLKKLEEEqiiLEDQNcklaKEKKLLEDRIAEFTTNLTEEEEksksLAKLK 1025
Cdd:COG3096 491 SQAWQTARellrryrsQQALAQRLQQlRAQLAELEQR---LRQQQ----NAERLLEEFCQRIGQQLDAAEE----LEELL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1026 NKHEAMITDLEERLRREEKQRQELektRRKLEgdstdlsdqiaELQAQIAELKmQLAKKEEELQAALARVEEEAAQknmA 1105
Cdd:COG3096 560 AELEAQLEELEEQAAEAVEQRSEL---RQQLE-----------QLRARIKELA-ARAPAWLAAQDALERLREQSGE---A 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1106 LKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALkteledTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1185
Cdd:COG3096 622 LADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL------SQPGGAEDPRLLALAERLGGVLLSEIYDDVTL 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1186 HEAQIQEMR---QKHSQAVEELAeqleqtkRVKANLEKAKQTLEN----ERGELANEVKVLlqgkgDSEHKRKKVEAQLQ 1258
Cdd:COG3096 696 EDAPYFSALygpARHAIVVPDLS-------AVKEQLAGLEDCPEDlyliEGDPDSFDDSVF-----DAEELEDAVVVKLS 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1259 ELQVKFNE-------GERVRTELADkvtKLQVELDNVTGLLSQSD---SKSSKLTKDFSALESQ------LQDTQELLQE 1322
Cdd:COG3096 764 DRQWRYSRfpevplfGRAAREKRLE---ELRAERDELAEQYAKASfdvQKLQRLHQAFSQFVGGhlavafAPDPEAELAA 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1323 ENRQklslstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGclETAEEVKRKLQKDLEGLS- 1401
Cdd:COG3096 841 LRQR-------RSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLA--DRLEELREELDAAQEAQAf 911
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1402 -QRHEEKVAaydKLEKTKTRLQQELDdllvdldhqrqsacNLEKKQKKFDQLLAEEKTISAK---YAEERDRAEAEAREK 1477
Cdd:COG3096 912 iQQHGKALA---QLEPLVAVLQSDPE--------------QFEQLQADYLQAKEQQRRLKQQifaLSEVVQRRPHFSYED 974
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1478 ETKALSLARALEEAMEQK---AELERLnkQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELedELQAT 1554
Cdd:COG3096 975 AVGLLGENSDLNEKLRARleqAEEARR--EAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL--GVQAD 1050
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1555 EDAKLRLEVNLQAMKAQFERDLQGRDE------QSEEKKKQLVRQVREMEAELEDERKQRSMAVA 1613
Cdd:COG3096 1051 AEAEERARIRRDELHEELSQNRSRRSQlekqltRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA 1115
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1029-1870 |
6.71e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.06 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1029 EAMITDLEERLRREEKQRQELEKTRRKL-----EGDSTDLSDQIAELQAQI-AELKMQLAK-------KEEELQAALARV 1095
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQNMETATVELhlsniENKKNELLDIIVEIKKHIhGEINKDLNKiledfknKEKELSNKINDY 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1096 EEEAAQKNMALKKIRELESQISElQEDLESerasrNKAEKQKRDLGEELEALKTeledtldsTAAQQELRSKREQEVnil 1175
Cdd:TIGR01612 775 AKEKDELNKYKSKISEIKNHYND-QINIDN-----IKDEDAKQNYDKSKEYIKT--------ISIKEDEIFKIINEM--- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1176 kKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQL-EQTKRVKANLEKAKQTLE----NERGELANEVKVLLQGKGDSEHKR 1250
Cdd:TIGR01612 838 -KFMKDDFLNKVDKFINFENNCKEKIDSEHEQFaELTNKIKAEISDDKLNDYekkfNDSKSLINEINKSIEEEYQNINTL 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1251 KKVEaqlQELQVKFNEGERVRtELADKVTKLQVELDNVTGLLSQSDS---------------KSSKLTKDFS--ALESQL 1313
Cdd:TIGR01612 917 KKVD---EYIKICENTKESIE-KFHNKQNILKEILNKNIDTIKESNLieksykdkfdntlidKINELDKAFKdaSLNDYE 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1314 QDTQELLQEENRQKLSLSTklkqveDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVgcLETAEEVKRKL 1393
Cdd:TIGR01612 993 AKNNELIKYFNDLKANLGK------NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI--YNIIDEIEKEI 1064
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1394 QKDLEGLSQRHEEKV-AAYDKLEKTKTRLqqelddllvdldhqrqsacnlekKQKKFDQLLAEEktiSAKYAEERDRAea 1472
Cdd:TIGR01612 1065 GKNIELLNKEILEEAeINITNFNEIKEKL-----------------------KHYNFDDFGKEE---NIKYADEINKI-- 1116
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1473 eareketkalslaraleeameqKAELERLNKQfrtemedlmsskddVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQ 1552
Cdd:TIGR01612 1117 ----------------------KDDIKNLDQK--------------IDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1553 AT---EDAKlRLEVNLQAMKAQFERDLQGRDEQseekkKQLVRQVREMEAELEDERKQRSMAVAARKKLEmdlKDLEAHI 1629
Cdd:TIGR01612 1161 KAisnDDPE-EIEKKIENIVTKIDKKKNIYDEI-----KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLG---KLFLEKI 1231
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1630 DSANKNRDEAIKQLRKLqaqmkdcMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEelaaaERAKRQAQQERDEL 1709
Cdd:TIGR01612 1232 DEEKKKSEHMIKAMEAY-------IEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD-----DKDHHIISKKHDEN 1299
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1710 ADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKK-AN----LQIDQINTDLNLERSHAQKnenarq 1784
Cdd:TIGR01612 1300 ISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEiANiyniLKLNKIKKIIDEVKEYTKE------ 1373
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1785 qLERQNKELKVKLQEMEGTVKsKYKASITALEAKiAQLEEQLDNetkerqaacKQVRRTEKKLKDVLLQVDDERRNAEQY 1864
Cdd:TIGR01612 1374 -IEENNKNIKDELDKSEKLIK-KIKDDINLEECK-SKIESTLDD---------KDIDECIKKIKELKNHILSEESNIDTY 1441
|
....*.
gi 972988096 1865 KDQADK 1870
Cdd:TIGR01612 1442 FKNADE 1447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1360-1617 |
6.76e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1360 KQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQElddllvdldhqrqsa 1439
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE--------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1440 cnLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDV 1519
Cdd:COG4942 85 --LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1520 GKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAmkaqferdLQGRDEQSEEKKKQLVRQVREMEA 1599
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE--------LAAELAELQQEAEELEALIARLEA 234
|
250
....*....|....*...
gi 972988096 1600 ELEDERKQRSMAVAARKK 1617
Cdd:COG4942 235 EAAAAAERTPAAGFAALK 252
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1028-1280 |
8.31e-07 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 53.22 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1028 HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalk 1107
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1108 kirELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ--EVNILKKTLEEEAKT 1185
Cdd:pfam09787 115 ---ELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQltETLIQKQTMLEALST 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1186 heaqiqemrQKHSQAVEelaeqleqtkrvkanLEKAKQTLENERGELANEVKVLLQGKGDSEHKRkkveaqLQELQVKFN 1265
Cdd:pfam09787 192 ---------EKNSLVLQ---------------LERMEQQIKELQGEGSNGTSINMEGISDGEGTR------LRNVPGLFS 241
|
250
....*....|....*
gi 972988096 1266 EGERVRTELADKVTK 1280
Cdd:pfam09787 242 ESDSDRAGMYGKVRK 256
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
857-1705 |
9.59e-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: 54.19 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 857 LVKVREKQLAAENRLTEMetlqsqlmAEKLQLQEQLQA--ETELCAEAEELRARLTAKKQ---------ELEEICHDLEA 925
Cdd:COG3096 294 LFGARRQLAEEQYRLVEM--------ARELEELSARESdlEQDYQAASDHLNLVQTALRQqekieryqeDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 926 R---VEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILedQNCKLAKEKklLED 1002
Cdd:COG3096 366 QeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALC--GLPDLTPEN--AED 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1003 RIAEFTtnlteeeekskslAKLKNKHEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQiaelkmQLA 1082
Cdd:COG3096 442 YLAAFR-------------AKEQQATEEVL-ELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTAR------ELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1083 KKEEELQAALARVEEEAAQknmalkkIRELEsQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDStaAQQ 1162
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQ-------LAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE--LEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1163 ELRSKREQevnilKKTLEEEAKTHEAQIQEMRQKH------SQAVEELAEQLEQTKRVKANLEKAKQT-LENERGelane 1235
Cdd:COG3096 572 QAAEAVEQ-----RSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEALADSQEVTAAMQQlLERERE----- 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1236 vkvLLQGKGDSEHKRKKVEAQLQEL-QVKFNEGERVRTeLADKV--TKLQVELDNVT--------GLLsqSDSKSSKLTK 1304
Cdd:COG3096 642 ---ATVERDELAARKQALESQIERLsQPGGAEDPRLLA-LAERLggVLLSEIYDDVTledapyfsALY--GPARHAIVVP 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1305 DFSALESQLQDTQE-----LLQEENRQKLSLST-KLKQVEDE---KNSFReQLEEEEEAKHNL------EKQIATLHAQv 1369
Cdd:COG3096 716 DLSAVKEQLAGLEDcpedlYLIEGDPDSFDDSVfDAEELEDAvvvKLSDR-QWRYSRFPEVPLfgraarEKRLEELRAE- 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1370 ADmkkkmEDSVGCLETAEEVkRKLQKDLEGLSQ---RH------EEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAC 1440
Cdd:COG3096 794 RD-----ELAEQYAKASFDV-QKLQRLHQAFSQfvgGHlavafaPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLD 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1441 NLEKKQKKFDQLLAEEKTISAKYAEERDRaeaEAREKetkalslaraLEEAMEQKAELERLNKQFRtEMEDLMSSKDDVG 1520
Cdd:COG3096 868 QLKEQLQLLNKLLPQANLLADETLADRLE---ELREE----------LDAAQEAQAFIQQHGKALA-QLEPLVAVLQSDP 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1521 KSVHELEKSKRALEQQVEEMKTQLEELEDELQ-----ATEDAKLRLEVN---LQAMKAQFERDLQGRdEQSEEKKKQLVR 1592
Cdd:COG3096 934 EQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLGENsdlNEKLRARLEQAEEAR-REAREQLRQAQA 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1593 QVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRdeAIKQLRKLQAQmkdcmreLDDTRASREEIlaqak 1672
Cdd:COG3096 1013 QYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEER--ARIRRDELHEE-------LSQNRSRRSQL----- 1078
|
890 900 910
....*....|....*....|....*....|...
gi 972988096 1673 enEKKLKSMEAEMIQLQEELAAAERAKRQAQQE 1705
Cdd:COG3096 1079 --EKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
794-1252 |
9.60e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 794 RGYLARKAFAKRQQQLTAMKVLQRNCAAYLKLRNWQWWRLFT---KVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENR 870
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQ 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 871 LTEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEICHDLEARVEEEeercQHLQAEKKKMQQNIQ 949
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEdVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD----NRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 950 ELEEQLEEEESARQKLQLEKVTTEAKLK-KLEEEQIILEDQNCklAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKh 1028
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQpEQDLQDVRLHLQQC--SQELALKLTALHALQLTLTQERVREHALSIRVLP- 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1029 eamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1108
Cdd:TIGR00618 672 -------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQS 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1109 IRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA 1188
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1189 QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEnergELANEVKVLLQGKGDSEHKRKK 1252
Cdd:TIGR00618 825 TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----QLTQEQAKIIQLSDKLNGINQI 884
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
900-1506 |
9.78e-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: 53.98 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 900 AEAEELRARLTAKKQELE--EICH-----DLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKlQLEkvtt 972
Cdd:pfam05557 2 AELIESKARLSQLQNEKKqmELEHkrariELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALRE-QAE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 973 EAKLKKLEEEQIiledqnCKLAKEKKLLEDRIAEFTTNLTEEeeksksLAKLknKHEAMITDLEERLRREEKQ--RQELE 1050
Cdd:pfam05557 77 LNRLKKKYLEAL------NKKLNEKESQLADAREVISCLKNE------LSEL--RRQIQRAELELQSTNSELEelQERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1051 KTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKEEelqaaLARVEEEAAQKNMALKKIRELESQISELQEDLESERASR 1130
Cdd:pfam05557 143 LLKAKA----SEAEQLRQNLEKQQSSLAEAEQRIKE-----LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1131 NKAEKQKRD---LGEELEALKTELEDTLDSTAAQQELRSKREQevniLKKTLEEEAKTHEAQIQEMRQKhsqavEELAEQ 1207
Cdd:pfam05557 214 KHLNENIENkllLKEEVEDLKRKLEREEKYREEAATLELEKEK----LEQELQSWVKLAQDTGLNLRSP-----EDLSRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1208 LEQTKRVKANLEKAKQTLENERGELANEVKVLlqgkgdsEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDN 1287
Cdd:pfam05557 285 IEQLQQREIVLKEENSSLTSSARQLEKARREL-------EQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1288 VTGLLSQSDSK------SSKLTKDFSALESQLQDTQELLQEenrqklsLSTKLKQVEDEKNSFREQLEEeeeakhnLEKQ 1361
Cdd:pfam05557 358 YRAILESYDKEltmsnySPQLLERIEEAEDMTQKMQAHNEE-------MEAQLSVAEEELGGYKQQAQT-------LERE 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1362 IATLHAQVAdmkkkMEDSVGCLETAEEVKRKLQkDLEGLSQRHEEKVAAYDkLEKTKTRLQQELDDLLVDLDHQRQSACN 1441
Cdd:pfam05557 424 LQALRQQES-----LADPSYSKEEVDSLRRKLE-TLELERQRLREQKNELE-MELERRCLQGDYDPKKTKVLHLSMNPAA 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1442 LEKKQKK--FDQLLAEEKTISAKYAEERDRAEAEAREKETkalSLARALEEAMEQKAELERLNKQFR 1506
Cdd:pfam05557 497 EAYQQRKnqLEKLQAEIERLKRLLKKLEDDLEQVLRLPET---TSTMNFKEVLDLRKELESAELKNQ 560
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1021-1155 |
9.81e-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: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1021 LAKLKNKHEAmiTDLEERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE---EELQAALARVEE 1097
Cdd:COG2433 382 LEELIEKELP--EEEPEAEREKEHEERELTEEEEEIR----RLEEQVERLEAEVEELEAELEEKDeriERLERELSEARS 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1098 EAAQKNMALKKIRELESQISELQEDLESErasRNKAEKQKRDLGEELEALKTELEDTL 1155
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1068-1343 |
1.10e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1068 AELQAQIAELKMQlaKKEEELQAALARVEEEAAQknmALKKIRELESQISELQEDLEserasrnKAEKQKRDLGEELEAL 1147
Cdd:PRK11281 39 ADVQAQLDALNKQ--KLLEAEDKLVQQDLEQTLA---LLDKIDRQKEETEQLKQQLA-------QAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1148 KTELEDTLDSTAAQQELRskreqevnilkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN 1227
Cdd:PRK11281 107 KDDNDEETRETLSTLSLR------------QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1228 ERGELANevkVLLQGKGDSEHKRKKVEAQLQ--ELQVKFNegervRTELADKvTKLQvELDNvtgllSQSDSKSSKLTKd 1305
Cdd:PRK11281 175 IRNLLKG---GKVGGKALRPSQRVLLQAEQAllNAQNDLQ-----RKSLEGN-TQLQ-DLLQ-----KQRDYLTARIQR- 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 972988096 1306 fsaLESQLQDTQELLqeeNRQKLSLSTklKQVEDEKNS 1343
Cdd:PRK11281 239 ---LEHQLQLLQEAI---NSKRLTLSE--KTVQEAQSQ 268
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1003-1327 |
1.18e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.75 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1003 RIAEFTTNLTEEEEKSKSLAKLKNkheAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA 1082
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSD---FQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1083 KKEEELQAalarveeeAAQKNMalkKIRELESQISELQEDLESERASRNKAEKQkrdLGEELEALKTE---LEDtlDSTA 1159
Cdd:PLN02939 181 ETDARIKL--------AAQEKI---HVEILEEQLEKLRNELLIRGATEGLCVHS---LSKELDVLKEEnmlLKD--DIQF 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1160 AQQELRSKREQEVNILKktLEEEAKTHEAQIQEMRQKHSQAVEELAEQleQTKRVKANLEKAkQTLENERGELANEVK-- 1237
Cdd:PLN02939 245 LKAELIEVAETEERVFK--LEKERSLLDASLRELESKFIVAQEDVSKL--SPLQYDCWWEKV-ENLQDLLDRATNQVEka 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1238 -VLLQGKGDSEHKRKKVEAQLQELQV-KFNegervrtelADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQD 1315
Cdd:PLN02939 320 aLVLDQNQDLRDKVDKLEASLKEANVsKFS---------SYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
330
....*....|..
gi 972988096 1316 TQELLQEENRQK 1327
Cdd:PLN02939 391 TLSKLKEESKKR 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1525-1746 |
1.21e-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: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1525 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQSEEKKKQLVRQVREMEAELEDE 1604
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1605 RKQ-RSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1683
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLLSPEDFL----DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 972988096 1684 EMIQLQEELAAAERAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQLEEELEEEQG 1746
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLE--------------KELAELAAELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1271-1500 |
1.26e-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: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1271 RTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEE 1350
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1351 EeeaKHNLEKQIATLHaqvadmKKKMEDSVGCLETAEEVKRkLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLV 1430
Cdd:COG4942 102 Q---KEELAELLRALY------RLGRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1431 DLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELER 1500
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1384-1913 |
1.48e-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: 53.57 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1384 ETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKY 1463
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1464 AEERDRAEAEAREKETKALSLARALE------EAMEQKAELERLNKQFR--TEMEDLMSSKDDVGKSVHELEKSKRALEQ 1535
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEkmilafEELRVQAENARLEMHFKlkEDHEKIQHLEEEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1536 QVEEMKTQLEELEDELQATEDAKLRLEvnlqamkaqferdlqGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAAR 1615
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLE---------------EKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1616 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE----NEKKLKSMEAEMIQLQEE 1691
Cdd:pfam05483 313 KALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNEDQLKIITMELQKKSSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1692 LAAAERAKRQAQQERDEL--------------------ADEIANSSGKGALALEEKRR----LEARI-----AQLEEELE 1742
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELkkilaedeklldekkqfekiAEELKGKEQELIFLLQAREKeihdLEIQLtaiktSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1743 EEQGNTELINDRLKKANL------------QIDQINTDLNLE-RSHAQKNENARQQLERQNKELKvKLQEMEGTVKSKYK 1809
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELtahcdklllenkELTQEASDMTLElKKHQEDIINCKKQEERMLKQIE-NLEEKEMNLRDELE 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1810 ASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEA 1889
Cdd:pfam05483 552 SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
570 580
....*....|....*....|....
gi 972988096 1890 QRANASRRKLQRELEDATETADAM 1913
Cdd:pfam05483 632 NAYEIKVNKLELELASAKQKFEEI 655
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
863-1562 |
1.56e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.22 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 863 KQLAAENRLTEMETLQSQ--LMAEKLQLQEQLQAETELCAEAEELRARLTAKkqelEEICHDLEARVEEEEERCQHLQAE 940
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKmrLEAQAMELDALAVAEKAGQAEAEGLRAALAGA----EMVRKNLEEGSQRELEEIQRLHQE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 941 kkkmQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQncklaKEKKLLEDRIAEfttnLTEEEEKSKS 1020
Cdd:pfam07111 152 ----QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQ-----KEAELLRKQLSK----TQEELEAQVT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1021 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQ---AALARVEE 1097
Cdd:pfam07111 219 LVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTrkiQPSDSLEP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1098 EAAQKNMALkkIRELESQISELQEDLESERASRNKAEKQKRDLGEELealkteledtldstaaqQELRSKREQEVNILKK 1177
Cdd:pfam07111 299 EFPKKCRSL--LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL-----------------QEQVTSQSQEQAILQR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1178 TLEEeaKTHEAQIQEMRQKHSQAveELAEQLEQTKRVKANLEKAKQTLENERGELanevkvllqgkgdsehkrKKVEAQL 1257
Cdd:pfam07111 360 ALQD--KAAEVEVERMSAKGLQM--ELSRAQEARRRQQQQTASAEEQLKFVVNAM------------------SSTQIWL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1258 QELQVKFNEGERVRTELADKVTKLQVELDNVTGL------LSQSDSKSSKLTKDFSALESQLQ-DTQELLQEENRQKLSL 1330
Cdd:pfam07111 418 ETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLmarkvaLAQLRQESCPPPPPAPPVDADLSlELEQLREERNRLDAEL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1331 STKLKQVEDEKNSFREQ----LEEEEEAKHNLEKQIATLHAQVADMKKKMEDSV-GCLETAEE---VKRKLQKDLEGLSQ 1402
Cdd:pfam07111 498 QLSAHLIQQEVGRAREQgeaeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARqGQQESTEEaasLRQELTQQQEIYGQ 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1403 RHEEKVAaydkleKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISakyaEERDRAEAEAREKEtkAL 1482
Cdd:pfam07111 578 ALQEKVA------EVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERN----QELRRLQDEARKEE--GQ 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1483 SLARALEE----------AMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV---EEMKTQLEELED 1549
Cdd:pfam07111 646 RLARRVQElerdknlmlaTLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPIPAAVptrESIKGSLTVLLD 725
|
730
....*....|...
gi 972988096 1550 ELQATEDAKLRLE 1562
Cdd:pfam07111 726 NLQGLSEAISREE 738
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1435-1803 |
1.87e-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: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1435 QRQSACNLEKKQKKFDqllaeektisaKYAEERDRAEAEAREKEtkalslaraleeaMEQKAELERLNKQFRTEMEDlms 1514
Cdd:pfam17380 279 QHQKAVSERQQQEKFE-----------KMEQERLRQEKEEKARE-------------VERRRKLEEAEKARQAEMDR--- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1515 skddvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLrlevnlqAMKAQFERDLQgRDEQSEEKKKQLVRQv 1594
Cdd:pfam17380 332 ------QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEI-------AMEISRMRELE-RLQMERQQKNERVRQ- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1595 remeaELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN 1674
Cdd:pfam17380 397 -----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1675 EKKLKSmeaemiqlqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRR-LEARIAQLEEELEEEQGNTELIND 1753
Cdd:pfam17380 472 RKRKKL----------ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERRREAEEE 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1754 RLKKANL----QIDQINTDLNLERSHAQKNENARQQLeRQNKELKVKLQEMEGT 1803
Cdd:pfam17380 542 RRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
996-1221 |
1.99e-06 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 53.40 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 996 EKKLLEDRiaeftTNLTEEEEKSKSLAklknkhEAMITDLEERLRREEKQRQELEKTRR-----------KLEGDSTDLs 1064
Cdd:PLN03188 1046 EKKLEQER-----LRWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRcaeelkeamqmAMEGHARML- 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1065 DQIAELQaqiaELKMQLAKKEEELQAALARVEEEAAQ---KNMALKKIRELESQISELQedleSERasrnkaEKQKRDLG 1141
Cdd:PLN03188 1114 EQYADLE----EKHIQLLARHRRIQEGIDDVKKAAARagvRGAESKFINALAAEISALK----VER------EKERRYLR 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1142 EELEALKTELEDTLDSTAAQQEL--RSKREQEVNIL--KKTLEEEAKTHEA--QIQEMRQKHSQAVEELAEQLEQTKRVK 1215
Cdd:PLN03188 1180 DENKSLQAQLRDTAEAVQAAGELlvRLKEAEEALTVaqKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPK 1259
|
....*.
gi 972988096 1216 ANLEKA 1221
Cdd:PLN03188 1260 EAIRPA 1265
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1661-1926 |
2.17e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1661 RASREEiLAQAKENEKKLKSMEAEMIQ----LQEELAAAERAKRQAQQERDELADEIANSSGKgalALEEKRRLEARIAQ 1736
Cdd:TIGR02169 173 EKALEE-LEEVEENIERLDLIIDEKRQqlerLRREREKAERYQALLKEKREYEGYELLKEKEA---LERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1737 LEEELEEEQGNTELINDRLKKANLQIDQINTDLNlershaQKNENARQQLERQNKELKvklqemegtvkskykASITALE 1816
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIK------DLGEEEQLRVKEKIGELE---------------AEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1817 AKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASR 1896
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270
....*....|....*....|....*....|
gi 972988096 1897 RKLQRELEDATETADAMNREVSSLKNKLRR 1926
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
921-1924 |
2.31e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.13 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 921 HDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlEKVTTEAK----LKKLEEEQIILEDQNCKLAKE 996
Cdd:TIGR01612 561 HEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELK-EKIKNISDkneyIKKAIDLKKIIENNNAYIDEL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 997 KKLLEDRIAEFTTNL-----TEEEEKSK----SLAKLKN--------------KHEAMITDLEERLRREEKQRQELEKTR 1053
Cdd:TIGR01612 640 AKISPYQVPEHLKNKdkiysTIKSELSKiyedDIDALYNelssivkenaidntEDKAKLDDLKSKIDKEYDKIQNMETAT 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1054 RKL-----EGDSTDLSDQIAELQAQI-AELKMQLAK-------KEEELQAALARVEEEAAQKNMALKKIRELESQISElQ 1120
Cdd:TIGR01612 720 VELhlsniENKKNELLDIIVEIKKHIhGEINKDLNKiledfknKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND-Q 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1121 EDLESerasrNKAEKQKRDLGEELEALKTeledtldsTAAQQELRSKREQEVnilkKTLEEEAKTHEAQIQEMRQKHSQA 1200
Cdd:TIGR01612 799 INIDN-----IKDEDAKQNYDKSKEYIKT--------ISIKEDEIFKIINEM----KFMKDDFLNKVDKFINFENNCKEK 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1201 VEELAEQL-EQTKRVKANLEKAKQTLE----NERGELANEVKVLLQGKGDSEHKRKKVEaqlQELQVKFNEGERVRtELA 1275
Cdd:TIGR01612 862 IDSEHEQFaELTNKIKAEISDDKLNDYekkfNDSKSLINEINKSIEEEYQNINTLKKVD---EYIKICENTKESIE-KFH 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1276 DKVTKLQVELDNVTGLLSQSDS---------------KSSKLTKDFS--ALESQLQDTQELLQEENRQKLSLSTklkqve 1338
Cdd:TIGR01612 938 NKQNILKEILNKNIDTIKESNLieksykdkfdntlidKINELDKAFKdaSLNDYEAKNNELIKYFNDLKANLGK------ 1011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1339 DEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVgcLETAEEVKRKLQKDLEGLSQRHEEKV-AAYDKLEKT 1417
Cdd:TIGR01612 1012 NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI--YNIIDEIEKEIGKNIELLNKEILEEAeINITNFNEI 1089
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1418 KTRLqqelddllvdldhqrqsacnlekKQKKFDQLLAEEktiSAKYAEERDRAEAEAREKETKALSLARALEEAmeqKAE 1497
Cdd:TIGR01612 1090 KEKL-----------------------KHYNFDDFGKEE---NIKYADEINKIKDDIKNLDQKIDHHIKALEEI---KKK 1140
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1498 LERLNKQFRTEMEDLMSSKDDV--GKSVHELEKSKRALEQQVEEMKTQLEELE---DELQATEDAKLRLEvNLQAMKAQF 1572
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDVADKAisNDDPEEIEKKIENIVTKIDKKKNIYDEIKkllNEIAEIEKDKTSLE-EVKGINLSY 1219
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1573 ERDLQGRD-EQSEEKKKQLVRQVREMEAELE--DERKQRSMAVAARKKLEMDLK------------DLEAHIDSanKNRD 1637
Cdd:TIGR01612 1220 GKNLGKLFlEKIDEEKKKSEHMIKAMEAYIEdlDEIKEKSPEIENEMGIEMDIKaemetfnishddDKDHHIIS--KKHD 1297
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1638 EAIKQLRKLQAQM-KDCMRE--LDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAEraKRQAQQERDELADEIA 1714
Cdd:TIGR01612 1298 ENISDIREKSLKIiEDFSEEsdINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNK--IKKIIDEVKEYTKEIE 1375
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1715 NSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDrlKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELK 1794
Cdd:TIGR01612 1376 ENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDD--KDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVL 1453
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1795 VKLQEMEGT-------VKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKlKDVLLQVDDE---------- 1857
Cdd:TIGR01612 1454 LLFKNIEMAdnksqhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELFEQYKKDvtellnkysa 1532
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1858 ---RRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNKL 1924
Cdd:TIGR01612 1533 laiKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSL 1602
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1012-1228 |
2.31e-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: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1012 TEEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA 1091
Cdd:COG3883 16 PQIQAKQKELSELQAE----LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1092 LARVEE------------------EAAQKNMALKKIRELESQ-ISELQEDLESERASRNKAEKQKrdlgEELEALKTELE 1152
Cdd:COG3883 92 ARALYRsggsvsyldvllgsesfsDFLDRLSALSKIADADADlLEELKADKAELEAKKAELEAKL----AELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1153 DTLDSTAAQQElrskreqEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENE 1228
Cdd:COG3883 168 AAKAELEAQQA-------EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
861-1102 |
2.42e-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: 52.07 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 861 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcaeaEELRARLTAKKQELeeicHDLEARVEEEEERCQHLQAE 940
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQL----------AALERRIAALARRI----RALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 941 KKKMQQNIqeleeqleeeesARQKLQLEKVTTEA-KLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEE-EEKS 1018
Cdd:COG4942 92 IAELRAEL------------EAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEElRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1019 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEE 1098
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAE 235
|
....
gi 972988096 1099 AAQK 1102
Cdd:COG4942 236 AAAA 239
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
862-1323 |
2.65e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.88 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 862 EKQLAAENR--------LTEMETLQSQLMAEKLQLQEQLQAET---------ELCAEAEELR----------ARLTAKKQ 914
Cdd:PRK10246 232 EKQLLTAQQqqqqslnwLTRLDELQQEASRRQQALQQALAAEEkaqpqlaalSLAQPARQLRphweriqeqsAALAHTRQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 915 ELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlEKVTTEAKLKKLEEEQIILEDQNCKLA 994
Cdd:PRK10246 312 QIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNN-ELAGWRAQFSQQTSDREQLRQWQQQLT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 995 KEKKLLeDRIAEFTTNLTeEEEKSKSLAKLKNKHEamitdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQI 1074
Cdd:PRK10246 391 HAEQKL-NALPAITLTLT-ADEVAAALAQHAEQRP-----LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1075 AELKMQLAKKEEELQAALARVEEEAaqknmalkKIRELESQISELQE---------------------DLESERASRNKA 1133
Cdd:PRK10246 464 NEMRQRYKEKTQQLADVKTICEQEA--------RIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLDAL 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1134 EKQKRDLGEE-------LEALKTEL---EDTLDSTAAQQELRSKREQEV----NILKKTLEE------EAKTHEAQIQEM 1193
Cdd:PRK10246 536 EKEVKKLGEEgaalrgqLDALTKQLqrdESEAQSLRQEEQALTQQWQAVcaslNITLQPQDDiqpwldAQEEHERQLRLL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1194 RQKHS-QAveELAEQLEQTKRVKANLEKAKQTLENERGELAnevkVLLQGKGDSE---HKRKKVEAQLQELQVKFNEGER 1269
Cdd:PRK10246 616 SQRHElQG--QIAAHNQQIIQYQQQIEQRQQQLLTALAGYA----LTLPQEDEEAswlATRQQEAQSWQQRQNELTALQN 689
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1270 VRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1323
Cdd:PRK10246 690 RIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLE 743
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1202-1824 |
2.73e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1202 EELAEQLEQTKRVKANLEKAKQTLENERGELAN--EVKVLLQGKGDS-EHKRKKVEAQLQELQVKFNEGERVRTELADKV 1278
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNidYLEEKLKSSNLElENIKKQIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1279 TKLQVELDNVTGLLSQSDSKSsKLTKDFSALESQLQdtqeLLQEENRQKLSLSTKLKQVEDEKnsfreqleeeEEAKHNL 1358
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKN-RYESEIKTAESDLS----MELEKNNYYKELEERHMKIINDP----------VYKNRNY 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1359 EKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQkDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDhqrqs 1438
Cdd:PRK01156 297 INDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLK----- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1439 acNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAreketkalslaralEEAMEQKAELERLNKQFRTEMEDLMSSKDD 1518
Cdd:PRK01156 371 --SIESLKKKIEEYSKNIERMSAFISEILKIQEIDP--------------DAIKKELNEINVKLQDISSKVSSLNQRIRA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1519 VGKSVHELEKSKRALEQQ----VEEMKTQLEELEDELQATEDAKLRLEVNLQamkaQFERDLQGRDEQSEEKKKQLVRQV 1594
Cdd:PRK01156 435 LRENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIR----EIEIEVKDIDEKIVDLKKRKEYLE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1595 REMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRE-------------LDDTR 1661
Cdd:PRK01156 511 SEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYE----EIKNRYKSLKLEDLDSKRTswlnalavislidIETNR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1662 ASREEILAQAKENEKKLKSMEAEMiqlqeelaaaERAKRQAQQERDELADEIANSSGKGALALEEKRRLEaRIAQLEEEL 1741
Cdd:PRK01156 587 SRSNEIKKQLNDLESRLQEIEIGF----------PDDKSYIDKSIREIENEANNLNNKYNEIQENKILIE-KLRGKIDNY 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1742 EEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYK--ASITALEAKI 1819
Cdd:PRK01156 656 KKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINEtlESMKKIKKAI 735
|
....*
gi 972988096 1820 AQLEE 1824
Cdd:PRK01156 736 GDLKR 740
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1469-1882 |
3.50e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1469 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 1524
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDleqdyqaasdhlnlvqtalrqqekIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1525 ELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1590
Cdd:PRK04863 356 DLEELEERLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQQTRAIQYQQAvQALERAKQLcglpdl 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1591 -VRQVREMEAELEDERKQrsmAVAARKKLEMDLKDLEAhidsANKNRDEAIKQLRKLQAQMkdcmrelddtraSREEILA 1669
Cdd:PRK04863 436 tADNAEDWLEEFQAKEQE---ATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEV------------SRSEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1670 QAKENEKKLKSMEAEMIQLQE---ELAAAERAKRQaQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEeleeeqg 1746
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQlrmRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE------- 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1747 ntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKVKLQEMEgtvkSKYKASITALEAkIAQLEEQL 1826
Cdd:PRK04863 569 ---------------------SLSESVSEARER---RMALRQQLEQLQARIQRLA----ARAPAWLAAQDA-LARLREQS 619
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 972988096 1827 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKAS-------TRLKQLKRQL 1882
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSqpggsedPRLNALAERF 682
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
965-1184 |
3.89e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.21 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 965 LQLEKVTTEAKLKKLEEEQI---ILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEE--KSKSLAkLKNKHEAM------IT 1033
Cdd:PLN02939 175 LEMRLSETDARIKLAAQEKIhveILEEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1034 DLEERLRREEKQRQELEKTRRKLEgdSTDLSDQiaELQAQIAELKMQ-LAKKEEELQAALARVEEEAAQKNMALKKIREL 1112
Cdd:PLN02939 254 ETEERVFKLEKERSLLDASLRELE--SKFIVAQ--EDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDL 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 972988096 1113 ESQISELQEDLESERASRNKAEKQKRdLGEELEALKTELEDTLDSTAAQQELRSKREQEV-NILKKTLEEEAK 1184
Cdd:PLN02939 330 RDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFqDTLSKLKEESKK 401
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1151-1926 |
4.40e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1151 LEDTLDSTAAQQELRSKREQEVNILKKTLEEEAkTHEAQIQEMRQKHSQAVEELA------EQLEQTKRVKANLEKAkqt 1224
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELA-ELNEAESDLEQDYQAASDHLNlvqtalRQQEKIERYQADLEEL--- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1225 leNERGELANEVKVLLQGKGDsEHKRKKVEAQLqelqvkfnEGERVRTELADKVTKLQVE-------------LDNVTGL 1291
Cdd:PRK04863 361 --EERLEEQNEVVEEADEQQE-ENEARAEAAEE--------EVDELKSQLADYQQALDVQqtraiqyqqavqaLERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1292 LSQSDSKSSKLTKDFSALESQLQD-TQELLQEEnrQKLSLSTKLKQV-----------------EDEKNSFREQLEEEEE 1353
Cdd:PRK04863 430 CGLPDLTADNAEDWLEEFQAKEQEaTEELLSLE--QKLSVAQAAHSQfeqayqlvrkiagevsrSEAWDVARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1354 AKHnLEKQIATLHAQVADMKKKMEDsvgcletaeevKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLD 1433
Cdd:PRK04863 508 QRH-LAEQLQQLRMRLSELEQRLRQ-----------QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1434 HQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAeAREKETKALSLARALEEAMEQKAELERlnkQFRTEMEdlm 1513
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR-LREQSGEEFEDSQDVTEYMQQLLERER---ELTVERD--- 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1514 sskddvgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQATEDAKLRLEVNLQ-----------AMKAQFERD 1575
Cdd:PRK04863 649 -----------ELAARKQALDEEIERLSqpggsedPRLNALAERFGGVLLSEIYDDVSLEdapyfsalygpARHAIVVPD 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1576 LQGrdeqseekkkqlvrqVREMEAELEDerkqrsmavaarkkLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDcmR 1655
Cdd:PRK04863 718 LSD---------------AAEQLAGLED--------------CPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--R 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1656 ELddtRASR--EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgALALE-----EKR 1728
Cdd:PRK04863 767 QW---RYSRfpEVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHL---AVAFEadpeaELR 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1729 RLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQIN-----TDLNLERSHAQKNENARQQLERqnkelkvkLQEMEGT 1803
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprLNLLADETLADRVEEIREQLDE--------AEEAKRF 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1804 VKsKYKASITALEAKIAQL---EEQLDNETKERQAAcKQVRRTEKKLKDVLLQVDdERRNAEQYKDQAD---KASTRLKQ 1877
Cdd:PRK04863 913 VQ-QHGNALAQLEPIVSVLqsdPEQFEQLKQDYQQA-QQTQRDAKQQAFALTEVV-QRRAHFSYEDAAEmlaKNSDLNEK 989
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 972988096 1878 LKRQLEeaeeeaqRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1926
Cdd:PRK04863 990 LRQRLE-------QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1047-1365 |
4.40e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.84 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1047 QELEKTRRKLegdstdlsDQIAELQAQIAELKMQLAKKEEELQ------AALARVEEEAAQKNMALKKIRELESQISELQ 1120
Cdd:PRK11281 63 QDLEQTLALL--------DKIDRQKEETEQLKQQLAQAPAKLRqaqaelEALKDDNDEETRETLSTLSLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1121 EDLESERASRNKAEKQkrdlgeeLEALKTELEDtldstaAQQEL--RSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHS 1198
Cdd:PRK11281 135 DQLQNAQNDLAEYNSQ-------LVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1199 QAVEELAEQLEQTKRVKANLekakQTLENERGELANEvkvllqgkgdsehKRKKVEAQLQELQVKFNEGERVRTElaDKV 1278
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNTQL----QDLLQKQRDYLTA-------------RIQRLEHQLQLLQEAINSKRLTLSE--KTV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1279 TKLQveldnvtgllsqsdsksskltkdfSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF-------REQLEEE 1351
Cdd:PRK11281 263 QEAQ------------------------SQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLtqqnlrvKNWLDRL 318
|
330
....*....|....
gi 972988096 1352 EEAKHNLEKQIATL 1365
Cdd:PRK11281 319 TQSERNIKEQISVL 332
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
996-1291 |
4.63e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.76 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 996 EKKL--LEDRIAEFTTnLTEE---EEKSKSLAKLKNKheamITDLEERLRREEKQRQELEktrrklegdsTDLSDQIAEL 1070
Cdd:PRK04778 171 EKQLenLEEEFSQFVE-LTESgdyVEAREILDQLEEE----LAALEQIMEEIPELLKELQ----------TELPDQLQEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1071 QAQIAELKMQ--------LAKKEEELQAALARVEEEAAQKNM--ALKKIRELESQISELQEDLESERASRNKAEKQKRDL 1140
Cdd:PRK04778 236 KAGYRELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDLdeAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1141 GEELEALKTELEDTldstaaQQELRskREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEK 1220
Cdd:PRK04778 316 PDFLEHAKEQNKEL------KEEID--RVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEE 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1221 AKQTL---ENERGELANEVKVLlqgkgdsehkrKKVEAQLQElqvkfnEGERVRTELADkvTKLQVELDNVTGL 1291
Cdd:PRK04778 388 ILKQLeeiEKEQEKLSEMLQGL-----------RKDELEARE------KLERYRNKLHE--IKRYLEKSNLPGL 442
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1465-1707 |
4.84e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1465 EERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 1544
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1545 EELEDELQATEDAKLRLEvNLQAMKAQFERDLQGRDeQSEEKKKQLVRQVREMEAELEDERKQRsmavaarkKLEMDLKD 1624
Cdd:COG1340 95 DELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKAL--------EKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1625 LEAHIDSANKNRDEAIKQLRKLQ-------AQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL----- 1692
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELrelrk 244
|
250 260
....*....|....*....|....
gi 972988096 1693 ---------AAAERAKRQAQQERD 1707
Cdd:COG1340 245 elkklrkkqRALKREKEKEELEEK 268
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1459-1660 |
5.81e-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: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1459 ISAKYAEERDRAEAEAREkeTKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkddvgksvhELEKSKRALEQQVE 1538
Cdd:COG2433 355 VEKKVPPDVDRDEVKARV--IRGLSIEEALEELIEKELPEEEPEAEREKEHEERELT---------EEEEEIRRLEEQVE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1539 EMKTQLEELEDELQATEDAKLRLEvnlqaMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsmavaARKKL 1618
Cdd:COG2433 424 RLEAEVEELEAELEEKDERIERLE-----RELSEARSEERREIRKDREISRLDREIERLERELEEERE-------RIEEL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 972988096 1619 EMDLKDLEAHIDSANKNRDEAIKQLRKLQaqmKDCMRELDDT 1660
Cdd:COG2433 492 KRKLERLKELWKLEHSGELVPVKVVEKFT---KEAIRRLEEE 530
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1012-1272 |
6.08e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1012 TEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAA 1091
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLR-------EELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1092 LARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQE 1171
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1172 VNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK 1251
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260
....*....|....*....|.
gi 972988096 1252 KVEAQLQELQVKFNEGERVRT 1272
Cdd:COG4372 239 LDALELEEDKEELLEEVILKE 259
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
994-1736 |
7.00e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.49 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 994 AKEKKLLEDRIAEFTTNLTEEEEKsksLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQ--IAELQ 1071
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQ---LAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQekIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1072 AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESE-------RASRNKAEKQKR------ 1138
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyQQAVQALEKARAlcglpd 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1139 ----DLGEELEALKTElEDTLDST---------------------------------------AAQQELRSKREQevnil 1175
Cdd:COG3096 434 ltpeNAEDYLAAFRAK-EQQATEEvleleqklsvadaarrqfekayelvckiageversqawqTARELLRRYRSQ----- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1176 kKTLEEEAKTHEAQIQEMRQKHS--QAVEELAEQLEQTKRVK----ANLEKAKQTLENERGELANEVKVLLQGKGDSEHK 1249
Cdd:COG3096 508 -QALAQRLQQLRAQLAELEQRLRqqQNAERLLEEFCQRIGQQldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1250 RKKVEAQLQELQVKfnegERVRTELADKVTKLQ----VELDNVTGLLSQSDSKSSKLTKdFSALESQLQDTQELLQEENR 1325
Cdd:COG3096 587 LEQLRARIKELAAR----APAWLAAQDALERLReqsgEALADSQEVTAAMQQLLERERE-ATVERDELAARKQALESQIE 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1326 QKL----SLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATL----HAQVAD----MKKKMEDSVGCLETAEEVKRKL 1393
Cdd:COG3096 662 RLSqpggAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYFSALYgparHAIVVPdlsaVKEQLAGLEDCPEDLYLIEGDP 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1394 QKDLEGLSQRHEEKVAAYDKLEKTKTRlqqelddllvdldHQRQSACNL---EKKQKKFDQLLAEEKTISAKYAEER--- 1467
Cdd:COG3096 742 DSFDDSVFDAEELEDAVVVKLSDRQWR-------------YSRFPEVPLfgrAAREKRLEELRAERDELAEQYAKASfdv 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1468 ---DRAEAEAREKETKALSLA------RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEK--------SK 1530
Cdd:COG3096 809 qklQRLHQAFSQFVGGHLAVAfapdpeAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllAD 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1531 RALEQQVEEMKTQLEELED---ELQATEDAKLRLEVNLQAMK---AQFERdLQGRDEQSEEKKKQLVRQVREMEaeledE 1604
Cdd:COG3096 889 ETLADRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----E 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1605 RKQRSMAVAARKKLEM-----DLKD-LEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASReeilaQAKENEkkL 1678
Cdd:COG3096 963 VVQRRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR-----DAKQQT--L 1035
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1679 KSMEAEMIQLqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1736
Cdd:COG3096 1036 QELEQELEEL--GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
840-1460 |
7.81e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 840 LLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEqlqaetelcaeaeelrarLTAKKQELEEI 919
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQS------------------LCKELDILQRE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 920 CHDLEARVEEEEERCQHLQAEKKKMQqniqeleeqLEEEESARQKLQLEKVTTEAKLKKLEEEqiiledqncKLAKEKKL 999
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQE---------LQQRYAELCAAAITCTAQCEKLEKIHLQ---------ESAQSLKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1000 LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKqrqelektrrklegdstdlsdqiaelqaqiaelKM 1079
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNP---------------------------------AR 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1080 QLAKKEEELQAALARVEEEAAQKNMALKKIR----ELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTL 1155
Cdd:TIGR00618 518 QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1156 DSTAAQQELRSKREQEVNILKKTLEeeaktHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEnergelane 1235
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQ-----PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH--------- 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1236 vkvLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQD 1315
Cdd:TIGR00618 664 ---ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDA 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1316 TQELLQEENRQKlslSTKLK-QVEDEKNSFREQLEEEEeakhnLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQ 1394
Cdd:TIGR00618 741 LNQSLKELMHQA---RTVLKaRTEAHFNNNEEVTAALQ-----TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1395 KDLEGLSQRHEEKVAAydKLEKTKTRLQQELDDLLVDLDHQRQsacnLEKKQKKFDQLLAEEKTIS 1460
Cdd:TIGR00618 813 PSDEDILNLQCETLVQ--EEEQFLSRLEEKSATLGEITHQLLK----YEECSKQLAQLTQEQAKII 872
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1453-1602 |
8.02e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1453 LAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEdlmsskddvgksvhELEKSKRA 1532
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQ--------------KLEKRLLQ 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1533 LEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ--------SEEKKKQLVRQVREmEAELE 1602
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEILLEKVEE-EARHE 170
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
872-1596 |
8.93e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.95 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 872 TEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEIchdlearveEEEERCQHLQAEKKKMQQniQE 950
Cdd:PRK10246 198 TELEKLQAQASGVALLTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSL---------NWLTRLDELQQEASRRQQ--AL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 951 LEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQiilEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEA 1030
Cdd:PRK10246 267 QQALAAEEKAQPQLAALSLAQPARQLRPHWERI---QEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1031 MITDLEERLRREEKQR---QELEKTRRKLEGDSTDlSDQIAELQAQIAELKMQLAKKEEelqAALARVEEEAAQKNMALK 1107
Cdd:PRK10246 344 QQQSLNTWLAEHDRFRqwnNELAGWRAQFSQQTSD-REQLRQWQQQLTHAEQKLNALPA---ITLTLTADEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1108 KIRELESQISELQEDLeserasrnkAEKQKRdlgeelealKTELEDTLDSTAAQQELRskreqevnilkktleeeakthE 1187
Cdd:PRK10246 420 EQRPLRQRLVALHGQI---------VPQQKR---------LAQLQVAIQNVTQEQTQR---------------------N 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1188 AQIQEMRQKHSQAVEELAeqleqtkRVKA--NLEKAKQTLENERGELANEVKVLLQGKgdSEHKrkkVEAQLQELQVKFN 1265
Cdd:PRK10246 461 AALNEMRQRYKEKTQQLA-------DVKTicEQEARIKDLEAQRAQLQAGQPCPLCGS--TSHP---AVEAYQALEPGVN 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1266 EgeRVRTELADKVTKLQVEldnVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVED-----E 1340
Cdd:PRK10246 529 Q--SRLDALEKEVKKLGEE---GAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDiqpwlD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1341 KNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETaeevkrklQKDLEGLSQRHEEKVAAYDKLEKTKTR 1420
Cdd:PRK10246 604 AQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLT--------ALAGYALTLPQEDEEASWLATRQQEAQ 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1421 LQQelddllvdldhQRQSacNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEA---REKETKALSLARALEEAMEQKA- 1496
Cdd:PRK10246 676 SWQ-----------QRQN--ELTALQNRIQQLTPLLETLPQSDDLPHSEETVALdnwRQVHEQCLSLHSQLQTLQQQDVl 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1497 ELERLNK---QFRTEMED---------LMSSKDDvgKSVHELEKSKRALEQQVEEMKTQLEELEDELQAtedaklrlevN 1564
Cdd:PRK10246 743 EAQRLQKaqaQFDTALQAsvfddqqafLAALLDE--ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQ----------H 810
|
730 740 750
....*....|....*....|....*....|..
gi 972988096 1565 LQAMKAQFerDLQGRDEQSEEKKKQLVRQVRE 1596
Cdd:PRK10246 811 QQHRPDGL--DLTVTVEQIQQELAQLAQQLRE 840
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1623-1926 |
9.33e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1623 KDLEAHIDSANKNRDeaikqlrkLQAQMKDCMRELDDTRASREEILAQAKENEkklksmeaemiQLQEELAAAERAKRQA 1702
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETE-----------QLKQQLAQAPAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1703 QQERDELADEiANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANLQIDQINTDL-----NLERSHAQ 1777
Cdd:PRK11281 100 QAELEALKDD-NDEETRETLSTLSLRQLESRLAQ--------------TLDQLQNAQNDLAEYNSQLvslqtQPERAQAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1778 KNENAR--QQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNET-------KERQAACKQVRRTEKKLK 1848
Cdd:PRK11281 165 LYANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlqdllqKQRDYLTARIQRLEHQLQ 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1849 dvLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANasrRKLQRELEDATETADAMNREVSSLKNKLRR 1926
Cdd:PRK11281 245 --LLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEIN---LQLSQRLLKATEKLNTLTQQNLRVKNWLDR 317
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1029-1284 |
9.53e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1029 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1108
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1109 IRELESQISELQEdlesERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQEL--RSKR-EQEVNILKKTLEEEAKT 1185
Cdd:COG1340 87 LNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1186 HE--AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLE--NERGELANEVKVLLQGKGDSEHKrkkveaQLQELQ 1261
Cdd:COG1340 163 KElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADelRKEADELHKEIVEAQEKADELHE------EIIELQ 236
|
250 260
....*....|....*....|...
gi 972988096 1262 VKFNEGERVRTELADKVTKLQVE 1284
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKRE 259
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1107-1925 |
9.58e-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: 50.82 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1107 KKIRELESQISELQEDLESERASRNKAEKQKRDLGE---ELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEA 1183
Cdd:TIGR00606 217 EKACEIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVF 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1184 KTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL-LQGKGDSEHKRKKvEAQLQELQV 1262
Cdd:TIGR00606 297 QGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqLQADRHQEHIRAR-DSLIQSLAT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1263 kfnegeRVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTkdfSALESQLQDTQELLQEEnrqklslstkLKQVEDEKN 1342
Cdd:TIGR00606 376 ------RLELDGFERGPFSERQIKNFHTLVIERQEDEAKTA---AQLCADLQSKERLKQEQ----------ADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1343 SFREQLEEEeeaKHNLEKQIAtlhaQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQrhEEKVAAYDKLEKTKTRLQ 1422
Cdd:TIGR00606 437 GLGRTIELK---KEILEKKQE----ELKFVIKELQQLEGSSDRILELDQELRKAERELSK--AEKNSLTETLKKEVKSLQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1423 QELDdllvdldhqrqsacNLEKKQKKFDQLLAEEKtisakyaeerdraeaEAREKETKALSLARALEEAMEQKAELERLN 1502
Cdd:TIGR00606 508 NEKA--------------DLDRKLRKLDQEMEQLN---------------HHTTTRTQMEMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1503 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ 1582
Cdd:TIGR00606 559 SDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1583 SEekkkqlvrqVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRA 1662
Cdd:TIGR00606 639 SD---------LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1663 SREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalalEEKRRLEARIAQLEEELE 1742
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ----------RLKNDIEEQETLLGTIMP 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1743 EEQGNTELINDrlkKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKskykasitaleaKIAQL 1822
Cdd:TIGR00606 780 EEESAKVCLTD---VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD------------TVVSK 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1823 EEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRE 1902
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE 924
|
810 820
....*....|....*....|....*..
gi 972988096 1903 LEDATETADAMNR----EVSSLKNKLR 1925
Cdd:TIGR00606 925 KEELISSKETSNKkaqdKVNDIKEKVK 951
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1525-1686 |
9.77e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1525 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDlqgrdeqseEKKKQLVRQVREMEA---EL 1601
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---------EEQLGNVRNNKEYEAlqkEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1602 EDERKQRSmavaarkklemdlkDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSM 1681
Cdd:COG1579 99 ESLKRRIS--------------DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*
gi 972988096 1682 EAEMI 1686
Cdd:COG1579 165 REELA 169
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1621-1715 |
9.84e-06 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 50.07 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1621 DLKDLEAHIDS-----ANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEI---LAQAKENEKKLKSMEAEMIQLQEEL 1692
Cdd:PRK05431 3 DIKLIRENPEAvkealAKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEI 82
|
90 100
....*....|....*....|...
gi 972988096 1693 AAAERAKRQAQQERDELADEIAN 1715
Cdd:PRK05431 83 KALEAELDELEAELEELLLRIPN 105
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
975-1924 |
1.02e-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: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 975 KLKKLEEEQIILEDQNCKLAKEKklLEDRIAEFTTNLTEE--EEKSKSLAKLKNKHEamitDLEERLRREEKQRQELEKT 1052
Cdd:TIGR01612 711 KIQNMETATVELHLSNIENKKNE--LLDIIVEIKKHIHGEinKDLNKILEDFKNKEK----ELSNKINDYAKEKDELNKY 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1053 RRKLEGDSTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVEEEAAQ-----KNMA---LKKIRELESQISELQEDLE 1124
Cdd:TIGR01612 785 KSKISEIKNHYNDQINIDNIKDEDAK-QNYDKSKEYIKTISIKEDEIFKiinemKFMKddfLNKVDKFINFENNCKEKID 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1125 SERAS----RNKAEKQKRDlgEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE--EEAKTHEAQIQEMRQKHS 1198
Cdd:TIGR01612 864 SEHEQfaelTNKIKAEISD--DKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEyiKICENTKESIEKFHNKQN 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1199 QAVEELAEQLEQTKRV----KANLEKAKQTLENERGELANEVKVLlqGKGDSEHKRKKVEAQLQELQV------------ 1262
Cdd:TIGR01612 942 ILKEILNKNIDTIKESnlieKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAKNNELIKYFNDLKAnlgknkenmlyh 1019
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1263 KFNEGERVRTELADKVTKLQVELDNV-----TGLLSQSDSKSSKLTKDFSALESQLQDTQELLQ---EENRQKLSLSTKL 1334
Cdd:TIGR01612 1020 QFDEKEKATNDIEQKIEDANKNIPNIeiaihTSIYNIIDEIEKEIGKNIELLNKEILEEAEINItnfNEIKEKLKHYNFD 1099
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1335 KQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETA----EEVKRKL--QKDLEGLSQRHEEKV 1408
Cdd:TIGR01612 1100 DFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQindlEDVADKAisNDDPEEIEKKIENIV 1179
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1409 AAYDK-----------------LEKTKTRLQ------------------QELDDLLVDLDHQRQSacnLEKKQKKFDQLL 1453
Cdd:TIGR01612 1180 TKIDKkkniydeikkllneiaeIEKDKTSLEevkginlsygknlgklflEKIDEEKKKSEHMIKA---MEAYIEDLDEIK 1256
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1454 AEEKTISAKYAEERD-RAEAEA--------------REKETKALSLAR----ALEEAMEQKAELERLNKQFRTEMEDLMS 1514
Cdd:TIGR01612 1257 EKSPEIENEMGIEMDiKAEMETfnishdddkdhhiiSKKHDENISDIRekslKIIEDFSEESDINDIKKELQKNLLDAQK 1336
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1515 SKDDVGKSVHE---------LEKSKRALEQqVEEMKTQLEE----LEDELQATED--AKLRLEVNLQAMKAQFERDLQGR 1579
Cdd:TIGR01612 1337 HNSDINLYLNEianiynilkLNKIKKIIDE-VKEYTKEIEEnnknIKDELDKSEKliKKIKDDINLEECKSKIESTLDDK 1415
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1580 D-EQSEEKKKQLVRQVREMEA-----------------------ELEDERKQRSMAVA---ARKKLEMDLKDLEAHIDSA 1632
Cdd:TIGR01612 1416 DiDECIKKIKELKNHILSEESnidtyfknadennenvlllfkniEMADNKSQHILKIKkdnATNDHDFNINELKEHIDKS 1495
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1633 NKNRDEAIKQLRKLQA------QMKDCMREL-------------DDTRASREEILAQAKE-----------NEKKLKSME 1682
Cdd:TIGR01612 1496 KGCKDEADKNAKAIEKnkelfeQYKKDVTELlnkysalaiknkfAKTKKDSEIIIKEIKDahkkfileaekSEQKIKEIK 1575
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1683 AEMIQLQEELAAAERAKRQA---QQERDELAD---EIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIN---- 1752
Cdd:TIGR01612 1576 KEKFRIEDDAAKNDKSNKAAidiQLSLENFENkflKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDNlnsl 1655
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1753 ----DRLKKANLQIDQINTDLNLERSHAQKNENARQQlERQNKELKV--KLQEMEGTVKSKYKASITALEAKIAQLEEQL 1826
Cdd:TIGR01612 1656 qeflESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQ-HKKNYEIGIieKIKEIAIANKEEIESIKELIEPTIENLISSF 1734
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1827 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA 1906
Cdd:TIGR01612 1735 NTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKKSKSYLDDI 1814
|
1130
....*....|....*...
gi 972988096 1907 teTADAMNREVSSLKNKL 1924
Cdd:TIGR01612 1815 --EAKEFDRIINHFKKKL 1830
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1201-1614 |
1.06e-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: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1201 VEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTK 1280
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1281 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEenrqklslstklkqVEDEKNSFREQLEEEEEAKHNLEK 1360
Cdd:pfam19220 116 KTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQR--------------AEGELATARERLALLEQENRRLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1361 QIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDkLEKTKTRLQQELDDLLVDLDHQRQSAC 1440
Cdd:pfam19220 182 LSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLE-EAVEAHRAERASLRMKLEALTARAAAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1441 nlekkqkkfDQLLAEEKTisakyaEERDRAEAeAREKEtkalslaRALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVG 1520
Cdd:pfam19220 261 ---------EQLLAEARN------QLRDRDEA-IRAAE-------RRLKEASIERDTLERRLAGLEADLERRTQQFQEMQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1521 KSVHELEKSKRALEQQVEEMKTQLEELEDELQatedaklrlevNLQAMKAQFERDLqgrdeqsEEKKKQLVRQVREMEAE 1600
Cdd:pfam19220 318 RARAELEERAEMLTKALAAKDAALERAEERIA-----------SLSDRIAELTKRF-------EVERAALEQANRRLKEE 379
|
410
....*....|....
gi 972988096 1601 LEDERKQRSMAVAA 1614
Cdd:pfam19220 380 LQRERAERALAQGA 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
862-1236 |
1.20e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 862 EKQLA-AENRLTEMETLQSQLM--AEKLQLQEQLQAE--TELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQH 936
Cdd:COG4913 344 EREIErLERELEERERRRARLEalLAALGLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 937 LQAEKKKMQQNIQELEEQLEEEESA-RQKLQLekvtTEAKLK--------KLEEEQ---------------IILEDQNCK 992
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRDAlAEALGL----DEAELPfvgelievRPEEERwrgaiervlggfaltLLVPPEHYA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 993 LAKE--------KKLLEDRIAEFTTNLTEEEEKSKSLA-KLKNK-HEA--------------MITDLEERLRRE------ 1042
Cdd:COG4913 500 AALRwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAgKLDFKpHPFrawleaelgrrfdyVCVDSPEELRRHpraitr 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1043 -----------EKQRQELEKTRRKLEGDSTD----LSDQIAELQAQIAELKMQLAKKEEELQA--ALARVEEEAAQKNMA 1105
Cdd:COG4913 580 agqvkgngtrhEKDDRRRIRSRYVLGFDNRAklaaLEAELAELEEELAEAEERLEALEAELDAlqERREALQRLAEYSWD 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1106 LKKIRELESQISELQEDLESERASRNKAEKqkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1185
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1186 HEAQIQEMRQKHSQAVEELAEQL---EQTKRVKANLEKAKQTLENERGELANEV 1236
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
862-1134 |
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 972988096 862 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 940
Cdd:pfam19220 124 ERQLAAETEQNRALEEENKALREEAQAAEKALQRAEgELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 941 KKKMQQNIQELEEQLEEEESARQKL------QLEKVTTE--AKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTtnlt 1012
Cdd:pfam19220 204 LDATRARLRALEGQLAAEQAERERAeaqleeAVEAHRAEraSLRMKLEALTARAAATEQLLAEARNQLRDRDEAIR---- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1013 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAL 1092
Cdd:pfam19220 280 AAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELT 359
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 972988096 1093 ARVEEEAAqknmalkkirELESQISELQEDLESERASRNKAE 1134
Cdd:pfam19220 360 KRFEVERA----------ALEQANRRLKEELQRERAERALAQ 391
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1059-1170 |
1.24e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1059 DSTDLSDQIAELQAQIAELKMQLAKKE---------EELQAALARVEEEAAQKNMALKKIRELESQ--ISelQEDLESER 1127
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVS--QQELDEAR 154
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 972988096 1128 ASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ 1170
Cdd:COG1566 155 AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAA 197
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1000-1718 |
1.46e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1000 LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITD---LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAE 1076
Cdd:PRK04863 518 LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1077 LKmQLAKKEEELQAALARVEEeaaQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALkteledTLD 1156
Cdd:PRK04863 598 LA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL------SQP 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1157 STAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHS-QAVeelaeqleqtkrVKANLEKAKQTLENERGELanE 1235
Cdd:PRK04863 668 GGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALYGPArHAI------------VVPDLSDAAEQLAGLEDCP--E 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1236 VKVLLQGKGDS-EHKRKKVEAQLQELQVKFNE--------------GERVRTELADkvtKLQVELDNVTGLLSQSDSKSS 1300
Cdd:PRK04863 734 DLYLIEGDPDSfDDSVFSVEELEKAVVVKIADrqwrysrfpevplfGRAAREKRIE---QLRAEREELAERYATLSFDVQ 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1301 KLTKDFSALESQL---------QDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEeeeeakhNLEKQIATLhaqvad 1371
Cdd:PRK04863 811 KLQRLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLE-------QAKEGLSAL------ 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1372 mkKKMEDSVGCLetaeevkrklqkDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLdhqrQSACNLEKKQKKFDQ 1451
Cdd:PRK04863 878 --NRLLPRLNLL------------ADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLE----PIVSVLQSDPEQFEQ 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1452 LlaeektisakyaeERDRAEAEAREKETKAlsLARALEEAMEQKAELERLNKQFRTEMEDLMSSKddvgksvheLEKSKR 1531
Cdd:PRK04863 940 L-------------KQDYQQAQQTQRDAKQ--QAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEK---------LRQRLE 995
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1532 ALEQQVEEMKTQLEELEDelQATEDAKLrlevnLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMA 1611
Cdd:PRK04863 996 QAEQERTRAREQLRQAQA--QLAQYNQV-----LASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDELHAR 1068
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1612 VAA----RKKLEMDLKDLEAHIDSANknrdeaiKQLRKLQAQMKDCMRELDDTRASREEILAQAKEN--EKKLKSMEAEM 1685
Cdd:PRK04863 1069 LSAnrsrRNQLEKQLTFCEAEMDNLT-------KKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERRLHRRELAY 1141
|
730 740 750
....*....|....*....|....*....|....*.
gi 972988096 1686 IQLQEELAAAERAK---RQAQQERDELADEIANSSG 1718
Cdd:PRK04863 1142 LSADELRSMSDKALgalRLAVADNEHLRDVLRLSED 1177
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1525-1709 |
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 972988096 1525 ELEKSKRALEQQVEEMKTQLEELEDELQA----------TEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVR 1592
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQqlSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1593 QVREMEAELEDE-----RKQRSMAVAARKKLEM-------DLKDLEAHIDSANKNRDEAIKQ-LRKLQAQMkdcmRELDD 1659
Cdd:COG3206 252 GPDALPELLQSPviqqlRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRiLASLEAEL----EALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 972988096 1660 TRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL 1709
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1443-1925 |
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 972988096 1443 EKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKEtkalslaraleeamEQKAELERLNKQFRTEmedlmssKDDVGKS 1522
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQE--------------ERQETSAELNQLLRTL-------DDQWKEK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1523 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELE 1602
Cdd:pfam12128 303 RDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSEL----ENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1603 DERKQRSMAVAArkKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMrelddtrasrEEILAQAKENEKKLKSME 1682
Cdd:pfam12128 379 RRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL----------EAGKLEFNEEEYRLKSRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1683 AEMIQLQEELAAAERAKRQ--AQQERDELADEIANSSGKGALALE-EKRRLEARIAQLEEELEEEQGNTELINDRLKKAN 1759
Cdd:pfam12128 447 GELKLRLNQATATPELLLQleNFDERIERAREEQEAANAEVERLQsELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1760 LQID-QINTDLNLERSHAQKNEN------ARQQLERQNKE----------------LKVKLQEMEgtvKSKYKASITALE 1816
Cdd:pfam12128 527 LQLFpQAGTLLHFLRKEAPDWEQsigkviSPELLHRTDLDpevwdgsvggelnlygVKLDLKRID---VPEWAASEEELR 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1817 AKIAQLEEQLDNETKERQAACKQVRRTEKKLkdvllqvdderrnaeqykdqaDKASTRLKQLKRQLEEAEEEAQRANASR 1896
Cdd:pfam12128 604 ERLDKAEEALQSAREKQAAAEEQLVQANGEL---------------------EKASREETFARTALKNARLDLRRLFDEK 662
|
490 500 510
....*....|....*....|....*....|
gi 972988096 1897 RKLQRELEDATETA-DAMNREVSSLKNKLR 1925
Cdd:pfam12128 663 QSEKDKKNKALAERkDSANERLNSLEAQLK 692
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1187-1395 |
2.03e-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: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1187 EAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnevkvllqgkgDSEHKRKKVEAQLQELQVKFNE 1266
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1267 GervRTELADKVTKLQVELDNVTGLLSQSDSKS-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1345
Cdd:COG3883 84 R---REELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 972988096 1346 EQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQK 1395
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1086-1266 |
2.29e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1086 EELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldstaaqQELR 1165
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-------EARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1166 SKREQEVNILKKTLEEEAKTHEAQIQEMRQkhSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGD 1245
Cdd:COG1579 76 KKYEEQLGNVRNNKEYEALQKEIESLKRRI--SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|.
gi 972988096 1246 SEHKRKKVEAQLQELQVKFNE 1266
Cdd:COG1579 154 LEAELEELEAEREELAAKIPP 174
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1446-1756 |
2.32e-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: 48.91 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1446 QKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLN---KQFRTEMEDLMSSKDDVGKS 1522
Cdd:pfam19220 54 EALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1523 VHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFER------DLQGRDEQSEEKKKQLVRQVRE 1596
Cdd:pfam19220 134 NRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEqaaelaELTRRLAELETQLDATRARLRA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1597 MEAELEDERKQRSMAVAA-----------RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRe 1665
Cdd:pfam19220 214 LEGQLAAEQAERERAEAQleeaveahraeRASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIER- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1666 eilaqaKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQ 1745
Cdd:pfam19220 293 ------DTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVER 366
|
330
....*....|.
gi 972988096 1746 GNTELINDRLK 1756
Cdd:pfam19220 367 AALEQANRRLK 377
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1494-1923 |
2.50e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1494 QKAELERLNKQFRTEMEDLMSSKD---DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKA 1570
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKelkNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1571 QFERDLQGRDEQSEEKKKqlvrqvreMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQM 1650
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNK--------LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1651 KDCMRELDDTRASR---EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEK 1727
Cdd:TIGR04523 183 LNIQKNIDKIKNKLlklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1728 RRLEARIAQLeeeleeeQGNTELINDRLKKANLQIDQINTDLnlERSHAQKNENARQQLERQNKELKVKLQEMEGTVkSK 1807
Cdd:TIGR04523 263 NKIKKQLSEK-------QKELEQNNKKIKELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI-SQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1808 YKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVL--------------LQVDDERRNAEQYKDQADKAST 1873
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenqsykqeiknleSQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 972988096 1874 RLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLKNK 1923
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1181-1910 |
2.72e-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: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1181 EEAKTHEAQIQEMRQKHSQAVEELAE---QLEQTKRVKANLEKAKQTLENERgELANEVKVLLQGKGDSEHKRKKVEAQL 1257
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEeqyRLVEMARELEELSARESDLEQDY-QAASDHLNLVQTALRQQEKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1258 QELQVKFNEGERVRTELADKVTKLQVELDNVTgllSQSDSKSSKLTKDFSALESQ-------------LQDTQELLQEEN 1324
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAE---EEVDSLKSQLADYQQALDVQqtraiqyqqavqaLEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1325 ---------------------RQKLSLSTKLKQVEDEKNSF-----------------------REQLEEEEEAKHNLEk 1360
Cdd:COG3096 434 ltpenaedylaafrakeqqatEEVLELEQKLSVADAARRQFekayelvckiageversqawqtaRELLRRYRSQQALAQ- 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1361 QIATLHAQVADmkkkmedsvgcLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSAC 1440
Cdd:COG3096 513 RLQQLRAQLAE-----------LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1441 NLEKKQkkfDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLA--RALEEAMEQKAELERLNKQfrtemedlmsSKDd 1518
Cdd:COG3096 582 ELRQQL---EQLRARIKELAARAPAWLAAQDALERLREQSGEALAdsQEVTAAMQQLLEREREATV----------ERD- 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1519 vgksvhELEKSKRALEQQVEEMK-------TQLEELEDELQAT-----------EDA--------KLR---LEVNLQAMK 1569
Cdd:COG3096 648 ------ELAARKQALESQIERLSqpggaedPRLLALAERLGGVllseiyddvtlEDApyfsalygPARhaiVVPDLSAVK 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1570 AQF-------------ERDLQGRDEQS----EEKKKQLV----RQVR--------------------EMEAELEDERKQR 1608
Cdd:COG3096 722 EQLagledcpedlyliEGDPDSFDDSVfdaeELEDAVVVklsdRQWRysrfpevplfgraarekrleELRAERDELAEQY 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1609 SMAVAARKKLEMDLKDLEA----HIDSA-NKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1683
Cdd:COG3096 802 AKASFDVQKLQRLHQAFSQfvggHLAVAfAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLP 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1684 EMIQLQEElAAAERAkRQAQQERDElADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQID 1763
Cdd:COG3096 882 QANLLADE-TLADRL-EELREELDA-AQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIF 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1764 QInTDLnLERSHAQKNENARQQLERQ---NKELKVKLQEMEgTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQV 1840
Cdd:COG3096 959 AL-SEV-VQRRPHFSYEDAVGLLGENsdlNEKLRARLEQAE-EARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTL 1035
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1841 RRTEKKLKDVLLQVDDE-----RRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETA 1910
Cdd:COG3096 1036 QELEQELEELGVQADAEaeeraRIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1465-1721 |
3.09e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 49.22 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1465 EERDRAEAEareketKALSLAR-ALEEAMEQKA---ELERLNKQFRTEMEDLMsskddvgksvhelekskRALEQQVEEM 1540
Cdd:pfam13779 480 EDGDLSDAE------RRLRAAQeRLSEALERGAsdeEIAKLMQELREALDDYM-----------------QALAEQAQQN 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1541 KTQLEELEDELQATEDAKlrlevNLQAMKAQFERDLQ-GRDEQSEekkkQLVRQVREMEAELEDERKQRSMAVAARKKLE 1619
Cdd:pfam13779 537 PQDLQQPDDPNAQEMTQQ-----DLQRMLDRIEELARsGRRAEAQ----QMLSQLQQMLENLQAGQPQQQQQQGQSEMQQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1620 MdLKDLEAHIDSANKNRDEAIKQLRKLQAQmkdcmrelDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK 1699
Cdd:pfam13779 608 A-MDELGDLLREQQQLLDETFRQLQQQGGQ--------QQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAE 678
|
250 260
....*....|....*....|....
gi 972988096 1700 RQAQ--QERDELADEIANSSGKGA 1721
Cdd:pfam13779 679 RQQAlrRRLEELQDELKELGGKEP 702
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1022-1156 |
3.17e-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: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1022 AKLKNKHEAM---ITDLEERLRREEKQRQELEKtrrklegdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1098
Cdd:COG0542 400 ARVRMEIDSKpeeLDELERRLEQLEIEKEALKK-------------EQDEASFERLAELRDELAELEEELEALKARWEAE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1099 aaqknmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLD 1156
Cdd:COG0542 467 -----------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1465-1707 |
3.36e-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: 47.33 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1465 EERDRAEAEAREKETKalsLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTql 1544
Cdd:pfam00261 8 EELDEAEERLKEAMKK---LEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1545 eeLEDELQATEDAKLRLEVNLQAMKaqferdlqGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDL-- 1622
Cdd:pfam00261 83 --LENRALKDEEKMEILEAQLKEAK--------EIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELkv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1623 -----KDLEAHIDSANKNRDEAIKQLRKLQAQMKdcmrelddtrasreEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1697
Cdd:pfam00261 153 vgnnlKSLEASEEKASEREDKYEEQIRFLTEKLK--------------EAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|
gi 972988096 1698 AKRQAQQERD 1707
Cdd:pfam00261 219 KYKAISEELD 228
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1036-1215 |
3.65e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.33 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1036 EERLRREEKQRQ-ELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlAKKEEELQAALARVEEEAAQKNMalkkirELES 1114
Cdd:COG2268 211 ETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEERRE-AETARAEAEAAYEIAEANAEREV------QRQL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1115 QISELQEDLESERASRNKAEKQ-KRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVniLKKTLEEEAKTHEAQIQEM 1193
Cdd:COG2268 284 EIAEREREIELQEKEAEREEAElEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG--KRALAEAWNKLGDAAILLM 361
|
170 180
....*....|....*....|...
gi 972988096 1194 R-QKHSQAVEELAEQLEQTKRVK 1215
Cdd:COG2268 362 LiEKLPEIAEAAAKPLEKIDKIT 384
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1091-1300 |
3.74e-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: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1091 ALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKR-- 1168
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1169 -----EQEVNILKKTLE----EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1239
Cdd:COG3883 94 alyrsGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1240 LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSS 1300
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
998-1233 |
4.03e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 998 KLLEDRIAEFTtnlteeeEKSKSLAKLKNKHEAMITDLEERLRREEKQRQEL-EKTRRklegdstDLSDQIAELQAQIAE 1076
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIE-------DLRRQLDTLTVERAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1077 LKMQLAKKEEELQAALARVEEEAAQKnmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELED--- 1153
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1154 -------------------TLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAV----EELAE---- 1206
Cdd:pfam00038 146 elqaqvsdtqvnvemdaarKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALrsakEEITElrrt 225
|
250 260 270
....*....|....*....|....*....|...
gi 972988096 1207 ------QLEQTKRVKANLEKAKQTLEnERGELA 1233
Cdd:pfam00038 226 iqsleiELQSLKKQKASLERQLAETE-ERYELQ 257
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
653-677 |
4.33e-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: 4.33e-05
10 20
....*....|....*....|....*
gi 972988096 653 YKEQLAKLMATLRNTNPNFVRCIIP 677
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1059-1243 |
5.40e-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: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1059 DSTDLSDQIAELQAQIAelkmqlakkeeELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEkqkr 1138
Cdd:pfam00529 52 DPTDYQAALDSAEAQLA-----------KAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQ---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1139 dlgEELEALKTELEDTlDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK-RVKAN 1217
Cdd:pfam00529 117 ---AQLAQAQIDLARR-RVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELsGAQLQ 192
|
170 180
....*....|....*....|....*..
gi 972988096 1218 LEKAKQTLENERGELAN-EVKVLLQGK 1243
Cdd:pfam00529 193 IAEAEAELKLAKLDLERtEIRAPVDGT 219
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1441-1793 |
6.00e-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: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1441 NLEKKQKKFDQLLAEEKTISA---KYAEERDRAEAEAREKEtkALSLARALEEAMEQKAElERLNKqfrteMEDLMSSKD 1517
Cdd:COG3096 276 HANERRELSERALELRRELFGarrQLAEEQYRLVEMARELE--ELSARESDLEQDYQAAS-DHLNL-----VQTALRQQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1518 DVGKSVHELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQ------------- 1577
Cdd:COG3096 348 KIERYQEDLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQTRAIQyqqavqalekara 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1578 -------------GRDEQSEEKKKQLVRQVREMEAEL---EDERKQ----------------RSMAVAARKKLEMDLKDL 1625
Cdd:COG3096 428 lcglpdltpenaeDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQfekayelvckiageveRSQAWQTARELLRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1626 EAHIDSANKNRDEaIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQE 1705
Cdd:COG3096 508 QALAQRLQQLRAQ-LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1706 RDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKanlqidqiNTDLNLERSHAQKnenARQQ 1785
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER--------EREATVERDELAA---RKQA 655
|
....*...
gi 972988096 1786 LERQNKEL 1793
Cdd:COG3096 656 LESQIERL 663
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1384-1667 |
7.76e-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: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1384 ETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTR----LQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLA--EEK 1457
Cdd:pfam05667 215 ELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRiaeqLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTtdTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1458 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQK--AELERLNKQFrtemEDLMSSKDDVGKSVHELEKSKRALEQ 1535
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQreEELEELQEQL----EDLESSIQELEKEIKKLESSIKQVEE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1536 QVEEMKTQLEELEDELQATE-------DAKLRLEvNLQAMKAQFERDLQGRDEQSEEKKKQLV---RQVREMEAELEDER 1605
Cdd:pfam05667 371 ELEELKEQNEELEKQYKVKKktldllpDAEENIA-KLQALVDASAQRLVELAGQWEKHRVPLIeeyRALKEAKSNKEDES 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1606 KQ------------RSMAVAARKKLEMdLKDLEAHIDSANK--NRD-------EAIKQLRKlqaQMKDCMRELDDTRASR 1664
Cdd:pfam05667 450 QRkleeikelrekiKEVAEEAKQKEEL-YKQLVAEYERLPKdvSRSaytrrilEIVKNIKK---QKEEITKILSDTKSLQ 525
|
...
gi 972988096 1665 EEI 1667
Cdd:pfam05667 526 KEI 528
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1469-1877 |
7.79e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1469 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 1524
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDleqdyqaasdhlnlvqtalrqqekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1525 ELEKSKRALEQQ---VEEMKTQLEELEDELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1590
Cdd:COG3096 355 DLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQTRAIQYQQAvQALEKARALcglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1591 -VRQVREMEAELEDERKQRSMAV-AARKKLEMDlkdleahiDSANKNRDEAIKQLRKLQAQMkdcmrELDDTRASREEIL 1668
Cdd:COG3096 435 tPENAEDYLAAFRAKEQQATEEVlELEQKLSVA--------DAARRQFEKAYELVCKIAGEV-----ERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1669 AQAKEnekkLKSMEAEMIQLQEELAAAERAKRQaQQERDELADEIANSSGK---GALALEE-KRRLEARIAqleeeleee 1744
Cdd:COG3096 502 RRYRS----QQALAQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQqldAAEELEElLAELEAQLE--------- 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1745 qgntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKVKLQEMEgtvkSKYKASITALEAkIAQLEE 1824
Cdd:COG3096 568 -----------------------ELEEQAAEAVEQ---RSELRQQLEQLRARIKELA----ARAPAWLAAQDA-LERLRE 616
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 972988096 1825 QLDNETKERQAACKQVRRTEKKLKdvllQVDDERRNAEQYKDQADKASTRLKQ 1877
Cdd:COG3096 617 QSGEALADSQEVTAAMQQLLERER----EATVERDELAARKQALESQIERLSQ 665
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1483-1590 |
7.95e-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: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1483 SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE 1562
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90 100
....*....|....*....|....*...
gi 972988096 1563 VNLQAMKAQFERDLQGRDEQSEEKKKQL 1590
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRDREIEKLKERL 149
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1442-1601 |
8.66e-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: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1442 LEKKQKKFDQLLAEEKTISAKYAE---ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD- 1517
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAEledELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1518 -DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVRE 1596
Cdd:COG1579 92 eALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
....*
gi 972988096 1597 MEAEL 1601
Cdd:COG1579 172 IPPEL 176
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1581-1736 |
9.08e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.97 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1581 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQ-----LRKLQAQMKDCMR 1655
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgredlAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1656 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSSGKGALALEEkrRLEARIA 1735
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL-KARAKAAKAQEKVNEALSGIDSDDATSALE--RMEEKIE 175
|
.
gi 972988096 1736 Q 1736
Cdd:COG1842 176 E 176
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1054-1342 |
1.05e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.54 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1054 RKLEGDSTDlsdqIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKnmaLKKirELESQISE------LQEDLESER 1127
Cdd:PLN03229 422 KKREAVKTP----VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LKK--EIDLEYTEaviamgLQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1128 ASRNKAEKQK----RDLGEELEALKTELEDTLDSTAAQQELRSKRE--QEVNILKKTLEEEAKTHEAQiQEMRQKhSQAV 1201
Cdd:PLN03229 493 EEFSKANSQDqlmhPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKK-FKEV 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1202 EELAEQLEQTKRVKANLEKA------------KQTLENERGELANEVKVLLQGKG-DSEHKRKKveaQLQELQVKFNEGE 1268
Cdd:PLN03229 571 MDRPEIKEKMEALKAEVASSgassgdeldddlKEKVEKMKKEIELELAGVLKSMGlEVIGVTKK---NKDTAEQTPPPNL 647
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1269 RVRTE-LADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSL---STKLKQVEDEKN 1342
Cdd:PLN03229 648 QEKIEsLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEalnSSELKEKFEELE 725
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1467-1732 |
1.06e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.23 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1467 RDRAEAEAREKETKALSLARALEEAMEQkaeLERLNKQFRTEMEDLMS-SKDDVGKSVHELEKSKRALEQQVEEMKTQLE 1545
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEALDK---LRSYLPKLNPLREEKKKvSVKSLEELIKDVEEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1546 ELEDELQATEDAKLRLEVnLQAMKAQFERDLQGR---------DEQSEEKKKQLVRQVremEAELEDERKQRSMAVAArk 1616
Cdd:PRK05771 111 ELENEIKELEQEIERLEP-WGNFDLDLSLLLGFKyvsvfvgtvPEDKLEELKLESDVE---NVEYISTDKGYVYVVVV-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1617 klemdlkdleahidSANKNRDEAIKQLRKLQAQMKdcmrELDDTRASREEIlaqaKENEKKLKSMEAEMIQLQEELAAae 1696
Cdd:PRK05771 185 --------------VLKELSDEVEEELKKLGFERL----ELEEEGTPSELI----REIKEELEEIEKERESLLEELKE-- 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 972988096 1697 rakrqaqqERDELADEIANSSGkgaLALEEKRRLEA 1732
Cdd:PRK05771 241 --------LAKKYLEELLALYE---YLEIELERAEA 265
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1078-1224 |
1.11e-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: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1078 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEdleserasrnkaekQKRDLGEELEALK---TELEDT 1154
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA--------------EVEELEAELEEKDeriERLERE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1155 LDSTAAQQELRSKREQEVNIlkktLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKANLEKAKQT 1224
Cdd:COG2433 450 LSEARSEERREIRKDREISR----LDREIERLERELEEERER----IEELKRKLERLKELWKLEHSGELV 511
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
992-1154 |
1.15e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 992 KLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ 1071
Cdd:PHA02562 196 QIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1072 --------------------------AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLES 1125
Cdd:PHA02562 276 kvikmyekggvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT 355
|
170 180 190
....*....|....*....|....*....|....*.
gi 972988096 1126 ERASRNKAEK-------QKRDLGEELEALKTELEDT 1154
Cdd:PHA02562 356 LVDKAKKVKAaieelqaEFVDNAEELAKLQDELDKI 391
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1390-1625 |
1.17e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1390 KRKLQKDLEGLSQrheekVAAYDKLEKTKTR-LQQELDDLLVDLDH---------------QRQSACNLEKKQKKFDQLL 1453
Cdd:PHA02562 152 RRKLVEDLLDISV-----LSEMDKLNKDKIReLNQQIQTLDMKIDHiqqqiktynknieeqRKKNGENIARKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1454 AEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKqfrtemEDLMSSKDDV----GKSVHELEKS 1529
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQK------VIKMYEKGGVcptcTQQISEGPDR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1530 KRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAqfeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRS 1609
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250
....*....|....*.
gi 972988096 1610 MAVAARKKLEMDLKDL 1625
Cdd:PHA02562 376 DNAEELAKLQDELDKI 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1470-1718 |
1.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1470 AEAEAREKETKALSLARALEEAMEQKAELERlnkqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELED 1549
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1550 EL-------QATEDAKLRLEVNLQA-------MKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsmAVAAR 1615
Cdd:COG3883 87 ELgeraralYRSGGSVSYLDVLLGSesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1616 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1695
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260
....*....|....*....|...
gi 972988096 1696 ERAKRQAQQERDELADEIANSSG 1718
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1187-1423 |
1.41e-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: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1187 EAQIQEMRQKHSQAVEELAEQLEQtkrVKANLEKAKQTLENERGElanevkvllQGKGDSEHKRKKVEAQLQELQVKFNE 1266
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1267 gerVRTELADkvtkLQVELDNVTGLLSQSDSKSSKLTKD--FSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF 1344
Cdd:COG3206 231 ---ARAELAE----AEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1345 REQLEEE-EEAKHNLEKQIATLHAQVADMKKKMEdsvgclETAEEVKR--KLQKDLEGLSQRHEEKVAAYDKLEKtktRL 1421
Cdd:COG3206 304 RAQLQQEaQRILASLEAELEALQAREASLQAQLA------QLEARLAElpELEAELRRLEREVEVARELYESLLQ---RL 374
|
..
gi 972988096 1422 QQ 1423
Cdd:COG3206 375 EE 376
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1630-1934 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1630 DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRE-EILAQAK---ENEKKLKSMEAEMIQLQEElaaaERAKRQAQQE 1705
Cdd:pfam17380 291 EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAiyaEQERMAMERERELERIRQE----ERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1706 RDELADEIANSSGKGALALEEKRRLEaRIAQLEEELEEEQGNTELINDRLKKANLQIDQINTdlnlERSHAQKNENARQQ 1785
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA----EQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1786 LERQNKELKVKLQEMEgtvKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRT-EKKLKDVLLQ-VDDERRNAEQ 1863
Cdd:pfam17380 442 EERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRKLL 518
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1864 YKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETA---DAMNREVSSLK----NKLRRGDLPFVVP 1934
Cdd:pfam17380 519 EKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMEREREMMRqiveSEKARAEYEATTP 596
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1044-1279 |
1.51e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1044 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAEL-KMQLAKKE-EELQAA---LARVEEEAAQKNMALKKIRELE----S 1114
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELeAAALQPGEeEELEEErrrLSNAEKLREALQEALEALSGGEggalD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1115 QISELQEDLesERASRnkAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQ-EVNilkktlEEE-AKTHE--AQI 1190
Cdd:COG0497 245 LLGQALRAL--ERLAE--YDPSLAELAERLESALIELEE------AASELRRYLDSlEFD------PERlEEVEErlALL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1191 QEMRQKHSQAVEEL-------AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLlqgkgdSEhKRKK--------VEA 1255
Cdd:COG0497 309 RRLARKYGVTVEELlayaeelRAELAELENSDERLEELEAELAEAEAELLEAAEKL------SA-ARKKaakklekaVTA 381
|
250 260 270
....*....|....*....|....*....|.
gi 972988096 1256 QLQEL-------QVKFNEGERVRTELADKVT 1279
Cdd:COG0497 382 ELADLgmpnarfEVEVTPLEEPGPNGADQVE 412
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1377-1926 |
1.60e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1377 EDSVGCLETAEEVKRKLQKDLEglSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEE 1456
Cdd:TIGR00606 159 EDSNWPLSEGKALKQKFDEIFS--ATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1457 KTISAKYAEERDRAEAEAREKE---TKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD---------------- 1517
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDeqlndlyhnhqrtvre 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1518 ------DVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKK--- 1588
Cdd:TIGR00606 317 kerelvDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKnfh 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1589 QLVRQVREMEAEL---------EDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDE---AIKQLRKLQAQMKDCMrE 1656
Cdd:TIGR00606 397 TLVIERQEDEAKTaaqlcadlqSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEElkfVIKELQQLEGSSDRIL-E 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1657 LDDTRASREEILAQAKENEKkLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANS------SGKGALALEEKRRL 1730
Cdd:TIGR00606 476 LDQELRKAERELSKAEKNSL-TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRtqmemlTKDKMDKDEQIRKI 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1731 EARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDL---NLERSHAQKNENA-RQQLERQNKEL------------- 1793
Cdd:TIGR00606 555 KSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLaklNKELASLEQNKNHiNNELESKEEQLssyedklfdvcgs 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1794 ---KVKLQEMEGTVK--SKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQA 1868
Cdd:TIGR00606 635 qdeESDLERLKEEIEksSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1869 DKASTRLKqlKRQLEEAEEEAQRANASRRKLqreledatetadamnREVSSLKNKLRR 1926
Cdd:TIGR00606 715 ESELKKKE--KRRDEMLGLAPGRQSIIDLKE---------------KEIPELRNKLQK 755
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1077-1224 |
1.66e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1077 LKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQ--ISELQEDLESE-RASRNKAEKQKRDLGEELEALKTELED 1153
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1154 TLDStaaQQELrSKREQEVNILKKTLEEEAKTHEAQIQEMRQK--------HSQAVEELAEQLEQ------TKRVKANLE 1219
Cdd:PRK12704 105 LEKR---EEEL-EKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEILLEKVEEearheaAVLIKEIEE 180
|
....*
gi 972988096 1220 KAKQT 1224
Cdd:PRK12704 181 EAKEE 185
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
963-1398 |
1.90e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 963 QKLQLEKVTTEAKLKKLE---EEQIILEDQNCKLAKEKKLLEDRIAEFTTnLTEEEEKSKSLAKLKNKHEAMITDLEErl 1039
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEIENEMGIEMDIKAEMET-FNISHDDDKDHHIISKKHDENISDIRE-- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1040 rreekqrqeleKTRRKLEGDS--TDLSDQIAELQAQIAELKMQLAKKEEELQ--AALARVEEEAAQKNMaLKKIRELESQ 1115
Cdd:TIGR01612 1306 -----------KSLKIIEDFSeeSDINDIKKELQKNLLDAQKHNSDINLYLNeiANIYNILKLNKIKKI-IDEVKEYTKE 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1116 ISELQEDLESERASRNKAEKQKRDlGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKK-----TLEEEAKTHEAQI 1190
Cdd:TIGR01612 1374 IEENNKNIKDELDKSEKLIKKIKD-DINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEesnidTYFKNADENNENV 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1191 Q------EMRQKHSQAV----------------EELAEQLEQTKRVKANLEKAKQTLENER---GELANEVKVLL----- 1240
Cdd:TIGR01612 1453 LllfkniEMADNKSQHIlkikkdnatndhdfniNELKEHIDKSKGCKDEADKNAKAIEKNKelfEQYKKDVTELLnkysa 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1241 --------QGKGDSE---------HKRKKVEAQLQELQVKFNEGERVRTElaDKVTK----------LQVELDNV-TGLL 1292
Cdd:TIGR01612 1533 laiknkfaKTKKDSEiiikeikdaHKKFILEAEKSEQKIKEIKKEKFRIE--DDAAKndksnkaaidIQLSLENFeNKFL 1610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1293 SQSD--SKSSKLTKDFSALESQLQ----DTQEllqeenrqklslsTKLKQVEDEKNSFREQLEEEEEAKHNLEKQ----- 1361
Cdd:TIGR01612 1611 KISDikKKINDCLKETESIEKKISsfsiDSQD-------------TELKENGDNLNSLQEFLESLKDQKKNIEDKkkeld 1677
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 972988096 1362 -----IATLHAQVADMKKKMEdsVGCLETAEEVKRKLQKDLE 1398
Cdd:TIGR01612 1678 eldseIEKIEIDVDQHKKNYE--IGIIEKIKEIAIANKEEIE 1717
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
993-1118 |
1.90e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 993 LAKEKKL-LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLrreekqrQELEKTRRKLEGDSTDLSDQIAELQ 1071
Cdd:PRK09039 71 LERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1072 AQIAELKMQLAKKEEELQAALARVEEEAAQ-------KNMAL-KKIRELESQISE 1118
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKiadlgrrLNVALaQRVQELNRYRSE 198
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1621-1715 |
1.95e-04 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 46.15 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1621 DLKDLEAHIDS-----ANKNRDEAIKQLRKLQAQMKDCMRELDDTRASR----EEIlAQAKENEKKLKSMEAEMIQLQEE 1691
Cdd:COG0172 3 DIKLIRENPEAvkealAKRGFDLDVDELLELDEERRELQTEVEELRAERnalsKEI-GKAKKKGEEAEALIAEVKELKEE 81
|
90 100
....*....|....*....|....
gi 972988096 1692 LAAAERAKRQAQQERDELADEIAN 1715
Cdd:COG0172 82 IKELEEELKELEEELDELLLSIPN 105
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
973-1321 |
2.02e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 973 EAKLKKLEEEQ------IILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR 1046
Cdd:PRK01156 325 HAIIKKLSVLQkdyndyIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1047 QELEKTRRKLEGDSTDLSDQIAELQAQIAEL---KMQLAKKEEELQA-------------------------ALARVEEE 1098
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALrenLDELSRNMEMLNGqsvcpvcgttlgeeksnhiinhyneKKSRLEEK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1099 AAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeLEALKTELEDTLDSTAAQQE--------------- 1163
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDkhdkyeeiknryksl 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1164 ----LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1239
Cdd:PRK01156 559 kledLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEI 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1240 LQGKGDSEHKRKKVE------AQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQL 1313
Cdd:PRK01156 639 QENKILIEKLRGKIDnykkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
....*...
gi 972988096 1314 QDTQELLQ 1321
Cdd:PRK01156 719 NDINETLE 726
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1307-1515 |
2.16e-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: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1307 SALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETA 1386
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1387 EEVKRKLQ-----KDLEGLSQRHE--EKVAAYDK-----LEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLA 1454
Cdd:COG3883 99 GGSVSYLDvllgsESFSDFLDRLSalSKIADADAdlleeLKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1455 EEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSS 1515
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
976-1210 |
2.23e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 976 LKKLEEEQII-LEDQNCKLAKEK--KLLEDRI-AEFTTN-LTEEEEKSKSLAKLKNKHEamITDLEERLRREEKQRQELE 1050
Cdd:PRK05771 22 LEALHELGVVhIEDLKEELSNERlrKLRSLLTkLSEALDkLRSYLPKLNPLREEKKKVS--VKSLEELIKDVEEELEKIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1051 KTRRKLEGDSTDLSDQIAELQAQIAELK--------MQLAKKEEELQAALARVEEEaaqknmalkKIRELESQISELQED 1122
Cdd:PRK05771 100 KEIKELEEEISELENEIKELEQEIERLEpwgnfdldLSLLLGFKYVSVFVGTVPED---------KLEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1123 LESERASRN-----KAEKQKRDLGEELEALKTELEDTLDSTAAQQELrSKREQEVNILKKTLEEEakthEAQIQEMRQKH 1197
Cdd:PRK05771 171 YISTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSELI-REIKEELEEIEKERESL----LEELKELAKKY 245
|
250
....*....|...
gi 972988096 1198 SQAVEELAEQLEQ 1210
Cdd:PRK05771 246 LEELLALYEYLEI 258
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
995-1151 |
2.86e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 995 KEKKL--LEDRIAEFTTNLTEEEEKSKSLaklknkhEAMITDLEERLRREEKQRQelektrrKLEGDSTDLSDQIAELQA 1072
Cdd:PRK09039 51 KDSALdrLNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERS-------RLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 972988096 1073 QIAELKMQLAKKEEELQAALARVEEeaaqknmalkkireLESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL 1151
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVEL--------------LNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
861-1195 |
3.10e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 861 REKQLAAENRLtEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 940
Cdd:pfam07888 59 KEKERYKRDRE-QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 941 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKS 1020
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1021 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD-------QIAEL---QAQIAELKMQLAKKEEELQA 1090
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrTQAELhqaRLQAAQLTLQLADASLALRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1091 ALAR--VEEEAAQKNMALKK--IRELESQISELQEDLESERASRNKaekqkrdlgeeleaLKTELEDTLDSTAAQQELRS 1166
Cdd:pfam07888 298 GRARwaQERETLQQSAEADKdrIEKLSAELQRLEERLQEERMEREK--------------LEVELGREKDCNRVQLSESR 363
|
330 340
....*....|....*....|....*....
gi 972988096 1167 KREQEVNILKKTLEEEAKTHEAQIQEMRQ 1195
Cdd:pfam07888 364 RELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1039-1170 |
3.35e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1039 LRRE-EKQRQELEKTRRKLegdsTDLSDQIA-------ELQAQIAELKMQLAKKEEE---LQAALARVEEEAAqknmalk 1107
Cdd:PRK09039 44 LSREiSGKDSALDRLNSQI----AELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGAGA------- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1108 kirELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL---EDTLDstAAQQELRSKREQ 1170
Cdd:PRK09039 113 ---AAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALD--ASEKRDRESQAK 173
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1002-1273 |
3.41e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1002 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERL-RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQ 1080
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKReERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1081 LAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRD--LGEELEALKTELEDTLDST 1158
Cdd:pfam02029 114 SWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEnfAKEEVKDEKIKKEKKVKYE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1159 AAQQELRSKREQEVnilkKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQlEQTKRVKAnlEKAKQTLENERGELANEVKV 1238
Cdd:pfam02029 194 SKVFLDQKRGHPEV----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREE-EAEVFLEA--EQKLEELRRRRQEKESEEFE 266
|
250 260 270
....*....|....*....|....*....|....*
gi 972988096 1239 LLQgkgdseHKRKKVEAQLQELQVKFNEGERVRTE 1273
Cdd:pfam02029 267 KLR------QKQQEAELELEELKKKREERRKLLEE 295
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1503-1926 |
3.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1503 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQferdlqgrdeq 1582
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQ----------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1583 seEKKKQLVRQVREMEAELEderkQRSMAVA-ARKKLEMdlkdLEAHIDSANKNRDEaikqlrkLQAQMKDCMRELD--D 1659
Cdd:PRK04863 348 --EKIERYQADLEELEERLE----EQNEVVEeADEQQEE----NEARAEAAEEEVDE-------LKSQLADYQQALDvqQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1660 TRASREEILAQAKENEKKL-KSMEAEMIQLQEELAAAERAKRQAQQERDEL------ADEIANSSGKgalALEEKRRLEA 1732
Cdd:PRK04863 411 TRAIQYQQAVQALERAKQLcGLPDLTADNAEDWLEEFQAKEQEATEELLSLeqklsvAQAAHSQFEQ---AYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1733 RIAQLEEELEEEQGNTELINDRLKKANLQidQINTDLN-LERSHAQknenaRQQLERQNKELKVKLQEMEgtvkskykAS 1811
Cdd:PRK04863 488 EVSRSEAWDVARELLRRLREQRHLAEQLQ--QLRMRLSeLEQRLRQ-----QQRAERLLAEFCKRLGKNL--------DD 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1812 ITALEAKIAQLEEQLD--NETKERQAAckqvRRTEkkLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEA 1889
Cdd:PRK04863 553 EDELEQLQEELEARLEslSESVSEARE----RRMA--LRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS 626
|
410 420 430
....*....|....*....|....*....|....*..
gi 972988096 1890 QRANASRRKLQRELEDATETADAMNREVSSLKNKLRR 1926
Cdd:PRK04863 627 QDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1060-1216 |
3.88e-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: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1060 STDLSDQIAELQAQIAELKMQLA--KKEEELQAALARVEEEAAQKNMALKKIRELESQIS--ELQEDLESERASRNKAEK 1135
Cdd:pfam09731 282 NDDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRES 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1136 QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNIlKKTLEEEAKTHEAQIQEMRQK---HSQAVEELAEQLEQTK 1212
Cdd:pfam09731 362 YEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDI-KEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENR 440
|
....
gi 972988096 1213 RVKA 1216
Cdd:pfam09731 441 KAQQ 444
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
945-1241 |
3.94e-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: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 945 QQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKL 1024
Cdd:pfam15905 38 QPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKD-QKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1025 KNKHEAMITDLEERLRrEEKQRQELEKTRRKLEGDSTDLSDQIAELqaqiaelkMQLAKK-EEELQAALARVEEEAAQKN 1103
Cdd:pfam15905 117 KTSLSASVASLEKQLL-ELTRVNELLKAKFSEDGTQKKMSSLSMEL--------MKLRNKlEAKMKEVMAKQEGMEGKLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1104 MALKKIRELESQISELQEDLESERASRNKAEKQKRDLGE---ELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE 1180
Cdd:pfam15905 188 VTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEyitELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLE 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1181 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQ 1241
Cdd:pfam15905 268 EKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1540-1729 |
4.45e-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: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1540 MKTQLEELEDeLQATEDAKLRLEVNLQAMKAQFERdlqgrdeqSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLE 1619
Cdd:COG1579 2 MPEDLRALLD-LQELDSELDRLEHRLKELPAELAE--------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1620 MDLKDLEAHIDSANKNRD-EAI-KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1697
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEyEALqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|..
gi 972988096 1698 AKRQAQQERDELADEIANSSGKGALALEEKRR 1729
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1009-1273 |
4.48e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1009 TNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIA-------ELQAQIAELKMQL 1081
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQelrekrdELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1082 AKKEEELQAALARVEE---EAAQKNMALKKIRELESQISELQEDLESERASRNKAEK---QKRDLGEELEALKTELEDTL 1155
Cdd:COG1340 81 DELNEKLNELREELDElrkELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKElveKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1156 DSTAAQQELRSKREQ--EVNILKKTLEEEAKTHEAQIQEMRQKH---SQAVEELAEQLEQTKRVKANLEKAKQTLENERG 1230
Cdd:COG1340 161 KLKELRAELKELRKEaeEIHKKIKELAEEAQELHEEMIELYKEAdelRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 972988096 1231 ELANEVKVLLQGKGDSEHKRKK--VEAQLQELQVKFNEGERVRTE 1273
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLKKGEKLTTE 285
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
974-1163 |
4.68e-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: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 974 AKLKKLEEEQIILE----DQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR-QE 1048
Cdd:pfam04012 15 EGLDKAEDPEKMLEqairDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEkKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1049 LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARveEEAAQKNMALKK----------IRELEsQISE 1118
Cdd:pfam04012 95 LEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTslgslstssaTDSFE-RIEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 972988096 1119 LQEDLESERASRNKAEkQKRDLGEELEALKTELEDTLDSTAAQQE 1163
Cdd:pfam04012 172 KIEEREARADAAAELA-SAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1029-1712 |
4.70e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.59 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1029 EAMITDLEERLRREEKQRQE-LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakKEEELQAALARvEEEAAQKNMALK 1107
Cdd:NF041483 505 ERVRTEAIERATTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAAREL--REETERAIAAR-QAEAAEELTRLH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1108 KirELESQISELQEDLeseRASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE------------------------ 1163
Cdd:NF041483 582 T--EAEERLTAAEEAL---ADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEqeaerlrteaaadasaaraegenv 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1164 ---LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQK-HSQAVEELAEQLEQTKRVKAnleKAKQTLENERGELANE-VKV 1238
Cdd:NF041483 657 avrLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQErERA 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1239 LLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTEL--ADKVTKLQVElDNVTGLLSQSDSKSSKLTkdfSALESQLQDT 1316
Cdd:NF041483 734 REQSEELLASARKRVEEAQAEAQRLVEEADRRATELvsAAEQTAQQVR-DSVAGLQEQAEEEIAGLR---SAAEHAAERT 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1317 QELLQEENRQKLS--LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIAT-------LHAQVADMKKKM--EDSVGCLET 1385
Cdd:NF041483 810 RTEAQEEADRVRSdaYAERERASEDANRLRREAQEETEAAKALAERTVSEaiaeaerLRSDASEYAQRVrtEASDTLASA 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1386 AEEVKRKLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAE 1465
Cdd:NF041483 890 EQDAARTRADAREDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGE 969
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1466 -ERDRAEAeareketkALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVheLEKSKRALEQQVEEMKTQL 1544
Cdd:NF041483 970 aERLRAEA--------AETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRT--LDEARKDANKRRSEAAEQA 1039
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1545 EELEDElQATEDAKLRLEVNLQAMKAQFERDLQGrDEQSEEKKKQLVRQVREMEAE----LEDERKQ--------RSMAV 1612
Cdd:NF041483 1040 DTLITE-AAAEADQLTAKAQEEALRTTTEAEAQA-DTMVGAARKEAERIVAEATVEgnslVEKARTDadellvgaRRDAT 1117
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1613 AARKKLEMDLKDLEAHIDSAN-KNRDEAIKQLR----KLQAQMKDCMRELDDTRASREEILAQA------------KENE 1675
Cdd:NF041483 1118 AIRERAEELRDRITGEIEELHeRARRESAEQMKsageRCDALVKAAEEQLAEAEAKAKELVSDAnseaskvriaavKKAE 1197
|
730 740 750
....*....|....*....|....*....|....*..
gi 972988096 1676 KKLKSMEAEMIQLQEElaaAERAKRQAQQERDELADE 1712
Cdd:NF041483 1198 GLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEE 1231
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1523-1910 |
4.95e-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: 45.02 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1523 VHELEKSKRAleqqVEEMKTQLEELE-DELQATED---AKLRLEvnlqamkaqfERDLQGRDEQSEEKKkqlvrqvreme 1598
Cdd:pfam05701 69 LEELESTKRL----IEELKLNLERAQtEEAQAKQDselAKLRVE----------EMEQGIADEASVAAK----------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1599 AELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQ-------LRKLQAQMKDCMRELDDTRASREeiLAQA 1671
Cdd:pfam05701 124 AQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRaeeavsaSKEIEKTVEELTIELIATKESLE--SAHA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1672 KENEKKLKSMEAEMIQLQEELAAaERAKRQAQQERDELADEIANS-------SGKGALALEEKRRLEARIAQLEEELEEE 1744
Cdd:pfam05701 202 AHLEAEEHRIGAALAREQDKLNW-EKELKQAEEELQRLNQQLLSAkdlksklETASALLLDLKAELAAYMESKLKEEADG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1745 QGNTELINDRLKKA-----------NLQIDQINTDLNLERSHAqknENARQQLERQNKELkVKLQEMEGtvkskyKASIT 1813
Cdd:pfam05701 281 EGNEKKTSTSIQAAlasakkeleevKANIEKAKDEVNCLRVAA---ASLRSELEKEKAEL-ASLRQREG------MASIA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1814 aleakIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRAN 1893
Cdd:pfam05701 351 -----VSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVE 425
|
410
....*....|....*..
gi 972988096 1894 ASRRKLQRELEDATETA 1910
Cdd:pfam05701 426 SRLEAVLKEIEAAKASE 442
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1659-1957 |
5.42e-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: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1659 DTRASREEILAQAKENEKKLKSMEAEMIQLQEElAAAERAKRQAQQERDELADEIANSSGKgaLALEEKRRLEAriaQLE 1738
Cdd:NF012221 1532 DNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALET---NGQ 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1739 EELEEEQGNTELINDRLKKANLQIDQINTDLNlershaQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAK 1818
Cdd:NF012221 1606 AQRDAILEESRAVTKELTTLAQGLDALDSQAT------YAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQR 1679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1819 IAQLEEQLDNETKERQAAckqVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAeeeaqrANASRRK 1898
Cdd:NF012221 1680 HVDNQQKVKDAVAKSEAG---VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAA------ANDAQSR 1750
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1899 LQRELEDATETADAMNREVSSLknKLRRGDLPfvvprrmARKGA-GDG-SDEEVDGKADGA 1957
Cdd:NF012221 1751 GEQDASAAENKANQAQADAKGA--KQDESDKP-------NRQGAaGSGlSGKAYSVEGVAE 1802
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
863-1196 |
5.56e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 863 KQLAAENRLTEMETLQSQL------MAEKLQLQEQLQAETELCAEAE----ELRARLTAKKQELEEI--CHDLEARVEEE 930
Cdd:pfam05557 123 AELELQSTNSELEELQERLdllkakASEAEQLRQNLEKQQSSLAEAEqrikELEFEIQSQEQDSEIVknSKSELARIPEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 931 EERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlekvtteaKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTN 1010
Cdd:pfam05557 203 EKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE--------REEKYREEAATLELEKEKLEQELQSWVKLAQDTGLN 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1011 LTEEEEKSKSLAKLKNK---HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA---KK 1084
Cdd:pfam05557 275 LRSPEDLSRRIEQLQQReivLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLlltKE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1085 EEELQAALARVEEEAAQKNMALKK---IRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELedTLDSTAAQ 1161
Cdd:pfam05557 355 RDGYRAILESYDKELTMSNYSPQLlerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL--QALRQQES 432
|
330 340 350
....*....|....*....|....*....|....*
gi 972988096 1162 QELRSKREQEVNILKKTLEEeaktHEAQIQEMRQK 1196
Cdd:pfam05557 433 LADPSYSKEEVDSLRRKLET----LELERQRLREQ 463
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
842-1076 |
5.92e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 842 QVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcaeaEELRARLTAKKQELEEich 921
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI----------AELRAELEAQKEELAE--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 922 dlearveeeeercqHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeqiiLEDQNCKLAKEKKLLE 1001
Cdd:COG4942 109 --------------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1002 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAE 1076
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1338-1584 |
6.36e-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: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1338 EDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAYDKLekt 1417
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1418 kTRLQQELDDLLVdldhqrqsacnlekkqkKFDQLLAeektiSAKYAEERDRAEAEAREKETKalslARALEEAMEQKAE 1497
Cdd:COG3883 92 -ARALYRSGGSVS-----------------YLDVLLG-----SESFSDFLDRLSALSKIADAD----ADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1498 LERLNKQFRTEMEDLMSSKDdvgksvhELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQ 1577
Cdd:COG3883 145 LEAKKAELEAKLAELEALKA-------ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
....*..
gi 972988096 1578 GRDEQSE 1584
Cdd:COG3883 218 AAAAAAA 224
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
972-1115 |
6.50e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 972 TEAKLKKLEEEQIILEDQNcKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEK 1051
Cdd:PRK01156 617 IDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKA 695
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1052 TRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKeEELQAALARVEE--EAAQKNMALKKIRELESQ 1115
Cdd:PRK01156 696 NRARLESTIEILRTRINELSDRINDINETLESM-KKIKKAIGDLKRlrEAFDKSGVPAMIRKSASQ 760
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
908-1492 |
6.96e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 908 RLTAKKQELEEICHDLEARVEEEeercQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILE 987
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 988 D---QNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDleerlrREEKQRQELeKTRRKLEGDSTDLS 1064
Cdd:PRK01156 239 SalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIND------PVYKNRNYI-NDYFKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1065 DQIAELQAQIAELKmQLAKKEEELQAALARVEEEAAQKNmalkkirELESQISELQEDLESERASRNKAEKQKRDLGE-- 1142
Cdd:PRK01156 312 QILSNIDAEINKYH-AIIKKLSVLQKDYNDYIKKKSRYD-------DLNNQILELEGYEMDYNSYLKSIESLKKKIEEys 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1143 -ELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQkHSQAVEELAEQL------------- 1208
Cdd:PRK01156 384 kNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRE-NLDELSRNMEMLngqsvcpvcgttl 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1209 --EQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEA-QLQELQVKFNEGERVRTELADKVTKLQvEL 1285
Cdd:PRK01156 463 geEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARADLEDIKIKIN-EL 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1286 DNVTGLLSQSDSKSSKLtkDFSALESQLQDTQELLQEENrqklslSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATL 1365
Cdd:PRK01156 542 KDKHDKYEEIKNRYKSL--KLEDLDSKRTSWLNALAVIS------LIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1366 HAQVADMKKKMEDSVGCLET----AEEVKR---KLQKDLEGLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQS 1438
Cdd:PRK01156 614 KSYIDKSIREIENEANNLNNkyneIQENKIlieKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA 693
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1439 ACNLEKKQKKFDQLLAEEKTISAKYAEERDRaeAEAREKETKALSLARALEEAM 1492
Cdd:PRK01156 694 KANRARLESTIEILRTRINELSDRINDINET--LESMKKIKKAIGDLKRLREAF 745
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1530-1702 |
7.09e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1530 KRALEQQVEEMKTQ----LEELEDELQATEDAKLrLEVN--LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELED 1603
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1604 ERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDcmrelddtrASREEILAQAKEnekKLKSMEA 1683
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEILLEKVEE---EARHEAA 172
|
170
....*....|....*....
gi 972988096 1684 EMIQLQEELAAAErAKRQA 1702
Cdd:PRK12704 173 VLIKEIEEEAKEE-ADKKA 190
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1541-1832 |
7.34e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1541 KTQLEELEDELQATEDAKLRLEvnlqAMKAQFERDLQGRdeqsEEKKKQLVRQVRemeAELEDERkQRSMAVAARKKLEM 1620
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFE----ARQARLEREKAAR----EARHKKAAEARA---AKDKDAV-AAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1621 DLKDLEAHIDSANKNRDEAIKQLRKLQAqmkdcmrelddtRASREEILAQAKENEKKLKsmeaemIQlqeelAAAERAK- 1699
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQA------------RARQAEKQAAAAADPKKAA------VA-----AAIARAKa 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1700 RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIdqintdlnlershaqkn 1779
Cdd:PRK05035 560 KKAAQQAANAEAEEEVDPKKAAVA-AAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAI----------------- 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 972988096 1780 enARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKE 1832
Cdd:PRK05035 622 --ARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1040-1411 |
7.56e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1040 RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISEL 1119
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1120 QEDLESERASRNKAEkqkrdlgEELEALKTE---LEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQK 1196
Cdd:COG4372 86 NEQLQAAQAELAQAQ-------EELESLQEEaeeLQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1197 hsqaVEELAEQLEQTKRVKANLEKAKQTLE-NERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA 1275
Cdd:COG4372 159 ----LESLQEELAALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1276 DKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAK 1355
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1356 HNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVAAY 1411
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1004-1229 |
7.92e-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: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1004 IAEFTTNLTEEEEKSKSLAKlknkhEAMITDLEE--------RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA 1075
Cdd:pfam15709 302 TFVVTGNMESEEERSEEDPS-----KALLEKREQekasrdrlRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMRE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1076 ELKMQLAKKEEELQAALARVEEEAAQknmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTL 1155
Cdd:pfam15709 377 ELELEQQRRFEEIRLRKQRLEEERQR--------QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAE 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1156 DSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVkANLEKAKQTLENER 1229
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARL-ALEEAMKQAQEQAR 521
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1666-1840 |
8.16e-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: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1666 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEEKRRLEARIAQLEEELEEEQ 1745
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLE-------LEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1746 GNTElindrLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKykasITALEAKIAQLEEQ 1825
Cdd:COG1579 87 NNKE-----YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----KAELDEELAELEAE 157
|
170
....*....|....*
gi 972988096 1826 LDNETKERQAACKQV 1840
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
836-1134 |
9.45e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 836 KVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETL---QSQLMAEKLQLQEQLQAETELCAEAEELRARLTAK 912
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 913 KQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKlqlekvttEAKLKKLEEEQIILEDQNCK 992
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--------AEALKKEAEEAKKAEELKKK 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 993 LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDqiaELQA 1072
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE---ELDE 1787
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972988096 1073 QIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELEsqISELQEDLESERASRNKAE 1134
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME--DSAIKEVADSKNMQLEEAD 1847
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1307-1736 |
9.80e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1307 SALESQLQ-DTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEeeakHNLEKQIATLHAQVADMKKKmedsvgcLET 1385
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAE-------LEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1386 AEEVKRKLQKDLEgLSQRHEEKVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAE 1465
Cdd:COG4717 114 LREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1466 ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMED-----------------------------LMSSK 1516
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaaleerlkearlllliaaallallglggsLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1517 DDVGK------SVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQL 1590
Cdd:COG4717 273 LTIAGvlflvlGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1591 VRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIdsanknrdEAIKQLRKLQAQMKDCMRELDDTRASREEILAQ 1670
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL--------EQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1671 AKENEkklksMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGAL--ALEEKRRLEARIAQ 1736
Cdd:COG4717 425 LDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRE 487
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
911-1393 |
1.06e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 911 AKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEE-SARQKLQLEKVtteakLKKLEEEQIILEDQ 989
Cdd:pfam05622 7 EEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTpGGKKYLLLQKQ-----LEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 990 NCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAmitdLEERLRREEKQRQELEKTRRKLEgDSTDLSDQIAE 1069
Cdd:pfam05622 82 RDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDI----LRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1070 LQAQIAELKMQLAKKEEELQAAlarveeeaaqkNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKT 1149
Cdd:pfam05622 157 LEERNAEYMQRTLQLEEELKKA-----------NALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1150 EledtldstaaQQELRSKREqevnILKKTLEE-----EAKTHEAQIQEMRQKHSQAVEELAEQLeQTKRVKANLEKakqt 1224
Cdd:pfam05622 226 E----------KERLIIERD----TLRETNEElrcaqLQQAELSQADALLSPSSDPGDNLAAEI-MPAEIREKLIR---- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1225 lenergeLANEVKVL-LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKssklT 1303
Cdd:pfam05622 287 -------LQHENKMLrLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSK----A 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1304 KDFSALESQLQDTQELLQEENRQklsLSTKLKQVEDEKNSFREQLEEEEEakhNLEkqiATLHAQVADMKKKMEDSVGCL 1383
Cdd:pfam05622 356 EDSSLLKQKLEEHLEKLHEAQSE---LQKKKEQIEELEPKQDSNLAQKID---ELQ---EALRKKDEDMKAMEERYKKYV 426
|
490
....*....|
gi 972988096 1384 ETAEEVKRKL 1393
Cdd:pfam05622 427 EKAKSVIKTL 436
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1050-1280 |
1.06e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1050 EKTRRKLEGDSTDLSDQIAELQAQiaelKMQLAKKEEELQAALARVEEeaaqknmalkkirelesqiseLQEDLEseras 1129
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEEL----ERELEQKAEEAEALLKEAEK---------------------LKEELE----- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1130 rnkaeKQKRDLGEELEALKTELEDtldstAAQQELRSKREQEVNILKKTLEEEAKTHEA----QIQEMRQKHSQAVEELA 1205
Cdd:PRK00409 555 -----EKKEKLQEEEDKLLEEAEK-----EAQQAIKEAKKEADEIIKELRQLQKGGYASvkahELIEARKRLNKANEKKE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1206 EQLEQTKRVKANLEKakqtlenerGElanEVKVL-LQGKGDSEHKRKKVEAQLQE----LQVKFNEGERVRTELADKVTK 1280
Cdd:PRK00409 625 KKKKKQKEKQEELKV---------GD---EVKYLsLGQKGEVLSIPDDKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKK 692
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
975-1148 |
1.06e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 975 KLKKLEEEQIILEDQNCKL-AKE------KKLLEDRIAEFTTNLT----EEEEKSKSLAKLKNKHEAmITDLEERLRREE 1043
Cdd:smart00787 110 DVKLLMDKQFQLVKTFARLeAKKmwyewrMKLLEGLKEGLDENLEglkeDYKLLMKELELLNSIKPK-LRDRKDALEEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1044 KQRQELEKTRRKLEGDSTD-LSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkirELESQISELQED 1122
Cdd:smart00787 189 RQLKQLEDELEDCDPTELDrAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKS-------ELNTEIAEAEKK 261
|
170 180
....*....|....*....|....*.
gi 972988096 1123 LESERASRNKAEKQKRDLGEELEALK 1148
Cdd:smart00787 262 LEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1536-1924 |
1.12e-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: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1536 QVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLvRQVREMEAELEDERKQRSMAVAAR 1615
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI-RLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1616 KK----LEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEaemiQLQEE 1691
Cdd:pfam05557 82 KKyleaLNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE----QLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1692 LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLeARIAQLEEELeeeqgntelinDRLKKANLQIDQINTDLNL 1771
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKEL-----------ERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1772 ershaqknenarqqLERQNKELKVKLQEMEgtvksKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEK-KLKDV 1850
Cdd:pfam05557 226 --------------LKEEVEDLKRKLEREE-----KYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDlSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1851 LLQVDDERRNAEQYKDQADKASTR---------LKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADAMNREVSSLK 1921
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEkarreleqeLAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYD 366
|
...
gi 972988096 1922 NKL 1924
Cdd:pfam05557 367 KEL 369
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1032-1171 |
1.18e-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: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1032 ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK-KIR 1110
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELA 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1111 ELESQISELQEDLES-------ERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQE 1171
Cdd:pfam12795 160 ALKAQIDMLEQELLSnnnrqdlLKARRDLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1471-1882 |
1.18e-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: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1471 EAEAREKETKALSLARALEE--AMEQKAELERLNKQFRTEMEDLMSSK-DDVGKSVHELE---------KSKRAL---EQ 1535
Cdd:pfam06160 14 ELEERKNELMNLPVQEELSKvkKLNLTGETQEKFEEWRKKWDDIVTKSlPDIEELLFEAEelndkyrfkKAKKALdeiEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1536 QVEEMKTQLEELEDELQA--TEDAKLRLEVN-LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELE--DERKQRSM 1610
Cdd:pfam06160 94 LLDDIEEDIKQILEELDEllESEEKNREEVEeLKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSqfEELTESGD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1611 AVAARK---KLEMDLKDLEAHIDS-------ANKNRDEAIKQLRKLQAQMKDCMRELDDtrasrEEILAQAKENEKKLKS 1680
Cdd:pfam06160 174 YLEAREvleKLEEETDALEELMEDipplyeeLKTELPDQLEELKEGYREMEEEGYALEH-----LNVDKEIQQLEEQLEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1681 MEAEMIQLqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANL 1760
Cdd:pfam06160 249 NLALLENL--ELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEH--------------AEEQNKELKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1761 QIDQINTDLNL---ERSHAQKNENARQQLERQNKELKVKLQEMEGT---VKSKYK---ASITALEAKIAQLEEQLDNETK 1831
Cdd:pfam06160 313 ELERVQQSYTLnenELERVRGLEKQLEELEKRYDEIVERLEEKEVAyseLQEELEeilEQLEEIEEEQEEFKESLQSLRK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1832 ERQAACKQVRRTEKKLKDVLLQVddERRN----AEQYKDQADKASTRLKQLKRQL 1882
Cdd:pfam06160 393 DELEAREKLDEFKLELREIKRLV--EKSNlpglPESYLDYFFDVSDEIEDLADEL 445
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1053-1182 |
1.26e-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: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1053 RRKLEGDSTdlSDQIAELQAQIAELKMQlakkeeelQAALARVEEEAAQKnmalkKIRELESQISELQEDLESERAsRNK 1132
Cdd:COG0542 401 RVRMEIDSK--PEELDELERRLEQLEIE--------KEALKKEQDEASFE-----RLAELRDELAELEEELEALKA-RWE 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 972988096 1133 AEKQkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEE 1182
Cdd:COG0542 465 AEKE---LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
1035-1163 |
1.38e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 43.30 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1035 LEERLRREEKQR--QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlakKEEELQAALARVEEEAAQKNMALKKIREL 1112
Cdd:PRK00247 288 AEQRAQYREKQKekKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKT---RTAEKNEAKARKKEIAQKRRAAEREINRE 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1113 ESQisELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1163
Cdd:PRK00247 365 ARQ--ERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQV 413
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1061-1138 |
1.41e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1061 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKR 1138
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1172-1500 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1172 VNILKKTLEEEAKTHEAQIQEMRQKHSQaveelaEQLEQTKRVKA-NLEKAKQTLENERgelANEVKVLLQGKGDSEHKR 1250
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQ------ERLRQEKEEKArEVERRRKLEEAEK---ARQAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1251 KKVEAQLQ----ELQVKFNEGERVRTEladkvtKLQVELDNVTGLlsqsdsksskltkdfsaleSQLQDTQELLQEENRQ 1326
Cdd:pfam17380 342 MAMEREREleriRQEERKRELERIRQE------EIAMEISRMREL-------------------ERLQMERQQKNERVRQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1327 KLSLSTKLKQVEDEKN-SFREQLEEEEEAKHNLEKqiatlhAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHE 1405
Cdd:pfam17380 397 ELEAARKVKILEEERQrKIQQQKVEMEQIRAEQEE------ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1406 E---KVAAYDKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAR------- 1475
Cdd:pfam17380 471 ErkrKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRkqqemee 550
|
330 340
....*....|....*....|....*....
gi 972988096 1476 ----EKETKALSLARALEEAMEQKAELER 1500
Cdd:pfam17380 551 rrriQEQMRKATEERSRLEAMEREREMMR 579
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1463-1643 |
1.57e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1463 YAEERDRAEAEAREKEtkalslARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 1542
Cdd:PRK12705 26 KKRQRLAKEAERILQE------AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1543 qLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVrqVREMEAELEDERKQRSMAVAARKKLEMDL 1622
Cdd:PRK12705 100 -LDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLL--LKLLDAELEEEKAQRVKKIEEEADLEAER 176
|
170 180
....*....|....*....|.
gi 972988096 1623 KDLEAHIDSANKNRDEAIKQL 1643
Cdd:PRK12705 177 KAQNILAQAMQRIASETASDL 197
|
|
| Cortex-I_coil |
pfam09304 |
Cortexillin I, coiled coil; Members of this family are predominantly found in the ... |
1053-1156 |
1.61e-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: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1053 RRKLEGDSTDLSDQIAELQAQIAELKM---QLAKKEEELQAALARVEEEAAQKNmalKKIRELESQISELQEDLESERAS 1129
Cdd:pfam09304 4 KERLEASKNSLANKLAGLENSLESEKTsreQLIKQKDELESLLASLEQENAERE---KRLRELEAKLDEALKNLELEKLA 80
|
90 100
....*....|....*....|....*..
gi 972988096 1130 RNKAEKQKRDLGEELEALKTELEDTLD 1156
Cdd:pfam09304 81 RMELESRLSKTEKDKAILELKLAEALD 107
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1458-1912 |
1.62e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1458 TISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV 1537
Cdd:COG5278 72 TGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALM 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1538 EEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKK 1617
Cdd:COG5278 152 DEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1618 LEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1697
Cdd:COG5278 232 LELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1698 AKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQ 1777
Cdd:COG5278 312 AAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1778 KNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDE 1857
Cdd:COG5278 392 VLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAV 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1858 RRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDATETADA 1912
Cdd:COG5278 472 AALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1398-1635 |
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 972988096 1398 EGLSQRHEEKVAAYDK--LEKTKTRLQQELddllvdldhQRQSAcNLEKKQKKFDQllAEEKTISAKYAEERDRAEAEAR 1475
Cdd:NF012221 1549 KHAKQDDAAQNALADKerAEADRQRLEQEK---------QQQLA-AISGSQSQLES--TDQNALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1476 EKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMssKDDVGKSvheLEKSKRALEQQVEEMKTQleeLEDELQATE 1555
Cdd:NF012221 1617 AVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQEQ---LDDAKKISGKQLADAKQR---HVDNQQKVK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1556 DAKLRLEVNL-QAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAElEDERKQRSMAVAARKKLEMDLKDLEAHIDSANK 1634
Cdd:NF012221 1689 DAVAKSEAGVaQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQ-QAESDANAAANDAQSRGEQDASAAENKANQAQA 1767
|
.
gi 972988096 1635 N 1635
Cdd:NF012221 1768 D 1768
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
859-1239 |
1.73e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 859 KVREKQlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQ 938
Cdd:pfam12128 475 RAREEQ---EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 939 AEKKKMQQNIQELEEQLEEEESARQ-------KLQLEKV----------TTEAKLKKLEE----EQIILEDQNCKLAKEK 997
Cdd:pfam12128 552 GKVISPELLHRTDLDPEVWDGSVGGelnlygvKLDLKRIdvpewaaseeELRERLDKAEEalqsAREKQAAAEEQLVQAN 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 998 KLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE----EKQRQELEKTRRKLEGDSTDLSDQIaelQAQ 1073
Cdd:pfam12128 632 GELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERkdsaNERLNSLEAQLKQLDKKHQAWLEEQ---KEQ 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1074 IAELKMQLAKK----EEELQAALARVEEEAAQKNMALKkireleSQISELQEDLESERASRNKAEKQKRDLGEELEALKT 1149
Cdd:pfam12128 709 KREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAK------AELKALETWYKRDLASLGVDPDVIAKLKREIRTLER 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1150 ELEDTldstaaqqelrSKREQEV----NILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL 1225
Cdd:pfam12128 783 KIERI-----------AVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKAS 851
|
410
....*....|....
gi 972988096 1226 ENERGELANEVKVL 1239
Cdd:pfam12128 852 EKQQVRLSENLRGL 865
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1113-1329 |
1.83e-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: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1113 ESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELrskreqevnilkKTLEEEAKTHEAQIQE 1192
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE------LQAEL------------EALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1193 MRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER-GELANEVKVLLQ-GKGDSE------HKRKKVEAQLQELQVKF 1264
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKiADADADlleelkADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1265 NEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1329
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1060-1282 |
1.87e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1060 STDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQIS-------ELQEDLESERASRNK 1132
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQelrekrdELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1133 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSK-----REQEVNILKKTLE----EEAKTHEAQIQEMRQKHSQAvEE 1203
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEierleWRQQTEVLSPEEEkelvEKIKELEKELEKAKKALEKN-EK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 972988096 1204 LAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQ 1282
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1056-1665 |
1.87e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1056 LEGDSTDLSDQIAELQAQIaelkmqlakkeeelqaalarvEEEAAQKNMALKKIRELESQIselqedleserasrNKAEK 1135
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQI---------------------ADDEKSHSITLKEIERLSIEY--------------NNAMD 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1136 QKRDLGEELEALKTELE--DTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEaqiqemrqkhSQAVEELAEQLEQTKR 1213
Cdd:PRK01156 233 DYNNLKSALNELSSLEDmkNRYESEIKTAESDLSMELEKNNYYKELEERHMKII----------NDPVYKNRNYINDYFK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1214 VKANLEKAKQTLENERGELanevkvllqgkgDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLS 1293
Cdd:PRK01156 303 YKNDIENKKQILSNIDAEI------------NKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1294 QSDSKSSKL------TKDFSALESQLQDTQELLQEE-NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLH 1366
Cdd:PRK01156 371 SIESLKKKIeeysknIERMSAFISEILKIQEIDPDAiKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1367 AQVAdmkkkmeDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVaayDKLEKTKTRLQQElddllvdLDHQRQSACNLEKkq 1446
Cdd:PRK01156 451 GQSV-------CPVCGTTLGEEKSNHIINHYNEKKSRLEEKI---REIEIEVKDIDEK-------IVDLKKRKEYLES-- 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1447 KKFDQLLAEEKTISAKYAEERD--RAEAEAREKETKALSLARALE----EAMEQKAE--LERLNKQFRTEMEDLMSSKDD 1518
Cdd:PRK01156 512 EEINKSINEYNKIESARADLEDikIKINELKDKHDKYEEIKNRYKslklEDLDSKRTswLNALAVISLIDIETNRSRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1519 VGKSVHELEKSKRALEQQVEEMKT----QLEELEDELQATEDAKLRLEVNLQAMKA------QFERDLQGRDEQsEEKKK 1588
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILIEKlrgkidNYKKQIAEIDSI-IPDLK 670
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1589 QLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRELDDTRASRE 1665
Cdd:PRK01156 671 EITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS----DRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1055-1209 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1055 KLEGDSTDLSDQIAELQAQIA----ELKMQLAKKEEELQAALARVEEEAAQK---------NMALKKIRELESQISELQE 1121
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGpvaqELVDRLEKETEALRERLQKDLEEVRAKlepyleelqAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1122 DLEsERASRnKAEKQKRDLGEELEALKTELEDTLDSTAAQ-----QELRSKREQEVNILKKTLEEEAKTHEAQ----IQE 1192
Cdd:pfam01442 81 ELR-KRLNA-DAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQE 158
|
170
....*....|....*..
gi 972988096 1193 MRQKHSQAVEELAEQLE 1209
Cdd:pfam01442 159 LREKLEPQAEDLREKLD 175
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
963-1251 |
2.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 963 QKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE 1042
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1043 EKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAalARVEEEAAQKNMALKKIRELESQISELQED 1122
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA--LEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1123 LESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVE 1202
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 972988096 1203 ELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK 1251
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1606-1900 |
2.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1606 KQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1685
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1686 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRlkKANLQIDQI 1765
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1766 NTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEK 1845
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1846 KLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQ 1900
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1456-1606 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1456 EKTISAKYAEERDRAEAEAREKETKAL-SLARALEEAMEQ------------KAELERLNKQFRTEM----------EDL 1512
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKRCQALLqELSAPLEEKISQgsysvpggyqlyLEDREKLVEKYRQVPrkgvkaeevlQEF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1513 MSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDL-QGRDEQSEEKKKQLV 1591
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLrQLKEKMEEERENLLK 255
|
170
....*....|....*
gi 972988096 1592 RQVREMEAELEDERK 1606
Cdd:cd16269 256 EQERALESKLKEQEA 270
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1038-1170 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1038 RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKkeeeLQAALARVEEEAAQKNMALKKIRELESQIS 1117
Cdd:pfam00529 76 RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ----AQIDLARRRVLAPIGGISRESLVTAGALVA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1118 ELQEDLESERASRNKAEKQKRDLGEELEAL--KTELEDTLDSTAAQQELRSKREQ 1170
Cdd:pfam00529 152 QAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEAEAELKLAKLD 206
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1053-1300 |
2.26e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1053 RRKLEGDSTDLS----------DQIAELQAQIAELKMQL----------AKKEEELQA-ALARVEEEAAQKNMALKKIRE 1111
Cdd:PHA02562 152 RRKLVEDLLDISvlsemdklnkDKIRELNQQIQTLDMKIdhiqqqiktyNKNIEEQRKkNGENIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1112 LESQISELQEDL-------ESERASRNKAEKQKRDLGEELEALKTEL----EDTLDSTAAQQelrskREQEVNILKKtLE 1180
Cdd:PHA02562 232 IKAEIEELTDELlnlvmdiEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQ-----ISEGPDRITK-IK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1181 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRV---KANLEKAKQTLENERGELanevkvllqgkgdsehkrKKVEAQL 1257
Cdd:PHA02562 306 DKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKA------------------KKVKAAI 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 972988096 1258 QELQVKF----NEGERVRTELADKVTKLQ------VELDNVTGLLSQSDSKSS 1300
Cdd:PHA02562 368 EELQAEFvdnaEELAKLQDELDKIVKTKSelvkekYHRGIVTDLLKDSGIKAS 420
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1201-1334 |
2.40e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1201 VEELAEQLEQTKRVKANLEkakQTLENERGELANevkvllqgkgdSEHKRKKVEAQLqelqvkfNEGERVRTELADKVTK 1280
Cdd:PRK09039 62 IAELADLLSLERQGNQDLQ---DSVANLRASLSA-----------AEAERSRLQALL-------AELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 972988096 1281 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELL-------QEENRQKLSLSTKL 1334
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQAKIADLGRRL 181
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1078-1228 |
2.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1078 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDS 1157
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQ 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1158 TAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEmrqkhsQAVEELAEQL------EQTKRVKANLEKAKQTLENE 1228
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPE------QARKLLLKLLdaeleeEKAQRVKKIEEEADLEAERK 177
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1635-1788 |
2.59e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1635 NRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEnekKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIA 1714
Cdd:PRK09039 50 GKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRA---SLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELD 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1715 NSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLerSHAQKNenarQQLER 1788
Cdd:PRK09039 127 SEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV--ALAQRV----QELNR 194
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1106-1409 |
2.89e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1106 LKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELE----------ALKTELEDTLDSTAAQQELRSKREQEvniL 1175
Cdd:pfam17380 274 LLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVErrrkleeaekARQAEMDRQAAIYAEQERMAMERERE---L 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1176 KKTLEEEAKTHEAQIQE----MRQKHSQAVEELA-EQLEQTKRVKANLEKAKQT--LENERGELANEVKVLLQGKGDSEH 1248
Cdd:pfam17380 351 ERIRQEERKRELERIRQeeiaMEISRMRELERLQmERQQKNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1249 KRKKVEAQLQElQVKFNEGERVRTELADKVTKLQVELDNvtgllsQSDSKSSKLTKDFSALESQL--------------Q 1314
Cdd:pfam17380 431 EARQREVRRLE-EERAREMERVRLEEQERQQQVERLRQQ------EEERKRKKLELEKEKRDRKRaeeqrrkilekeleE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1315 DTQELLQEENRQKLSlstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQ 1394
Cdd:pfam17380 504 RKQAMIEEERKRKLL----EKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMR 579
|
330
....*....|....*
gi 972988096 1395 KDLEGLSQRHEEKVA 1409
Cdd:pfam17380 580 QIVESEKARAEYEAT 594
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
868-1157 |
2.90e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 868 ENRLTEMETLQSQLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQN 947
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELK---ELAEKRDELNAQVKELREEAQE----LREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 948 IQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEdriaefttnlteeeeKSKSLAKLKNK 1027
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVE---------------KIKELEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1028 HEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK 1107
Cdd:COG1340 152 AKKAL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 972988096 1108 KIRELESQISELQEDLESERASRNKAEKQKRDlgEELEALKTELEDTLDS 1157
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKK 278
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1303-1733 |
2.92e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1303 TKDFSALESQLQDTQELLQeenrqklslSTKLKQVEDEKNSFREQLEEeeeakhnLEKQIATLHAQVADMKKKMEDSVGC 1382
Cdd:PRK04778 78 TNSLPDIEEQLFEAEELND---------KFRFRKAKHEINEIESLLDL-------IEEDIEQILEELQELLESEEKNREE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1383 LETAEEVKRKLQKDLegLSQRHEEKVAaYDKLEKtktRLQqelddllvdldhqrqsacNLEKKQKKFDQLlaeekTISAK 1462
Cdd:PRK04778 142 VEQLKDLYRELRKSL--LANRFSFGPA-LDELEK---QLE------------------NLEEEFSQFVEL-----TESGD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1463 YAEERDRAEaEAREKETkalslarALEEAMEQ-KAELERLNKQFRTEMEDL------MSSKDDVGKSVhELEKSKRALEQ 1535
Cdd:PRK04778 193 YVEAREILD-QLEEELA-------ALEQIMEEiPELLKELQTELPDQLQELkagyreLVEEGYHLDHL-DIEKEIQDLKE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1536 QVEEMKTQLEELEdeLQATEDAKLRLEVNLQAMKAQFERDLQGRDEqSEEKKKQLVRQVREMEAELEDerkqrsmavaar 1615
Cdd:PRK04778 264 QIDENLALLEELD--LDEAEEKNEEIQERIDQLYDILEREVKARKY-VEKNSDTLPDFLEHAKEQNKE------------ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1616 KKLEMDLKDLEAHI-DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAA 1694
Cdd:PRK04778 329 LKEEIDRVKQSYTLnESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQG 408
|
410 420 430
....*....|....*....|....*....|....*....
gi 972988096 1695 AERAKRQAQQERDELADEIANSsgkgalaleeKRRLEAR 1733
Cdd:PRK04778 409 LRKDELEAREKLERYRNKLHEI----------KRYLEKS 437
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1493-1641 |
3.07e-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: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1493 EQKAELERLNKQfrtEMEDLMSSKDDVgksVHELEKSKRALEQ---QVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK 1569
Cdd:pfam05911 677 DLKTEENKRLKE---EFEQLKSEKENL---EVELASCTENLEStksQLQESEQLIAELRSELASLKESNSLAETQLKCMA 750
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972988096 1570 AQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIK 1641
Cdd:pfam05911 751 ESYE-DLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDADQEDKK 821
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
885-1110 |
3.12e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 885 KLQLQEQLQAETELCAEAEELRARLTAKKQELEEIchDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQK 964
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEF--RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 965 LQLEKVTTEAKLKKLEEEQIILEdqnckLAKEKKLLEDRIAEFTTNLTEE--------EEKSKSLAKLKNKHEAMITDLE 1036
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNhpdvialrAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1037 ERLRREEKQRQELEKTRRKLEGDStdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIR 1110
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
961-1222 |
3.14e-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: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 961 ARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLED-------------RIAEFTTN----LTEEEEKSKSLAK 1023
Cdd:TIGR01612 1556 AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflKISDIKKKindcLKETESIEKKISS 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1024 LK-NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSdqiaELQAQIAELKMQLAKKEEELQAALARVEEEAAQK 1102
Cdd:TIGR01612 1636 FSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIA 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1103 NMalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSkreqevNILkKTLEEE 1182
Cdd:TIGR01612 1712 NK-----EEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIA------GCL-ETVSKE 1779
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 972988096 1183 AKTHEaqiqEMRQKHSQAVEELAEQLEQTKRVKANLEKAK 1222
Cdd:TIGR01612 1780 PITYD----EIKNTRINAQNEFLKIIEIEKKSKSYLDDIE 1815
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1682-1849 |
3.26e-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: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1682 EAEMIQLQEELAAAERAKRQAQQERDELadeianssgkgalaleekRRLEARIAQLEEELEEEQGNTELINDRLKKANLQ 1761
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRL------------------QALESELAISRQDYDGATAQLRAAQAAVKAAQAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1762 IDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSK---YKASITALEAKIAQLEEQLDNETKERQAACK 1838
Cdd:pfam00529 119 LAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLdqiYVQITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
170
....*....|.
gi 972988096 1839 QVRRTEKKLKD 1849
Cdd:pfam00529 199 ELKLAKLDLER 209
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1060-1284 |
3.47e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1060 STDLSDQIAELQAQIAE--------------LKMQLaKKEEELQAALARveeeaaqknmalkKIRELESQISELQEDLES 1125
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAkeksvrqqqqqrasLLAQL-KKQEEAISQASR-------------KLRETQNTLNQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1126 ERASRNKAEKQK----RDLGEELEAL-----KTELEDTLDSTAAQQE---------LRSKREQEVNILKKTLEEEAkthe 1187
Cdd:PRK11637 108 LNASIAKLEQQQaaqeRLLAAQLDAAfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQTREELA---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1188 AQIQEMRQKHSQAVEELAEQLEQtkrvkanlekaKQTLENERGELANEVKVLlqgkgdsEHKRKKVEAQLQELQVkfNEg 1267
Cdd:PRK11637 184 AQKAELEEKQSQQKTLLYEQQAQ-----------QQKLEQARNERKKTLTGL-------ESSLQKDQQQLSELRA--NE- 242
|
250
....*....|....*..
gi 972988096 1268 ervrTELADKVTKLQVE 1284
Cdd:PRK11637 243 ----SRLRDSIARAERE 255
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1435-1594 |
3.55e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1435 QRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARalEEAMEQKAELERLNKQFRTEMEDlms 1514
Cdd:PRK00409 532 LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK--KEADEIIKELRQLQKGGYASVKA--- 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1515 skddvgksvHELEKSKRALEQQVEEMKTQL---EELEDELQATEDAKLR--------------LEVNLQA----MKAQfE 1573
Cdd:PRK00409 607 ---------HELIEARKRLNKANEKKEKKKkkqKEKQEELKVGDEVKYLslgqkgevlsipddKEAIVQAgimkMKVP-L 676
|
170 180
....*....|....*....|.
gi 972988096 1574 RDLQGRDEQSEEKKKQLVRQV 1594
Cdd:PRK00409 677 SDLEKIQKPKKKKKKKPKTVK 697
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1140-1527 |
3.68e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1140 LGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANle 1219
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1220 kakqtleneRGELANEVKVLLQGKGDSEHKRKKVEAQLQELqvkfnegervrtelADKVTKLQVELDNVTgllsQSDSKS 1299
Cdd:pfam07888 110 ---------SEELSEEKDALLAQRAAHEARIRELEEDIKTL--------------TQRVLERETELERMK----ERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1300 SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDS 1379
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1380 VGCLETAEEVKRKLQKDLEGL-SQR-------HEEKVAAYD---KLEKTKTRLQQELDDLLVDLDHQRQSAcnlEKKQKK 1448
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSMaAQRdrtqaelHQARLQAAQltlQLADASLALREGRARWAQERETLQQSA---EADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1449 FDQLLAEEKTISAKYAEER---DRAEAE-AREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVH 1524
Cdd:pfam07888 320 IEKLSAELQRLEERLQEERmerEKLEVElGREKDCNRVQLSESRRELQELKASLRVAQK----EKEQLQAEKQELLEYIR 395
|
...
gi 972988096 1525 ELE 1527
Cdd:pfam07888 396 QLE 398
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
886-1221 |
3.87e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 886 LQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQqniqeleeqleEEESARQKL 965
Cdd:pfam05622 62 LLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMD-----------ILRESSDKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 966 QLEKVTTEAKLKKLEEeqiiLEDqnckLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEA---MITDLEERLRRE 1042
Cdd:pfam05622 131 KKLEATVETYKKKLED----LGD----LRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETykrQVQELHGKLSEE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1043 EKQRQELEKTRRKLEG--------------DSTDLSDQIAEL---QAQIAELKMQLAKKEE---------------ELQA 1090
Cdd:pfam05622 203 SKKADKLEFEYKKLEEklealqkekerliiERDTLRETNEELrcaQLQQAELSQADALLSPssdpgdnlaaeimpaEIRE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1091 ALARVEEEaaQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQ 1170
Cdd:pfam05622 283 KLIRLQHE--NKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEEL---QKALQEQGSKAED 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 972988096 1171 EVNILKKTLEEEAKTHEAQIQemRQKHSQAVEELAEQLEQTKRVK-ANLEKA 1221
Cdd:pfam05622 358 SSLLKQKLEEHLEKLHEAQSE--LQKKKEQIEELEPKQDSNLAQKiDELQEA 407
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1148 |
4.40e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 859 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEeeeercqhlQ 938
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA---------E 1684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 939 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEaKLKKLEEEQIILEDQNCKLAKEKKlledRIAEfttNLTEEEEKS 1018
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDK----KKAE---EAKKDEEEK 1756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1019 KSLAKLKNKHEAMITDLEERLRR--EEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAlarVE 1096
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSA---IK 1833
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1097 EEAAQKNMALKKIRELESQI----SELQEDLESErASRNKAEKQKRDLGEELEALK 1148
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKfnknNENGEDGNKE-ADFNKEKDLKEDDEEEIEEAD 1888
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1445-1614 |
4.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1445 KQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVH 1524
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1525 ELEKSKRALEQQVEEMKTQLEELEDELQatEDAKLRLEVNLQAMKAQFERDLqgrdeqsEEKKKQLVRQVREmEAELEDE 1604
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELY--RVAGLTPEQARKLLLKLLDAEL-------EEEKAQRVKKIEE-EADLEAE 175
|
170
....*....|
gi 972988096 1605 RKQRSMAVAA 1614
Cdd:PRK12705 176 RKAQNILAQA 185
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
965-1136 |
4.45e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 40.27 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 965 LQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEK 1044
Cdd:pfam15619 16 LQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1045 QRQELEKTRRKLEGDSTDLS-DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAA----QKNMALKKIRELESQISEL 1119
Cdd:pfam15619 96 ELLRLRDQLKRLEKLSEDKNlAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfrrQLAAEKKKHKEAQEEVKIL 175
|
170
....*....|....*..
gi 972988096 1120 QEDLESERASRNKAEKQ 1136
Cdd:pfam15619 176 QEEIERLQQKLKEKERE 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1656-1895 |
4.53e-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: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1656 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalaleekrRLEARIA 1735
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA--------------EAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1736 QLeeeleeeqgnTELINDRLK---KANLQIDQINTDLN-------LERSHAQK--NENARQQLERQnKELKVKLQEMegt 1803
Cdd:COG3883 83 ER----------REELGERARalyRSGGSVSYLDVLLGsesfsdfLDRLSALSkiADADADLLEEL-KADKAELEAK--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1804 vKSKYKASITALEAKIAQLEEQ---LDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKR 1880
Cdd:COG3883 149 -KAELEAKLAELEALKAELEAAkaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250
....*....|....*
gi 972988096 1881 QLEEAEEEAQRANAS 1895
Cdd:COG3883 228 AAAAAAAAAAAAAAA 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1017-1203 |
4.56e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1017 KSKSLAKLKNKHEAMITDLEERLRREE--------KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL 1088
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEaikkeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1089 QaalarveeeaaqknmalKKIRELESQISELQEDLESerasrnkAEKQKrdlgEELEALKTELEDTLDSTAAQQelrskR 1168
Cdd:PRK12704 106 E-----------------KREEELEKKEKELEQKQQE-------LEKKE----EELEELIEEQLQELERISGLT-----A 152
|
170 180 190
....*....|....*....|....*....|....*
gi 972988096 1169 EQEVNILKKTLEEEAKtHEAQIQeMRQKHSQAVEE 1203
Cdd:PRK12704 153 EEAKEILLEKVEEEAR-HEAAVL-IKEIEEEAKEE 185
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1050-1287 |
4.61e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.59 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1050 EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQI----------SEL 1119
Cdd:pfam15742 33 EKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVlkqaqsiksqNSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1120 QEDLESERASRNKAEKQKRDLGEELE-ALKTELEDTLDSTAAQQELRSKREQEVnilkktlEEEAKTHEAQIQEMRQKHS 1198
Cdd:pfam15742 113 QEKLAQEKSRVADAEEKILELQQKLEhAHKVCLTDTCILEKKQLEERIKEASEN-------EAKLKQQYQEEQQKRKLLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1199 QAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK---KVEAQLQELQvkfNEGERVRTELA 1275
Cdd:pfam15742 186 QNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKsnqELSEKLSSLQ---QEKEALQEELQ 262
|
250
....*....|..
gi 972988096 1276 DKVTKLQVELDN 1287
Cdd:pfam15742 263 QVLKQLDVHVRK 274
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1526-1730 |
4.63e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1526 LEKSK-RALEQQVEEMKTQLEELEDELQATEDaklrLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDE 1604
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNK----NIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1605 RKQRSMAVAARKKLEMDLKDLEAHIDSANK----------------NRDEAIKQLRKLQAQMKDC---MRELDDTRASRE 1665
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELqhsLEKLDTAIDELE 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1666 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRL 1730
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1581-1785 |
4.89e-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: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1581 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMREL--D 1658
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1659 DTRASREEILAQAK---------ENEKKLKSMEAEMIQ----LQEELAAAERAKRQAQQERDELADEIANSSGKGALALE 1725
Cdd:COG3883 99 GGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEelkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1726 EKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQ 1785
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
1022-1215 |
4.93e-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: 40.69 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1022 AKLKNKHEAmITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQI--AELQAQIAELKMQLAKKEEELQAALARVEEEA 1099
Cdd:pfam06705 5 VKLSNMNER-VSGFHDKMENEIEVKRVDEDTRVKMIKEAIAHLEKLiqTESKKRQESFEDIQEEFKKEIDNMQETIKEEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1100 AQKNMALKK-IRELESQISELQEDLESERASRNKAekqkrdlgeeLEALKTELEDTL-DSTAAQQELRSKREQEVNILKK 1177
Cdd:pfam06705 84 DDMAANFRKaLAELNDTINNVETNLQNEIAIHNDA----------IEALRKEALKSLnDLETGIATENAERKKMYDQLNK 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 972988096 1178 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVK 1215
Cdd:pfam06705 154 KVAEGFARISAAIDTEKNARDSAVSAATTELTNTKLVE 191
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
963-1403 |
4.97e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 41.59 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 963 QKLQLEKvttEAKLKKLEEEQII-------LEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDL 1035
Cdd:pfam15070 7 KQLQTER---DQYAENLKEEGAVwqqkmqqLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAGPSEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1036 EERLRRE-EKQRQELEKTRRKLEG---DSTDLSDQIAELQAQIAELKMQL---AKKEEELQAALARVEEEAAQKNMALKK 1108
Cdd:pfam15070 84 EQRLQEEaEQLQKELEALAGQLQAqvqDNEQLSRLNQEQEQRLLELERAAerwGEQAEDRKQILEDMQSDRATISRALSQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1109 IRELESQISELQED--------------LESERASRNKAEKQKRDLGEELEALKTELEdtLDSTAAqQELRSKREQEVNi 1174
Cdd:pfam15070 164 NRELKEQLAELQNGfvkltnenmeltsaLQSEQHVKKELAKKLGQLQEELGELKETLE--LKSQEA-QSLQEQRDQYLA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1175 lkkTLEEEAKTHEAQIQEMRQKHSQAVE--ELAEQLEQTK-RVKANLEKAKQTLENERGELANEVKvllqgkgdsehKRK 1251
Cdd:pfam15070 240 ---HLQQYVAAYQQLASEKEELHKQYLLqtQLMDRLQHEEvQGKVAAEMARQELQETQERLEALTQ-----------QNQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1252 KVEAQLQELQVKfNEGERVRTELADKvtklqveldnvtgllsqsDSKSSKLT--KDFsalesqlqDTQELLQEenrqklS 1329
Cdd:pfam15070 306 QLQAQLSLLANP-GEGDGLESEEEEE------------------EAPRPSLSipEDF--------ESREAMVA------F 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972988096 1330 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLetAEEVKRKLQKDLEGLSQR 1403
Cdd:pfam15070 353 FNSALAQAEEERAELRRQLKEQKRRCRRLAQQAAPAQEEPEHEAHAPGTGGDSV--PVEVHQALQVAMEKLQSR 424
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1066-1161 |
5.01e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 40.80 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1066 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalkkIRELESQISELQEDLESERASRNKAEKQkrDLGEELE 1145
Cdd:COG4223 1 EIAALEAAVAELPAQLTALEQRLAALEAAPAAAAA--------TAALEARLAALRAALAAAREAVAAAAAA--ALEARLA 70
|
90
....*....|....*.
gi 972988096 1146 ALKTELEDTLDSTAAQ 1161
Cdd:COG4223 71 ALEAKAAAPEAEAAAA 86
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
987-1092 |
5.26e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 41.57 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 987 EDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRklegdstdlsdQ 1066
Cdd:smart00435 276 EKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKK-----------Q 344
|
90 100
....*....|....*....|....*.
gi 972988096 1067 IAELQAQIAELKMQLAKKEEELQAAL 1092
Cdd:smart00435 345 IERLEERIEKLEVQATDKEENKTVAL 370
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1250-1581 |
5.35e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1250 RKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1329
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1330 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKMEDSVGCLETAEEVKRKLQKDLEGLSQRHEEKVA 1409
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1410 AydKLEKTKTRLQQELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAEERDRAEAEAREKETKALSLARALE 1489
Cdd:COG4372 179 A--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1490 EAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMK 1569
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330
....*....|..
gi 972988096 1570 AQFERDLQGRDE 1581
Cdd:COG4372 337 AELADLLQLLLV 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
887-1229 |
5.68e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 887 QLQEQLQAETELCAEAEELRARLTAKKQELEEIchdlEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQ 966
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQL----EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 967 LEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR 1046
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1047 QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESE 1126
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1127 RASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAE 1206
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330 340
....*....|....*....|...
gi 972988096 1207 QLEQTKRVKANLEKAKQTLENER 1229
Cdd:COG4372 348 VGLLDNDVLELLSKGAEAGVADG 370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
863-1100 |
5.77e-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: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 863 KQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKK 942
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNE---EYNELQAELEALQAEIDK----LQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 943 K----MQQNIQELEEQLEEEES-----ARQKLQLEKVTTEAKLKKLEEeqiiLEDQNCKLAKEKKLLEDRIAEFTTNLTE 1013
Cdd:COG3883 90 EraraLYRSGGSVSYLDVLLGSesfsdFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1014 EEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKtrrklegdstdlsdQIAELQAQIAELKMQLAKKEEELQAALA 1093
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA--------------ELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*..
gi 972988096 1094 RVEEEAA 1100
Cdd:COG3883 232 AAAAAAA 238
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1529-1724 |
6.01e-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: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1529 SKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLqgrdEQSEEkkkqlvrQVREMEAELEDERkqr 1608
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEA----ESSRE-------QLQELEEQLATER--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1609 smavAARKKLEMDLKDLEAHIDSankNRDEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSMEAEM 1685
Cdd:pfam09787 107 ----SARREAEAELERLQEELRY---LEEELRRSKATLQSRIKDREAEIEKLRNqltSKSQSSSSQSELENRLHQLTETL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 972988096 1686 IQLQEELAA--AERAKRQAQQERDELADEIANSSGKGALAL 1724
Cdd:pfam09787 180 IQKQTMLEAlsTEKNSLVLQLERMEQQIKELQGEGSNGTSI 220
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
870-1229 |
6.11e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 870 RLTEMETLQSQLMAEKLQLQEQLQA----ETELCAEAEELRARLTAKKQELEE---IChDLEARVEEEEERCQHLQAEKK 942
Cdd:PRK10246 427 RLVALHGQIVPQQKRLAQLQVAIQNvtqeQTQRNAALNEMRQRYKEKTQQLADvktIC-EQEARIKDLEAQRAQLQAGQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 943 -----KMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEEQIILEDQNCKLAKEKKLLED---RIAEFTTNLTEE 1014
Cdd:PRK10246 506 cplcgSTSHPAVEAYQALEPGVNQSRLDALEK-----EVKKLGEEGAALRGQLDALTKQLQRDESeaqSLRQEEQALTQQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1015 -EEKSKSLAKLKNKHEamitDLEERLRREEKQRQELEKTRRKLEgdstdLSDQIAELQAQIAELKMQLAKKEEELQAALA 1093
Cdd:PRK10246 581 wQAVCASLNITLQPQD----DIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1094 RveeeaaqknMALkKIRELESQISELQEDlESERASRNKAEKQKRDLGEELEALKTELE-----DTLDSTAAQQELRSKR 1168
Cdd:PRK10246 652 G---------YAL-TLPQEDEEASWLATR-QQEAQSWQQRQNELTALQNRIQQLTPLLEtlpqsDDLPHSEETVALDNWR 720
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 972988096 1169 EQEVNILkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQT--------------KRVKANLEKAKQTLENER 1229
Cdd:PRK10246 721 QVHEQCL--SLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASvfddqqaflaalldEETLTQLEQLKQNLENQR 793
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
857-1227 |
6.31e-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: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 857 LVKVREKQLAAENRLTEMETLQSQLMAEklqLQEQLQAETELCAEAEELRARL-TAKKQ-------------ELEEICHD 922
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQILEE---LDELLESEEKNREEVEELKDKYrELRKTllanrfsygpaidELEKQLAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 923 LEARVEEEEERC---QHLQAEK--KKMQQNIQELEEQLEEEESARQKL------QLEKVttEAKLKKLEEEQIILEDQNc 991
Cdd:pfam06160 158 IEEEFSQFEELTesgDYLEAREvlEKLEEETDALEELMEDIPPLYEELktelpdQLEEL--KEGYREMEEEGYALEHLN- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 992 kLAKEKKLLEDRIAEFTTNL--TEEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAE 1069
Cdd:pfam06160 235 -VDKEIQQLEEQLEENLALLenLELDEAEEALEEIEER----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1070 LQAQIAELKM--QLAKKEEELQAAL-ARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEA 1146
Cdd:pfam06160 310 LKEELERVQQsyTLNENELERVRGLeKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1147 L-KTELEdtldstaAQQELrSKREQEVNILKKTLEeeaKTH----EAQIQEMRQKHSQAVEELAEQLEQT----KRVKAN 1217
Cdd:pfam06160 390 LrKDELE-------AREKL-DEFKLELREIKRLVE---KSNlpglPESYLDYFFDVSDEIEDLADELNEVplnmDEVNRL 458
|
410
....*....|
gi 972988096 1218 LEKAKQTLEN 1227
Cdd:pfam06160 459 LDEAQDDVDT 468
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1516-1651 |
6.32e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1516 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1595
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1596 EMEAELEDERKQRSMAVAARkklemDLKDLEAHIDSANKNRDEAIKQLRKLQAQMK 1651
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1614-1927 |
6.34e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1614 ARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELa 1693
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1694 aaeRAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQleeeleeeqgntelindrlkkanLQIDQINTDLNLER 1773
Cdd:COG1340 81 ---DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER-----------------------LEWRQQTEVLSPEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1774 shaqknenaRQQLERQNKELKVKLQEMEgtVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQ 1853
Cdd:COG1340 135 ---------EKELVEKIKELEKELEKAK--KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972988096 1854 VDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRANASRRKLQRELEDA--TETADAMNREVSSLKNKLRRG 1927
Cdd:COG1340 204 ADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALkrEKEKEELEEKAEEIFEKLKKG 279
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1065-1282 |
6.46e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1065 DQIAELQAQIAELKMQLAkkeeelqaalarVEEEAAQknmalkkirELESQISELQEDLESerasrnkaekqkrdlgeeL 1144
Cdd:PRK09039 53 SALDRLNSQIAELADLLS------------LERQGNQ---------DLQDSVANLRASLSA------------------A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1145 EALKTELEDTLDSTAAQQELRSKREQEvniLKKTLEEEAKTHEaqiQEMRQkhsqaVEELAEQLEQTKRVKANLEKAKQt 1224
Cdd:PRK09039 94 EAERSRLQALLAELAGAGAAAEGRAGE---LAQELDSEKQVSA---RALAQ-----VELLNQQIAALRRQLAALEAALD- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 972988096 1225 lenergelanevkvllqgkgDSEHKRKKVEAQLQELqvkfneGERVRTELADKVTKLQ 1282
Cdd:PRK09039 162 --------------------ASEKRDRESQAKIADL------GRRLNVALAQRVQELN 193
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1034-1380 |
6.64e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1034 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA-----ELKMQLAKKEEELQAALARVE--EEAAQKNM-- 1104
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSyeedsELKPSGQGGLDEEEAFLDRTAkrEERRQKRLqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1105 ALKKIRELESQISELQEDLESERASRNKAEKqkrdlgeelealkteledtldSTAAQQELRSKREQEVNILKKTLEEEAK 1184
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEEN---------------------SSWEKEEKRDSRLGRYKEEETEIREKEY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1185 THEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA--NEVKVLL-QGKGDSEHKRKKVEAQLQELQ 1261
Cdd:pfam02029 141 QENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvkYESKVFLdQKRGHPEVKSQNGEEEVTKLK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1262 VKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQE-----ENRQKLSLSTKLKQ 1336
Cdd:pfam02029 221 VTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEElkkkrEERRKLLEEEEQRR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 972988096 1337 VEDEKnsfrEQLEEEEEAKHNLEKQIATLHAQVADMKKKM-EDSV 1380
Cdd:pfam02029 301 KQEEA----ERKLREEEEKRRMKEEIERRRAEAAEKRQKLpEDSS 341
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1086-1193 |
6.98e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.21 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1086 EELQAALARVEEEAAqknmaLKKIRELESQISELQEDLESERASRNKAEKQ----KRDlGEELEALKteledtldstaaq 1161
Cdd:PRK05431 12 EAVKEALAKRGFPLD-----VDELLELDEERRELQTELEELQAERNALSKEigqaKRK-GEDAEALI------------- 72
|
90 100 110
....*....|....*....|....*....|....*
gi 972988096 1162 qelrskreQEVNILK---KTLEEEAKTHEAQIQEM 1193
Cdd:PRK05431 73 --------AEVKELKeeiKALEAELDELEAELEEL 99
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1219-1367 |
7.81e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1219 EKAKQTLenerGELANEVKVLLQGkgdSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNvtgLLSQSDSK 1298
Cdd:PRK00409 505 EEAKKLI----GEDKEKLNELIAS---LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKE 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 972988096 1299 SSKLTKdfSALESQLQDTQELLQEENRQKLSLstKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1367
Cdd:PRK00409 575 AQQAIK--EAKKEADEIIKELRQLQKGGYASV--KAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
960-1222 |
7.85e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 960 SARQKL--QLEKVTTEAKLKKLEEEQI-ILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKlknKHEAMITDLE 1036
Cdd:PHA02562 150 PARRKLveDLLDISVLSEMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA---RKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1037 ERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA--KKEEE--------------LQAALARVEEEAA 1100
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKmyekggvcptctqqISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1101 QKNMALKKIRELESQISELQEdLESErasRNKAEKQKRDLGEELEALKTELedtldstaaqqelrskreqevnilkKTLE 1180
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEE-IMDE---FNEQSKKLLELKNKISTNKQSL-------------------------ITLV 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 972988096 1181 EEAKTHEAQIQEM---RQKHSQAVEELAEQLEQTKRVKANLEKAK 1222
Cdd:PHA02562 358 DKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1005-1145 |
7.91e-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: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1005 AEFTTNLTE--EEEKSKSlAKLKNKHEAMITDLEERLRRE--------EKQRQELEKTRRKLEGDSTDLSDQIAELQAQI 1074
Cdd:pfam03148 203 EKFTQDNIEraEKERAAS-AQLRELIDSILEQTANDLRAQadavnfalRKRIEETEDAKNKLEWQLKKTLQEIAELEKNI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1075 AELKMQLAKKEEELQAALARVEEEAAQKNMAL----------KKIRELESQISELQEDLESERASRNKAEKQKRDLGEEL 1144
Cdd:pfam03148 282 EALEKAIRDKEAPLKLAQTRLENRTYRPNVELcrdeaqyglvDEVKELEETIEALKQKLAEAEASLQALERTRLRLEEDI 361
|
.
gi 972988096 1145 E 1145
Cdd:pfam03148 362 A 362
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1441-1650 |
8.00e-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: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1441 NLEKKQKKFDQLLAEEKTISAkyAEERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKddvg 1520
Cdd:COG3206 190 ELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP---- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1521 kSVHELEKSKRALEQQVEEMKTQLEELEDELQAtedaklrlevnLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAE 1600
Cdd:COG3206 264 -VIQQLRAQLAELEAELAELSARYTPNHPDVIA-----------LRAQIAALRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 972988096 1601 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQM 1650
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1503-1713 |
8.09e-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: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1503 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEDELQATED-AKLRLEVNLQAMKAQFERD-----L 1576
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEErLAEALEKLEEAEKAADESErgrkvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1577 QGRDEQSEEKKKQLVRQVRemEAELEDERKQRSMAVAARKklemdLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRE 1656
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLK--EAKEIAEEADRKYEEVARK-----LVVVEGDLERAEERAELAESKIVELEEELKVVGNN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 972988096 1657 LDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1713
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDEL 213
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1581-1717 |
8.16e-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: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1581 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRD------------EAIKQLRKLQA 1648
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaaltkgneelarEALAEKKSLEK 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 972988096 1649 QMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSS 1717
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA-KAQEAVQTSLGSLSTSSATDS 165
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1730-1929 |
8.85e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1730 LEARIAQLEEELEEEQGNTELIN-DRLKKANLQIDQI---NTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVK 1805
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAeekEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1806 -SKYKASITALEAKIAQLEEQLDnETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKAstRLKQLKRQLee 1884
Cdd:COG4717 127 lLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEEL-- 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 972988096 1885 aeeeaQRANASRRKLQRELEDATETADAMNREVSSLKNKLRRGDL 1929
Cdd:COG4717 202 -----EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
859-1188 |
9.37e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 859 KVREKQLAAENRLTEMETLQSQLMAEKLQlqEQLQAETELCAEAEELRARLTAKKQELeeichdleARVEEEEERCQHLQ 938
Cdd:PLN03229 440 KLKEQILKAKESSSKPSELALNEMIEKLK--KEIDLEYTEAVIAMGLQERLENLREEF--------SKANSQDQLMHPVL 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 939 AEK-KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlkkleeeqiILEDQNCKLAKEKKLLEDRIAEfTTNLTEEEEK 1017
Cdd:PLN03229 510 MEKiEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAK---------ALSEKKSKAEKLKAEINKKFKE-VMDRPEIKEK 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1018 SKSL-AKLKNKHEAMITDLEERLRRE-EKQRQELEKTRRKLEgDSTDLsdQIAELQAQIAELKMQLAkkEEELQAALARV 1095
Cdd:PLN03229 580 MEALkAEVASSGASSGDELDDDLKEKvEKMKKEIELELAGVL-KSMGL--EVIGVTKKNKDTAEQTP--PPNLQEKIESL 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1096 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeLEALKTELEDTLDSTAAQQELRSKREQevniL 1175
Cdd:PLN03229 655 NEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEK------IEALEQQIKQKIAEALNSSELKEKFEE----L 724
|
330
....*....|...
gi 972988096 1176 KKTLEEEAKTHEA 1188
Cdd:PLN03229 725 EAELAAARETAAE 737
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1525-1710 |
9.44e-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: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1525 ELEKSKRALEQQVEEMKTQLEELEDELQATEDAKlrlevnlqamkaqferdlqgRDEQSEEKKKQLVRQVREMEAELEDE 1604
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1605 RKQRSMAVAARKKLEmdlkdleahiDSANKNRDEAIKqlrKLQAQMKdcmRELDDTRASREEILAQAKENEKKLKSMEAE 1684
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 972988096 1685 MIQLQEELAAAERAKRQAQQERDELA 1710
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1470-1736 |
9.60e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.09 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1470 AEAEAREKETKALSLARALEEA----MEQKaELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLE 1545
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEArqarLERE-KAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1546 EledelqatedaklrlevNLQAMKAQFERDLQGRDEQSEEKkkqlvrqvremEAELEDERKQRSMAVAAR---KKLEMDL 1622
Cdd:PRK05035 515 D-----------------NSAVIAAREARKAQARARQAEKQ-----------AAAAADPKKAAVAAAIARakaKKAAQQA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1623 KDLEAHIDSANK----NRDEAIKQLRKLQAQMKD-----CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1693
Cdd:PRK05035 567 ANAEAEEEVDPKkaavAAAIARAKAKKAAQQAASaepeeQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA 646
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 972988096 1694 AAE----RAK-RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQ 1736
Cdd:PRK05035 647 AVAaaiaRAKaRKAAQQQANAEPEEAEDPKKAAVA-AAIARAKAKKAA 693
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1622-1880 |
9.65e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1622 LKDLEAHIDSANKNRDEAIKQLRKLQAQMKD-------CMRELDDTRASREEIlaqakenEKKLKSMEAEMIQLQeelaa 1694
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLKKqeeaisqASRKLRETQNTLNQL-------NKQIDELNASIAKLE----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1695 aeraKRQAQQERDeLADEIANSSGKG---ALAL----EEKRRLEaRIaqleeeleeeQGNTELINDRLKKANLQIDQINT 1767
Cdd:PRK11637 117 ----QQQAAQERL-LAAQLDAAFRQGehtGLQLilsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972988096 1768 DLNLERSHAQKNENARQQLERQNKELKVKLQEmegtVKSKYKASITALEAKIAQLEEQLdnetkerqaacKQVRRTEKKL 1847
Cdd:PRK11637 181 ELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQ----ARNERKKTLTGLESSLQKDQQQL-----------SELRANESRL 245
|
250 260 270
....*....|....*....|....*....|....
gi 972988096 1848 KDVLLQVDDE-RRNAEQYKDQADKASTRLKQLKR 1880
Cdd:PRK11637 246 RDSIARAEREaKARAEREAREAARVRDKQKQAKR 279
|
|
| |
