|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-829 |
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: 1303.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLE 358
Cdd:cd14930 153 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 359 SLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 438
Cdd:cd14930 233 SLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 439 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 518
Cdd:cd14930 313 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 519 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRD 598
Cdd:cd14930 393 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 599 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssais 678
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD------------------------------ 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 679 ppgVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLR 758
Cdd:cd14930 523 ---VEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLR 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743142585 759 CNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14930 600 CNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-829 |
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: 1279.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP--------GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETL 357
Cdd:cd14920 153 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQqDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14920 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd14920 473 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD----------------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 678 sppgVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd14920 524 ----VDRIVGLDQVTGMTETAfgSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLD 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14920 600 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
119-829 |
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: 1266.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESG-------KKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQ-ERELFQET 356
Cdd:cd01377 154 GSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVdDAEEFKLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd01377 234 DEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd01377 314 KGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK-FQRPRH 595
Cdd:cd01377 393 HMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 596 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggfqqfsflgsFPPSPPGSAERCSS 675
Cdd:cd01377 471 KKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDY------------EESGGGGGKKKKKG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 676 AisppgvegivgleqvsslgdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd01377 539 G------------------------------SFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLH 588
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01377 589 QLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
906-1986 |
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: 1223.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 906 TRQDEVLQARAQELQKVQELQQQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSEL 985
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 986 EARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDR 1065
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1066 LAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGR 1145
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1146 KEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1225
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1226 LRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTAR 1305
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1306 QEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEE 1385
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1386 TRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQR 1465
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1466 LAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALS 1545
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1546 LTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEV 1625
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1626 TVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQL 1705
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1706 RKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAI 1785
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1786 LEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAG 1865
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1866 ARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLE 1945
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1743142585 1946 EAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1986
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
119-829 |
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: 1156.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPAsvstVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIA----LSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGqQDKELFAETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14932 237 EAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14932 317 AQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14932 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD----------------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 678 sppgVEGIVGLEQVSSLGDGPP-GGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQ 756
Cdd:cd14932 528 ----VDRIVGLDKVAGMGESLHgAFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQ 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743142585 757 LRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14932 604 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
119-829 |
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: 1121.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGVPASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPrHL 596
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 597 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsAErcssa 676
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD---------------------AE----- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 677 isppgvegIVGLEQvSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQ 756
Cdd:cd14911 531 --------IVGMAQ-QALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQ 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743142585 757 LRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14911 602 LRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-829 |
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: 1095.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG-----------ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETL 357
Cdd:cd14919 150 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd14919 470 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD----------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 678 sppgVEGIVGLEQVSSLGDGPP--GGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd14919 521 ----VDRIIGLDQVAGMSETALpgAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLD 596
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14919 597 QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
119-829 |
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: 1088.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKD----QNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETL 357
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQdKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd15896 237 EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd15896 317 AQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd15896 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD----------------------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 678 sppgVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQL 757
Cdd:cd15896 528 ----VDRIVGLDKVSGMSEMPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQL 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743142585 758 RCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd15896 604 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
119-829 |
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: 1083.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvsYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI--------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETL 357
Cdd:cd14921 153 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDdEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsaercssai 677
Cdd:cd14921 473 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD----------------------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 678 sppgVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd14921 524 ----VDRIVGLDQMAKMTESSlpSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLE 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14921 600 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
108-829 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1062.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 108 EDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ 187
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 188 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNS 267
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSG------------SAGNVGRLEEQILQSNPILEAFGNAKTVRNNNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 268 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-P 346
Cdd:pfam00063 150 SRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTiD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 347 G-QERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLT 425
Cdd:pfam00063 230 GiDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 426 PRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQG 585
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 586 GHPKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggfqqfsflgsfPPS 665
Cdd:pfam00063 467 KHPHFQKPR-LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDY-------------ETA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 666 PPGSAERCSSAISPPGvegivgleqvsslgdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRA 745
Cdd:pfam00063 533 ESAAANESGKSTPKRT----------------------KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRA 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 746 GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSK 825
Cdd:pfam00063 591 GVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTK 670
|
....
gi 1743142585 826 IFFR 829
Cdd:pfam00063 671 IFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
100-841 |
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: 988.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 100 NPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTE 179
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 180 GAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstvsyGELERQLLQANPILEAFGNA 259
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV--------------GSVEDQILESNPILEAFGNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 260 KTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT 339
Cdd:smart00242 147 KTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 340 NGPSSS-PGQE-RELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNT-AAQKLCRLLGLGV 416
Cdd:smart00242 227 QGGCLTvDGIDdAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 417 TDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLN 496
Cdd:smart00242 307 EELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 497 SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSF 576
Cdd:smart00242 386 SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 577 VEKVAQEQGGHPKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggfqqf 656
Cdd:smart00242 463 LEKLNQHHKKHPHFSKPK-KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 657 sflgsfppsppgsaercssaisppgvegivgLEQVSSLGdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRC 736
Cdd:smart00242 535 -------------------------------VSNAGSKK-----------RFQTVGSQFKEQLNELMDTLNSTNPHFIRC 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 737 IVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDP 816
Cdd:smart00242 573 IKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDE 652
|
730 740
....*....|....*....|....*
gi 1743142585 817 NLYRVGQSKIFFRAGVLAQLEEERD 841
Cdd:smart00242 653 DEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
98-1216 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 909.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 98 RMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAV 177
Cdd:COG5022 59 RIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 178 TEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvSTVSYGELERQLLQANPILEAFG 257
Cdd:COG5022 139 AEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSS-------------STVEISSIEKQILATNPILEAFG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 258 NAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRF 337
Cdd:COG5022 206 NAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 338 LTNGPSSSPGQ--ERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQKLCRLLGLG 415
Cdd:COG5022 286 LSQGGCDKIDGidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGID 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 416 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQL 495
Cdd:COG5022 365 PSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 496 NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpANPPGLLALLDEECWFPKATDKS 575
Cdd:COG5022 444 NSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDES 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 576 FVEKVAQ--EQGGHPKFQRPRhLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggf 653
Cdd:COG5022 522 FTSKLAQrlNKNSNPKFKKSR-FRDNK-FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE---- 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 654 qqfsflgsfppsppgsaercssaisppgvegivglEQVSSLGdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSF 733
Cdd:COG5022 596 -----------------------------------ENIESKG-----------RFPTLGSRFKESLNSLMSTLNSTQPHY 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 734 VRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA----IPKGFMDGKQACEKMI 809
Cdd:COG5022 630 IRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSIL 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 810 QALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVSFQAAARGYLARRAFQKRQQQQSALRVMQRNCAAYLKLRH 889
Cdd:COG5022 710 EELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDY 789
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 890 WQWWRLFTKVKPLLQVTRQDEVLQARAQELQKVQ-ELQQQsaREVRELQgrvaqlEEERARLAEQLRAEAELCaeaeetr 968
Cdd:COG5022 790 ELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQkTIKRE--KKLRETE------EVEFSLKAEVLIQKFGRS------- 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 969 grLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELeahleaeegARQKLQLEKVTTEAKmKKFEEDLLL- 1047
Cdd:COG5022 855 --LKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSL---------KLVNLELESEIIELK-KSLSSDLIEn 922
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1048 LEDQNSKLSKERKLLEDRlaEFSSQAAEEEEKVKSLNKLRL---KYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSE 1124
Cdd:COG5022 923 LEFKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEvesKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKE 1000
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1125 LQEQMVEQQ--QRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSlreaqaALAEAQEDLEAERV-ARTKAEKQRRD 1201
Cdd:COG5022 1001 LAELSKQYGalQESTKQLKELPVEVAELQSASKIISSESTELSILKPL------QKLKGLLLLENNQLqARYKALKLRRE 1074
|
1130
....*....|....*
gi 1743142585 1202 LGEELEALRGELEDT 1216
Cdd:COG5022 1075 NSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
119-829 |
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: 827.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA---------SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-----PGQE-RE 351
Cdd:cd00124 152 FDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSgcdriDGVDdAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 352 LFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNI--ALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd00124 232 EFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIefEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ-GASFLGILDIAGFEIFQLNSFEQLCINYTNE 508
Cdd:cd00124 312 VGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 509 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHP 588
Cdd:cd00124 392 KLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 589 KFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTdrltaeiwkdehggfqQFsflgsfppsppg 668
Cdd:cd00124 469 RFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS----------------QF------------ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 669 saercssaisppgvegivgleqvsslgdgppggrprrgmfrtvgqlyKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKL 748
Cdd:cd00124 520 -----------------------------------------------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLF 552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 749 EPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFF 828
Cdd:cd00124 553 DPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFL 632
|
.
gi 1743142585 829 R 829
Cdd:cd00124 633 R 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
119-829 |
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: 767.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKA--QFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYdYHFCSQGVTTVDNmDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14927 319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14927 397 HHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 595 ---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsFLGSFPPSPP--GS 669
Cdd:cd14927 474 pdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEN---------YVGSDSTEDPksGV 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 670 AERCSSAISppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 749
Cdd:cd14927 545 KEKRKKAAS-----------------------------FQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMD 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 750 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK-GFMDGKQACEKMIQALELDPNLYRVGQSKIFF 828
Cdd:cd14927 596 PFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFF 675
|
.
gi 1743142585 829 R 829
Cdd:cd14927 676 K 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
120-829 |
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: 742.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdLAKKKDSKMK--------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQE 355
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVASiDDAEELLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 356 TLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd14913 234 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 513
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 514 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQR 592
Cdd:cd14913 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 593 PRHLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggFQQFSFLGSFPPSPPGSA 670
Cdd:cd14913 468 PKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHL-------YATFATADADSGKKKVAK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 671 ERCSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEP 750
Cdd:cd14913 541 KKGSS--------------------------------FQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEH 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 751 RLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14913 589 SLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
119-829 |
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: 730.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpasvsTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEA--------AKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPCSHYRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14909 153 GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNvDDGEEFSLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14909 233 DQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14909 313 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRH 595
Cdd:cd14909 392 HMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 596 LR---DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGgfqqfsflgsfPPSPPGSAEr 672
Cdd:cd14909 469 PKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-----------QSGGGEQAK- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 673 cssaisppGVEGIVGleqvsslgdgppggrprrGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14909 537 --------GGRGKKG------------------GGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHL 590
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743142585 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14909 591 VMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
119-829 |
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: 701.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvpasVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGK----------QSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQER-ELFQET 356
Cdd:cd14934 151 GTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPnPKEYHWVSQGVTVVDNMDDgEELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRH 595
Cdd:cd14934 390 HMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 596 LRD---QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGgfqqfsflgsfpPSPPGSAER 672
Cdd:cd14934 467 GKGkgpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEA------------PAGSKKQKR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 673 CSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14934 535 GSS--------------------------------FMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHL 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743142585 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14934 583 IMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
120-829 |
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: 691.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSG-LIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSpkgrkepgvpASVSTvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS----------SSGET----QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELFQET 356
Cdd:cd01380 148 DKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPViDGvDDAAEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 516 HTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK--FQRP 593
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 594 RhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdehggfqqfsflgsfppsppgsaerc 673
Cdd:cd01380 464 R--FSNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK-------------------------------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 674 ssaisppgvegivgleqvsslgdgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 753
Cdd:cd01380 510 -----------------------------------KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRV 554
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 754 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01380 555 VQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
120-829 |
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: 686.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14917 156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14917 315 KGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14917 393 HHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 595 HLRD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsFLGSFPP--SPPGSA 670
Cdd:cd14917 470 NIKGkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAPieKGKGKA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 671 ERCSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEP 750
Cdd:cd14917 541 KKGSS--------------------------------FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDN 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 751 RLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14917 589 PLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
119-829 |
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: 679.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGA-----------LEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14929 150 GARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESlDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14929 310 SQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRH 595
Cdd:cd14929 388 HMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 596 LRD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggFQQFSFLGSfpPSPPGSAERC 673
Cdd:cd14929 465 DKKkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASL-------FENYISTDS--AIQFGEKKRK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 674 SSAisppgvegivgleqvsslgdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 753
Cdd:cd14929 536 KGA------------------------------SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLV 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743142585 754 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14929 586 LQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
121-829 |
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: 670.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 121 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 200
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 201 GAGKTENTKKVIQYLAHVASSPKGRKEPgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 280
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEE------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 281 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLE 358
Cdd:cd14918 157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 359 SLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14918 237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRH 595
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 596 LRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdehggfqqfsflgsfppSPPGSAERC 673
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF------------------STYASAEAD 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 674 SSAISPPGVEGivgleqvsslgdgppggrprrGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 753
Cdd:cd14918 533 SGAKKGAKKKG---------------------SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELV 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743142585 754 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14918 592 LHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
120-829 |
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: 669.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVAS-SPKGRKEpgvpasVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKE------NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14916 156 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 435
Cdd:cd14916 236 DSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 436 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd14916 315 TKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 515 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP 593
Cdd:cd14916 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 594 RHL--RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGgfqqfsflgsfppsppgsae 671
Cdd:cd14916 470 RNVkgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS-------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 672 rcssAISPPGVEGIVGLEQVSSlgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd14916 530 ----ADTGDSGKGKGGKKKGSS--------------FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNP 591
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743142585 752 LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14916 592 LVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
120-829 |
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: 667.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETL 357
Cdd:cd14912 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14912 238 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14912 317 KGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPR 594
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 595 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdehgGFQQFSFLGSFPPSPPGSAER 672
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFS----GAQTAEGASAGGGAKKGGKKK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 673 CSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14912 548 GSS--------------------------------FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHEL 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14912 596 VLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
120-829 |
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: 662.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14910 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14910 238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14910 317 KGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 595 HLRD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdehggfqqfsflgsfppsppgSAER 672
Cdd:cd14910 472 PAKGkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF----------------------SGAA 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 673 CSSAISPPGVEGivGLEQVSSlgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14910 530 AAEAEEGGGKKG--GKKKGSS--------------FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHEL 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14910 594 VLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
120-829 |
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: 657.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14915 158 ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYdFAFVSQGEITVPSiDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14915 238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14915 317 KGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14915 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 595 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQStdrltaeiwkdehgGFQQFSFLgsfppsppGSAER 672
Cdd:cd14915 472 PAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKS--------------GMKTLAFL--------FSGGQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 673 CSSAISPPGVEGivGLEQVSSlgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 752
Cdd:cd14915 530 TAEAEGGGGKKG--GKKKGSS--------------FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHEL 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 753 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14915 594 VLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
120-829 |
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: 653.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGvPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQ-PGKMQ----GTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------EREL 352
Cdd:cd14923 157 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDF----PFVSQGEvtvasidDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 353 FQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVG 431
Cdd:cd14923 232 LLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 432 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKL 510
Cdd:cd14923 311 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 511 QQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPK 589
Cdd:cd14923 389 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 590 FQRPRHLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTaeiwkdehggfqqfsflgSFPPSPP 667
Cdd:cd14923 466 FQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLL------------------SFLFSNY 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 668 GSAERCSSAISPPGvegivGLEQVSSlgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGK 747
Cdd:cd14923 528 AGAEAGDSGGSKKG-----GKKKGSS--------------FQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGV 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 748 LEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKI 826
Cdd:cd14923 589 MDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKV 668
|
...
gi 1743142585 827 FFR 829
Cdd:cd14923 669 FFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
120-829 |
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: 631.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVasSPKGrkepgvPASVSTVSygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV--SGGS------ESEVERVK-----DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd01378 149 FKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGiDDAADFKEVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG---RDY 434
Cdd:cd01378 229 NAMKVIGFTEEEQDSIFRILAAILHLGNIQFA-EDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd01378 308 YEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 515 nhTMFVL--EQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd01378 388 --IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 592 RPR-HLRD-QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfpPSPPGS 669
Cdd:cd01378 463 CPSgHFELrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE---------------GVDLDS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 670 AERcssaisPPgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 749
Cdd:cd01378 528 KKR------PP-----------------------------TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFD 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 750 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01378 573 EELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
120-829 |
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: 618.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRgkKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-----------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETL 357
Cdd:cd01383 143 AAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNClTIDGvDDAKKFHELK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd01383 223 EALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd01383 303 KLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 518 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRprhlR 597
Cdd:cd01383 383 LFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----E 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGGFQQfsflgsfpPSPPGSAERCSSai 677
Cdd:cd01383 456 RGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRK--------ALPLTKASGSDS-- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 678 sppgvegivgleqvsslgdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQL 757
Cdd:cd01383 526 -----------------------------QKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQL 576
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743142585 758 RCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01383 577 RCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
120-829 |
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: 616.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVASSPKgrkepgvpasvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-----------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGE--QLKADLLLEPCSHYRFLT-NGPSSSPG-QERELFQE 355
Cdd:cd14883 145 ASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNiNDKKDFDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 356 TLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKR-ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRsPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd14883 305 TEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNP-GQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 515 NHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPR 594
Cdd:cd14883 384 NHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 595 HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdehggfqqfsflgsfppsPPGSAERCS 674
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFT------------------YPDLLALTG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 675 SAISPPGVEGIVGLEQVSSlgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVL 754
Cdd:cd14883 523 LSISLGGDTTSRGTSKGKP----------------TVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVL 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743142585 755 DQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14883 587 AQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
119-829 |
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: 591.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVAsspkGRKepgvpasvSTVsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS----GQH--------SWI-----EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPGQ-ERELFQET 356
Cdd:cd01381 144 NKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNClTCEGRdDAAEFADI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALK-RER-NTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd01381 224 RSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEaTVVdNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGET 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS--FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 512
Cdd:cd01381 304 VVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 513 LFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLI-ERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd01381 384 FFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 592 RPRHlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHggfqqfsflgsfppsPPGSAE 671
Cdd:cd01381 460 KPKS-DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI---------------SMGSET 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 672 RCSSAisppgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd01381 524 RKKSP---------------------------------TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRE 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 752 LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01381 571 LCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
119-829 |
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: 588.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAHVAsspkGRKEPGVpASVstvsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEG-RSV--------EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG--QERELFQE 355
Cdd:cd01384 148 FDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDgvDDAEEYRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 356 TLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTpRIKVGR 432
Cdd:cd01384 228 TRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIVTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 433 D-YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQ 511
Cdd:cd01384 307 DgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 512 QLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 592 RPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsflgsFPPSPPGSAE 671
Cdd:cd01384 463 KPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGL----------------FPPLPREGTS 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 672 RCSSaisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd01384 525 SSSK--------------------------------FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENA 572
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 752 LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 829
Cdd:cd01384 573 NVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
119-829 |
5.57e-176 |
|
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: 550.70 E-value: 5.57e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGS----------------GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPcshyrfLTNGPSSspgqerelFQETL 357
Cdd:cd01382 145 FNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDP------LLDDVGD--------FIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQA-TMPDNTAAQKL---CRLLGLGVTDF-----SRALLTPRI 428
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 429 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSprqgASFLGILDIAGFEIFQLNSFEQLCINYT 506
Cdd:cd01382 291 GAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIpfETS----SYFIGVLDIAGFEYFEVNSFEQFCINYC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 507 NEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGG 586
Cdd:cd01382 367 NEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 587 HPKFQRPR------H--LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsf 658
Cdd:cd01382 444 HFRLSIPRksklkiHrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSL------------- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 659 lgsFPPSPPGSAERCSSAisppgvegivgleqvsslgdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIV 738
Cdd:cd01382 511 ---FESSTNNNKDSKQKA---------------------------GKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIK 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 739 PNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNL 818
Cdd:cd01382 561 PNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNEND 638
|
730
....*....|.
gi 1743142585 819 YRVGQSKIFFR 829
Cdd:cd01382 639 FKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
119-829 |
5.21e-174 |
|
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: 545.91 E-value: 5.21e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ----DREDQS 193
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 194 ILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTVS--YGELERQLLQANPILEAFGNAKTVKNDNSSRFG 271
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 272 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-R 350
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDdA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 351 ELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATmpDNTAAQKL---CRLLGLGVTDFSRALLTPR 427
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLklaAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 428 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 507
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-SPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 508 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIE-RPANPPGLLALLDeECWFPKAT--DKSFV------- 577
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVsqlhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 578 ------EKVAQEQGGHPKFQRPRHLRDQaDFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdehg 651
Cdd:cd14890 476 grksgsGGTRRGSSQHPHFVHPKFDADK-QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR------------ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 652 gfqqfsflgsfppsppgsaercssaisppgvegivGLEQVSslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNP 731
Cdd:cd14890 543 -----------------------------------SIREVS------------------VGAQFRTQLQELMAKISLTNP 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 732 SFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAipkgfMDGKQACEKMIQA 811
Cdd:cd14890 570 RYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKM 644
|
730
....*....|....*...
gi 1743142585 812 LELDPNLYRVGQSKIFFR 829
Cdd:cd14890 645 LGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
119-829 |
3.27e-170 |
|
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: 535.13 E-value: 3.27e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-----------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAgeqlkadlllEPCSHYRFLTNGPSSSPGQEREL------ 352
Cdd:cd14872 144 DNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP----------DPASRGGWGSSAAYGYLSLSGCIevegvd 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 353 ----FQETLESLRVLGFTHEEIISMLRMVSAVLQFGNI---ALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLT 425
Cdd:cd14872 214 dvadFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIefaSGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 426 PRIKV-GRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCIN 504
Cdd:cd14872 294 RLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCIN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 505 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQ 584
Cdd:cd14872 374 FTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 585 GGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsflgsFPP 664
Cdd:cd14872 451 AAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVL----------------FPP 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 665 SPPGSAERcssaisppgvegivgleQVsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKR 744
Cdd:cd14872 515 SEGDQKTS-----------------KV------------------TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 745 AGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtPNAIPKGFM-DGKQACEKMIQALELDPNLYRVGQ 823
Cdd:cd14872 560 ARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGK 638
|
....*.
gi 1743142585 824 SKIFFR 829
Cdd:cd14872 639 TRVLYR 644
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
120-829 |
1.33e-162 |
|
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: 513.75 E-value: 1.33e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVASSPkgrkepgvpasvstvsYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKAN----------------NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPCSHYRFLTNGPSSSPGQE-----RELF 353
Cdd:cd01379 146 STGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVnnsgnREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 354 QETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQ----ATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 507
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 508 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCID-LIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGG 586
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 587 HPkFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTaeiwkdehggfQQfsflgsfppsp 666
Cdd:cd01379 462 KY-YWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-----------RQ----------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 667 pgsaercssaisppgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAG 746
Cdd:cd01379 517 -------------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAG 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 747 KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDgKQACEKMIQALELDPnlYRVGQSKI 826
Cdd:cd01379 554 KFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKV 630
|
...
gi 1743142585 827 FFR 829
Cdd:cd01379 631 FLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
119-829 |
9.94e-162 |
|
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: 512.38 E-value: 9.94e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPkgrkepgvPASVStvsygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVT--------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS-SPGQ-ERELFQET 356
Cdd:cd01387 145 E-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCeIAGKsDADDFRRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTD-QATMPDNTAA--QKLCRLLGLGVTDFSRALLTPRIKVGRD 433
Cdd:cd01387 224 LAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAeiQWVAHLLQISPEGLQKALTFKVTETRRE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNrALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 513
Cdd:cd01387 304 RIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 514 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRP 593
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAFA-DNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 594 RhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGGFQQfsflgsfppSPPGSAERC 673
Cdd:cd01387 460 R--MPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDK---------APPRLGKGR 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 674 SSAISPPGvegivgleqvsslgdgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 753
Cdd:cd01387 529 FVTMKPRT---------------------------PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVV 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743142585 754 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGfMDGKQACEKMIQALELDP-NLYRVGQSKIFFR 829
Cdd:cd01387 582 MAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
119-829 |
5.62e-161 |
|
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: 511.54 E-value: 5.62e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLahVASSPKGrkepgvpasvstvsYGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG--------------YGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGQERELFQE 355
Cdd:cd01385 145 YRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCYTLEGEDEKYEFER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 356 TLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRER-NTDQATMPDNTAAQKL-CRLLGLGVTDFSRALLTPRIKVGRD 433
Cdd:cd01385 225 LKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASfLGILDIAGFEIFQLNSFEQLCINYTNEK 509
Cdd:cd01385 305 TLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEH 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 510 LQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK 589
Cdd:cd01385 384 LQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 590 FQRPRhLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEHGGFQQFSFLGSFPPSPPGS 669
Cdd:cd01385 461 YEKPQ-VMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 670 AERCSSAIS-PPGVEGIVGLEQVSSLGDGPPGGRPRrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKL 748
Cdd:cd01385 539 REAGRRRAQrTAGHSLTLHDRTTKSLLHLHKKKKPP-----SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRF 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 749 EPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFF 828
Cdd:cd01385 614 DDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFL 689
|
.
gi 1743142585 829 R 829
Cdd:cd01385 690 K 690
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
119-829 |
2.22e-158 |
|
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: 502.30 E-value: 2.22e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKK-RHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD----------------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-------- 349
Cdd:cd14897 145 FTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNdseeleyy 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 350 RELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd14897 225 RQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:cd14897 305 IRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQG 585
Cdd:cd14897 385 SNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 586 GHPKFQRPRHlrDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsFLGSFpps 665
Cdd:cd14897 462 ESPRYVASPG--NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDL------------FTSYF--- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 666 ppgsaercssaisppgvegivgleqvsslgdgppggrprrgmfrtvgqlyKESLSRLMATLSNTNPSFVRCIVPNHEKRA 745
Cdd:cd14897 525 --------------------------------------------------KRSLSDLMTKLNSADPLFVRCIKPNNFLRP 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 746 GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSK 825
Cdd:cd14897 555 NKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTK 631
|
....
gi 1743142585 826 IFFR 829
Cdd:cd14897 632 VFLK 635
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
119-829 |
2.61e-158 |
|
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: 502.77 E-value: 2.61e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvSTVsygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLND----------STI------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLggAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQE 355
Cdd:cd14903 145 FDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGmSDRKHFAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 356 TLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATM--PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRD 433
Cdd:cd14903 223 TKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 513
Cdd:cd14903 303 VYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 514 FNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAqeqGGHPKFQR- 592
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDv 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 593 ---PRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdehggfqqfsfLGSFPPSPPGS 669
Cdd:cd14903 455 iefPRTSRTQ--FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK-----------EKVESPAAAST 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 670 AERCSSAISppgvegivgleQVSSLGDgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 749
Cdd:cd14903 522 SLARGARRR-----------RGGALTT------------TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELD 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 750 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAiPKGFMDGKQACEKMIQALELD-PNLYRVGQSKIFF 828
Cdd:cd14903 579 HLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYF 657
|
.
gi 1743142585 829 R 829
Cdd:cd14903 658 Q 658
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
119-827 |
6.12e-158 |
|
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: 502.01 E-value: 6.12e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY------RGKKRHEVPPHVYAVTEGAYRSMLQDRE-- 190
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 191 --DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNSS 268
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQ--------NATERENVRDRVLESNPILEAFGNARTNRNNNSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 269 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngpSSSPGQ 348
Cdd:cd14901 153 RFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL----NSSQCY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 349 ER-------ELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIA-LKRERNTDQATMPDNTAAQKLCRLLGLGVTDFS 420
Cdd:cd14901 229 DRrdgvddsVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 421 RALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS-FLGILDIAGFEIFQLNSFE 499
Cdd:cd14901 309 KTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 500 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEK 579
Cdd:cd14901 389 QLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 580 VAQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTdrltaeiwkdehggfqqFSFL 659
Cdd:cd14901 466 YYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSS-----------------NAFL 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 660 GSfppsppgsaercssaisppgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVP 739
Cdd:cd14901 529 SS------------------------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKP 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 740 NHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQA------LE 813
Cdd:cd14901 561 NDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIE 640
|
730
....*....|....
gi 1743142585 814 LDPNLYrVGQSKIF 827
Cdd:cd14901 641 HLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
119-829 |
2.52e-154 |
|
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: 491.62 E-value: 2.52e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVstvsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCV--------EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQE 355
Cdd:cd14873 153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTiSDQESFRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 356 TLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKrerNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 435
Cdd:cd14873 233 VITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 436 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14873 310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 516 HTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 595
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 596 LRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQStdrltaeiwkdehggfqQFSFLGSFppsppgsaercss 675
Cdd:cd14873 464 AVNN--FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRES-----------------RFDFIYDL------------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 676 aisppgvegivgLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 755
Cdd:cd14873 512 ------------FEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLN 579
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 756 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKqaCEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14873 580 QLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
119-791 |
2.54e-153 |
|
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: 489.59 E-value: 2.54e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvSTVsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKR--------SLV-----EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FD---------VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQL----------------------LGGAGEQLKAD 326
Cdd:cd14888 147 FSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLcaaareakntglsyeendeklaKGADAKPISID 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 327 LLL-EPCSHYRFLT-NGPSSSPG-QERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNT 403
Cdd:cd14888 227 MSSfEPHLKFRYLTkSSCHELPDvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSAS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 404 AAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS 480
Cdd:cd14888 307 CTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 481 FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLA 560
Cdd:cd14888 387 FCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 561 LLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDR 640
Cdd:cd14888 464 MLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 641 LTAEIWKdehggfqqfSFLGSFPPSPPgsaercssaisppgvegivgleqvsslgdgppggrpRRGMFRTVGQLYKESLS 720
Cdd:cd14888 542 FISNLFS---------AYLRRGTDGNT------------------------------------KKKKFVTVSSEFRNQLD 576
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743142585 721 RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 791
Cdd:cd14888 577 VLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
119-829 |
3.94e-151 |
|
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: 483.11 E-value: 3.94e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEV---PPHVYAVTEGAYRSMLQDR----ED 191
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 192 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTvsygELERQLLQANPILEAFGNAKTVKNDNSSRFG 271
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHE----SIEECVLLSNLILEAFGNAKTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 272 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PGQER 350
Cdd:cd14892 157 KYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEvDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 351 EL-FQETLESLRVLGFTHEEIISMLRMVSAVLQFGNiaLKRERNTDQATMP----DNTAAQKLCRLLGLGVTDFSRALLT 425
Cdd:cd14892 237 ATeFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVFaqsaDGVNVAKAAGLLGVDAAELMFKLVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 426 PRIKVGRDYV-QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ---------GASFLGILDIAGFEIFQL 495
Cdd:cd14892 315 QTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 496 NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFP-KATDK 574
Cdd:cd14892 395 NSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 575 SFVEKVAQEQ-GGHPKFQRPRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdehggf 653
Cdd:cd14892 472 QLLTIYHQTHlDKHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 654 qqfsflgsfppsppgsaercssaisppgvegivgleqvsslgdgppggrprrgmFRTvgqlykeSLSRLMATLSNTNPSF 733
Cdd:cd14892 536 ------------------------------------------------------FRT-------QLAELMEVLWSTTPSY 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 734 VRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN-AIPKGFMDGKQACEKM---- 808
Cdd:cd14892 555 IKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkce 634
|
730 740
....*....|....*....|..
gi 1743142585 809 -IQALELDPNLYRVGQSKIFFR 829
Cdd:cd14892 635 eIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
119-829 |
4.99e-148 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 474.90 E-value: 4.99e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH--------EVPPHVYAVTEGAYRSMLQDR 189
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 190 EDQSILCTGESGAGKTENTKKVIQYL------AHVASSPKGRKEPGVPASVSTVSygeLERQLLQANPILEAFGNAKTVK 263
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsqqEQNSEEVLTLTSSIRATSKSTKS---IEQKILSCNPILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 264 NDNSSRFGKFIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYRFLTNG 341
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 342 PSSSPGQER----ELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALK-RERNTDQATMPDNTAA-QKLCRLLGLG 415
Cdd:cd14907 238 KSNCYEVDTindeKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 416 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL------DRSPRQGASF-LGILDIA 488
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 489 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTF--LDFgLDLQPCIDLIERPanPPGLLALLDEEC 566
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKP--PIGIFNLLDDSC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 567 WFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIW 646
Cdd:cd14907 475 KLATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 647 KDEHGGFQQFSflgsfppsppgsaercssaisppgvegivGLEQVSSLGDgppggrprrgmfRTVGQLYKESLSRLMATL 726
Cdd:cd14907 554 SGEDGSQQQNQ-----------------------------SKQKKSQKKD------------KFLGSKFRNQMKQLMNEL 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 727 SNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNaipkgfmdgkqace 806
Cdd:cd14907 593 MQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN-------------- 658
|
730 740
....*....|....*....|...
gi 1743142585 807 kmiqaleldpnlYRVGQSKIFFR 829
Cdd:cd14907 659 ------------VLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
121-829 |
1.07e-139 |
|
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: 451.28 E-value: 1.07e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 121 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSML----QDREDQSILC 196
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 197 TGESGAGKTENTKKVIQYLAHVAsspKGRKEpgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 276
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNSQ--------------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 277 NFDvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPcSHYRFLTN--GPSSSPGQERELF 353
Cdd:cd14889 146 RFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNgaGCKREVQYWKKKY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 354 QETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALkrERNTDQA---TMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKV 430
Cdd:cd14889 224 DEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEAlkvENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 431 GRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASF----LGILDIAGFEIFQLNSFEQLCINYT 506
Cdd:cd14889 302 RGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVelreIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 507 NEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIerPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGG 586
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 587 HPKFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTdrltaeiwkdehggfqqfsflgsfppSP 666
Cdd:cd14889 457 NSYYGKSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSA--------------------------TP 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 667 PGSAERCSSAISPPGVEGIVGLEQVSSLGDGPPGGrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAG 746
Cdd:cd14889 509 LLSVLFTATRSRTGTLMPRAKLPQAGSDNFNSTRK-------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPG 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 747 KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL--TPNaIPKgfmdGKQACEKMIQALELDPnlYRVGQS 824
Cdd:cd14889 582 QLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKT 654
|
....*
gi 1743142585 825 KIFFR 829
Cdd:cd14889 655 RLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
120-789 |
1.53e-134 |
|
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: 435.50 E-value: 1.53e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMY-----------RGKKRHEVPPHVYAVTEGAYRSM-- 185
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 186 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgVPASVSTVSYGE-LERQLLQANPILEAFGNAKTV 262
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNN-------LAASVSMGKSTSgIAAKVLQTNILLESFGNARTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 263 KNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKAdlllepcshyrfltngp 342
Cdd:cd14900 155 RNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK----------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 343 ssspgqeRELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTD-QATMPDNTAAQKL------CRLLGLG 415
Cdd:cd14900 218 -------RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 416 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGAS-FLGILDIAGFE 491
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 492 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKA 571
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 572 TDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDplndnvaaLLHQstdrltaeiwkdehg 651
Cdd:cd14900 448 SDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQ--------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 652 gfqqfsflgsfppsppgsaercssaisppgvegivglEQVSslgdgppggrprrgMFRTVGQlYKESLSRLMATLSNTNP 731
Cdd:cd14900 505 -------------------------------------EAVD--------------LFVYGLQ-FKEQLTTLLETLQQTNP 532
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 732 SFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 789
Cdd:cd14900 533 HYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
119-829 |
8.84e-132 |
|
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: 428.98 E-value: 8.84e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAHVASspkGRKEpgvpasvSTVSygelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKD-------KTIA------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS--PG-QERELFQ 354
Cdd:cd14904 145 FDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMqiPGlDDAKLFA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 355 ETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd14904 225 STQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFD-KSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd14904 304 VTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 515 NHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKV---AQEQGGHPKFQ 591
Cdd:cd14904 384 TTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESID 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 592 RPRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdehggfqqfsflgsfppsppGSAE 671
Cdd:cd14904 460 FPKVKRTQ--FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF---------------------GSSE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 672 -RCSSAISPPGvegivgleqvsslgdgppggrPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEP 750
Cdd:cd14904 517 aPSETKEGKSG---------------------KGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDK 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 751 RLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGfmDGKQACEKMIQAL-ELDPNLYRVGQSKIFFR 829
Cdd:cd14904 576 RMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
119-829 |
2.40e-129 |
|
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: 421.76 E-value: 2.40e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERyySGLI----YTYSGLFCVVINPYKQLPiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE---D 191
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 192 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTVSYG--ELERQLLQANPILEAFGNAKTVKNDNSSR 269
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSvtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 270 FGKFIRINFDVAGY-IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSSPG 347
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 348 -QERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKrERNTDQ-----ATMPDNTAAQKLCRLLGLGVTDFSR 421
Cdd:cd14891 236 iDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFD-EEDTSEgeaeiASESDKEALATAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 422 ALLTPRIkVGRDYVQKAQ-TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRqGASFLGILDIAGFEIFQL-NSFE 499
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-PLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 500 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIpwtflDFGLDLQP----CIDLIErpANPPGLLALLDEECWFPKATDKS 575
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGI-----DVGVITWPdnreCLDLIA--SKPNGILPLLDNEARNPNPSDAK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 576 FVEKVAQEQGGHPKFQRPrHLRDQAD-FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQStdrltaeiwkdehggfQ 654
Cdd:cd14891 466 LNETLHKTHKRHPCFPRP-HPKDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------A 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 655 QFSflgsfppsppgsaercssaisppgvegivglEQVSSLGDgppggrprrgmfrtvgqlykeslsrlmaTLSNTNPSFV 734
Cdd:cd14891 529 KFS-------------------------------DQMQELVD----------------------------TLEATRCNFI 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 735 RCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQA-CEKMIQALE 813
Cdd:cd14891 550 RCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFR 629
|
730
....*....|....*.
gi 1743142585 814 LDPNLYRVGQSKIFFR 829
Cdd:cd14891 630 VPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
119-791 |
1.27e-126 |
|
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: 416.60 E-value: 1.27e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYR--------GKKRHEVPPHVYAVTEGAYRSMLQ-D 188
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 189 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASvstvsygELERQLLQANPILEAFGNAKTVKNDNSS 268
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAV-------EIGKRILQTNPILESFGNAQTIRNDNSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 269 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG 347
Cdd:cd14902 154 RFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnSYGPSFARK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 348 QER-----ELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKL---CRLLGLGVTDF 419
Cdd:cd14902 234 RAVadkyaQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 420 SRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--------RSPRQGASFLGILDIAGFE 491
Cdd:cd14902 314 ETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 492 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKA 571
Cdd:cd14902 394 SLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 572 TDKSFVEKVAQEQGGhpkfqrprhlRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehg 651
Cdd:cd14902 471 SNQALSTKFYRYHGG----------LGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAI------ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 652 gfqqfsflgsfppsppGSAERCSSAISPPGVEGivgleqvsslgdgppggRPRRGMFRT--VGQLYKESLSRLMATLSNT 729
Cdd:cd14902 533 ----------------GADENRDSPGADNGAAG-----------------RRRYSMLRApsVSAQFKSQLDRLIVQIGRT 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743142585 730 NPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 791
Cdd:cd14902 580 EAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
119-829 |
4.40e-124 |
|
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: 408.14 E-value: 4.40e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR--GKKRHE-------VPPHVYAVTEGAYRSMLQD- 188
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 189 REDQSILCTGESGAGKTENTKKVIQYLAHVasspkGRKEPGVPASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSS 268
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTL-----GNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 269 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKA--------DLLLEPCSHYRFLTN 340
Cdd:cd14908 156 RFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 341 G--PSSSPGQERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQK----LCRLLGL 414
Cdd:cd14908 236 GgaPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 415 GVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIF 493
Cdd:cd14908 315 DVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 494 QLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFP-KAT 572
Cdd:cd14908 395 AHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 573 DKSFVEKV--------AQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLM-KNMDPLNdnvaallhqstdrLTA 643
Cdd:cd14908 472 DANYASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------LTA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 644 EIwkdehggfqqfsflgsfppsppgsaercssaisppgvegivgleqvsslgdgppggrprrgMFRTvGQLYKESLSRLM 723
Cdd:cd14908 539 DS-------------------------------------------------------------LFES-GQQFKAQLHSLI 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 724 ATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPnAIPKGFM---- 799
Cdd:cd14908 557 EMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsm 635
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1743142585 800 ---DGKQACEKMI----------QALELDPNL----YRVGQSKIFFR 829
Cdd:cd14908 636 erlDPQKLCVKKMckdlvkgvlsPAMVSMKNIpedtMQLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
117-875 |
2.68e-121 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 404.80 E-value: 2.68e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 117 NEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHE-VPPHVYAVTEGAYRSMLQDREDQSIL 195
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 196 CTGESGAGKTENTKKVIQYLAhvasspkgrkepgvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 275
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---------------SSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 276 INFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQ 354
Cdd:PTZ00014 253 LQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGiDDVKDFE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 355 ETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALK-RERN--TDQAT-MPDNTAA-QKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:PTZ00014 333 EVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEgKEEGglTDAAAiSDESLEVfNEACELLFLDYESLKKELTVKVTY 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNE 508
Cdd:PTZ00014 413 AGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE--PPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 509 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGGHP 588
Cdd:PTZ00014 491 MLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNP 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 589 KFQRPRhlRDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdehggfqqfsflgsfppspp 667
Cdd:PTZ00014 568 KYKPAK--VDSnKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE-------------------- 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 668 gsaercssaisppGVE---GIVGLEQVsslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKR 744
Cdd:PTZ00014 626 -------------GVEvekGKLAKGQL-------------------IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKK 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 745 AGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQS 824
Cdd:PTZ00014 674 PLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKT 753
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 825 KIFFR---AGVLAQLEEERDLKVTDIIVSFQAAARGYLARRAFQKR----QQQQSALR 875
Cdd:PTZ00014 754 MVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNikslVRIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
119-829 |
3.50e-119 |
|
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: 392.61 E-value: 3.50e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvstvsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR----------------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQET 356
Cdd:cd14896 145 Q-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACrlQGKEDAQDFEGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQ--ATMPDNTAAQKLCRLLGLGvTDFSRALLTPRIKV-GRD 433
Cdd:cd14896 224 LKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdRSPRQGASF--LGILDIAGFEIFQLNSFEQLCINYTNEKLQ 511
Cdd:cd14896 303 RVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWL-APPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 512 QLFNHTMFVLEQEEYQREGIPWTFLDfGLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 592 RPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggFQQFSFLGSFPPSPPGSAE 671
Cdd:cd14896 459 KPQ--LPLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSL-------FQEAEPQYGLGQGKPTLAS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 672 RcssaisppgvegivgleqvsslgdgppggrprrgmfrtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd14896 530 R------------------------------------------FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVG 567
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 752 LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTpNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14896 568 HVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
119-825 |
2.11e-118 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 392.81 E-value: 2.11e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDREDQSILC 196
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 197 TGESGAGKTENTKKVIQYLAHVASSPKGRKepgvpaSVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 276
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQN------NNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 277 NFDVAGYIV-GANIETYLLEKSR-AIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFL-------------TN 340
Cdd:cd14906 155 EFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 341 GPSSSPGQEREL---FQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQAT--MPDNTAA-QKLCRLLGL 414
Cdd:cd14906 235 NKNSNHNNKTESiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 415 GVTDFSRALLTPRIKV-GRDYVQ-KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR----------SPRQGASFL 482
Cdd:cd14906 315 IESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 483 GILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALL 562
Cdd:cd14906 395 GVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 563 DEECWFPKATDKSFVEKVAQEQGGHPK-FQRPrhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRL 641
Cdd:cd14906 472 DDECIMPKGSEQSLLEKYNKQYHNTNQyYQRT---LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 642 TAEIwkdehggFQQFSFlgsfppSPPGSAERCSSAIsppgvegivgleqvsslgdgppggrprrgmfrTVGQLYKESLSR 721
Cdd:cd14906 549 KKSL-------FQQQIT------STTNTTKKQTQSN--------------------------------TVSGQFLEQLNQ 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 722 LMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDG 801
Cdd:cd14906 584 LIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNP 663
|
730 740
....*....|....*....|....
gi 1743142585 802 KQACEKMIQALELDPNLYRVGQSK 825
Cdd:cd14906 664 KLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
119-827 |
1.54e-117 |
|
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: 388.19 E-value: 1.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAhvasspkgrkepgvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIn 277
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---------------SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 fDVA--GYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQ 354
Cdd:cd14876 145 -DVAseGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGiDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 355 ETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRErntDQATMPDntAA----------QKLCRLLGLGVTDFSRALL 424
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 425 TPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCI 503
Cdd:cd14876 299 VKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 504 NYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQE 583
Cdd:cd14876 377 NITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 584 QGGHPKFQRPRHLRDQaDFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD---EHGGFQQFSFLG 660
Cdd:cd14876 454 LKSNGKFKPAKVDSNI-NFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGvvvEKGKIAKGSLIG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 661 SfppsppgsaercssaisppgvegivgleqvsslgdgppggrprrgmfrtvgQLYKeSLSRLMATLSNTNPSFVRCIVPN 740
Cdd:cd14876 533 S---------------------------------------------------QFLK-QLESLMGLINSTEPHFIRCIKPN 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 741 HEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYR 820
Cdd:cd14876 561 ETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYA 640
|
....*..
gi 1743142585 821 VGQSKIF 827
Cdd:cd14876 641 IGKTMVF 647
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
120-790 |
2.62e-117 |
|
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: 389.31 E-value: 2.62e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPiyteaivEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQ----- 187
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 188 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGrkepGVPASVSTVSYGElerQLLQANPILEAFGNAKTVKND 265
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTA----TSSSKRRRAISGS---ELLSANPILESFGNARTLRND 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 266 NSSRFGKFIRINF-----DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFL 338
Cdd:cd14895 148 NSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 339 TNG---PSSSPGQERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNI--ALKRERNTDQ-------------ATMP 400
Cdd:cd14895 228 SGGqcyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVlfVASSEDEGEEdngaasapcrlasASPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 401 DNTAAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR---- 473
Cdd:cd14895 308 SLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 474 -SPRQGAS-----FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCID 547
Cdd:cd14895 388 lNPNKAANkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 548 LIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQAD--FSVLHYAGKVDYKANEWLMKNMDP 625
Cdd:cd14895 467 MLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 626 LNDNVAALLHQSTDRLTAEIWKdehggFQQFSFLGSFPPSPPGSAERCSSaisppgvegivgleqVSSLGdgppggrprr 705
Cdd:cd14895 543 PNAELFSVLGKTSDAHLRELFE-----FFKASESAELSLGQPKLRRRSSV---------------LSSVG---------- 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 706 gmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 785
Cdd:cd14895 593 -----IGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQ 667
|
....*
gi 1743142585 786 YEILT 790
Cdd:cd14895 668 YRLLV 672
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
119-829 |
1.01e-115 |
|
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: 384.35 E-value: 1.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstVSYGELErqllQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----------LSVEKLN----AALTVLEAFGNVRTALNGNATRFSQLFSLDF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPC--SHYRFLTngPSSSPGQEREL---F 353
Cdd:cd01386 146 DQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIV--PLQKPEDKQKAaaaF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 354 QETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRAL---------- 423
Cdd:cd01386 224 SKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpq 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 424 --LTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGfeiFQLN----- 496
Cdd:cd01386 304 qsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPG---FQNPahsgs 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 497 ----SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERP---ANPP---------GLLA 560
Cdd:cd01386 380 qrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLW 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 561 LLDEECWFPKATDKSFVEKV--AQEQGGHPKFQRPRHLRDQA-DFSVLHYAGK--VDYKANEWLMK-NMDPLNDNVAALL 634
Cdd:cd01386 460 LLDEEALYPGSSDDTFLERLfsHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 635 HQSTDRLTAeiwkdehggfqqfsflgsfppsppgsAERCSSAIsppgvegivgleQVsslgdgppggrprrgmfrtvgql 714
Cdd:cd01386 540 QESQKETAA--------------------------VKRKSPCL------------QI----------------------- 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 715 yKESLSRLMATLSNTNPSFVRCIVPNHEkrAGKLEPR--------------LVLDQLRCNGVLEGIRICRQGFPNRILFQ 780
Cdd:cd01386 559 -KFQVDALIDTLRRTGLHFVHCLLPQHN--AGKDERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLG 635
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 781 EFRQRYEILTPNAIPKGF-----MDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd01386 636 EFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
119-791 |
1.95e-107 |
|
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: 359.16 E-value: 1.95e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDRE--DQSI 194
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 195 LCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgvpASVSTVSYGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKF 273
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP---------TSWESHKIAErIEQRILNSNPVMEAFGNACTLRNNNSSRFGKF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 274 IRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngPSSSPGQERELF 353
Cdd:cd14880 152 IQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL---PNPERNLEEDCF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 354 QETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTA---AQKLCRLLGLGVTDFSRALLTPRIKV 430
Cdd:cd14880 229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 431 GRDYV--QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNE 508
Cdd:cd14880 309 GKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 509 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKS-FVEKVAQEQGGH 587
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 588 PKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggfqqfsflgsFPPSPp 667
Cdd:cd14880 466 PCLGHNK-LSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKL----------------FPANP- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 668 gsaeRCSSAISPPGVEGIVGLEQVSSlgdgppggrprrgmfrtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGK 747
Cdd:cd14880 528 ----EEKTQEEPSGQSRAPVLTVVSK---------------------FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQT 582
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1743142585 748 LEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 791
Cdd:cd14880 583 FLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
119-829 |
2.26e-106 |
|
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: 355.73 E-value: 2.26e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH-----EVPPHVYAVTEGAYRSMLQDREDQ 192
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 193 SILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 272
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST----------------SSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 273 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QER 350
Cdd:cd14886 145 FIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGiDDQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 351 ELFQETLESLRVLgFTHEEIISMLRMVSAVLQFGNIALKRERN--TDQATMPDNTAA-QKLCRLLGLGVTDFSRALLTPR 427
Cdd:cd14886 225 KEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 428 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQgasFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:cd14886 304 VVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfDADARP---WIGILDIYGFEFFERNTYEQLLINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAqeqg 585
Cdd:cd14886 381 ANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCK---- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 586 ghpkfqrpRHLRD---------QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdehggfqqf 656
Cdd:cd14886 454 --------SKIKNnsfipgkgsQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNK------------ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 657 sflgsfppsppgsaerCSSAISP--PGVEGivgleqvsslgdgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFV 734
Cdd:cd14886 514 ----------------AFSDIPNedGNMKG------------------------KFLGSTFQLSIDQLMKTLSATKSHFI 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 735 RCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT--PNAIPKGFMDGKQACEKMIQAL 812
Cdd:cd14886 554 RCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENL 633
|
730
....*....|....*..
gi 1743142585 813 ELDPNLYRVGQSKIFFR 829
Cdd:cd14886 634 GIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
119-829 |
3.94e-102 |
|
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: 344.10 E-value: 3.94e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYS-GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRG-KKRHEVPPHVYAVTEGAYRSM-LQDREDQSIL 195
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 196 CTGESGAGKTENTKKVIQYL---AHVASSPKGRKepgvpaSVSTvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGK 272
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQR------SIAD----KIDENLKWSNPVMESFGNARTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 273 FIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYR-------FLTNGPS 343
Cdd:cd14875 151 YIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKclnggntFVRRGVD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 344 SSPGQERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQKLCRLLGLGVTDFSRAL 423
Cdd:cd14875 231 GKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 424 LtprIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPR---QGASFLGILDIAGFEIFQLNSFEQ 500
Cdd:cd14875 310 L---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASIT--PQgdcSGCKYIGLLDIFGFENFTRNSFEQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 501 LCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKV 580
Cdd:cd14875 385 LCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 581 AQEQGG-HPKFQRPRH-LRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdehggfqqfSF 658
Cdd:cd14875 462 WDQWANkSPYFVLPKStIPNQ--FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTD-----------------EF 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 659 LGSFPPSPPGSAERCssaisppgvegivgleqvsslgdgppggrprrgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIV 738
Cdd:cd14875 523 IRTLLSTEKGLARRK-----------------------------------QTVAIRFQRQLTDLRTELESTETQFIRCIK 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 739 PNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGK--QACEKMIQALE--- 813
Cdd:cd14875 568 PNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrly 647
|
730
....*....|....*...
gi 1743142585 814 --LDPNlYRVGQSKIFFR 829
Cdd:cd14875 648 gwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
119-786 |
4.28e-98 |
|
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: 333.99 E-value: 4.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVP------------PHVYAVTEGAYRSM 185
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGY--AYDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 186 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVS-TVSYGELERQLLQANPILEAFGNAKTVKN 264
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPaSPSRTTIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 265 DNSSRFGKFIRINF-DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-----AGEQLKADLLLEPCSHYRFL 338
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 339 TNGPSSSPG---QERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIAL-----KRERNT--DQATMPDNTAA--- 405
Cdd:cd14899 239 NQSLCSKRRdgvKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 406 --QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP-------- 475
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQAsapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 476 ------RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLI 549
Cdd:cd14899 399 sdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 550 ERpaNPPGLLALLDEECWFPKATDKSFVEKVAQE---QGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPL 626
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 627 NDNVAALLHQSTDRLTaeiwkdehggfqQFSFLGSFPPSPPGSAErcssaisPPGVEGIVGLEQVSSLGDGppggrprrg 706
Cdd:cd14899 556 CESAAQLLAGSSNPLI------------QALAAGSNDEDANGDSE-------LDGFGGRTRRRAKSAIAAV--------- 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 707 mfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 786
Cdd:cd14899 608 ---SVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
120-793 |
8.39e-94 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 316.84 E-value: 8.39e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQlpIYTEAIVEMYRGKKRHeVPPHVYAVTEGAYRSMLQdREDQSILCTGE 199
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHvasspkgrkepgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-----------------RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 vaGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLlepcsHYRFLTnGPSSSPGQERELFQETLES 359
Cdd:cd14898 141 --GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTA-GNKESIVQLSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 360 LRVLGFTHEEIISMLRMvsAVLQFGNIALKRERNTdqaTMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 439
Cdd:cd14898 213 MKSLGIANFKSIEDCLL--GILYLGSIQFVNDGIL---KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 440 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSprqGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 519
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 520 VLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGhpkfqrprHLRDQ 599
Cdd:cd14898 365 RAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIKKYLNG--------FINTK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 600 AD--FSVLHYAGKVDYKANEWLMKNmdplndnvaallhqstdrltaeiwkdehggfqqfsflgsfppsppgsaeRCSSAI 677
Cdd:cd14898 433 ARdkIKVSHYAGDVEYDLRDFLDKN-------------------------------------------------REKGQL 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 678 SPPGVEGIVGLEQVSSLgdgppggrprrgmfrtvGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQL 757
Cdd:cd14898 464 LIFKNLLINDEGSKEDL-----------------VKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQL 526
|
650 660 670
....*....|....*....|....*....|....*.
gi 1743142585 758 RCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 793
Cdd:cd14898 527 AECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
119-829 |
1.03e-92 |
|
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: 318.52 E-value: 1.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYS--------GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE 190
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 191 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRF 270
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG------------LEARLLQSGPVLEAFGNAHTVLNANSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 271 GKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGgaGEQLKADLLLEPCSHYRFLT---------NG 341
Cdd:cd14887 149 GKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCN--AAVAAATQKSSAGEGDPESTdlrritaamKT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 342 PSSSPGQERELFQeTLESLRVLG---FT---HEEIISMLRMVSAVLQFGNIALKR----ERNTDQATMPDNTAAQK---- 407
Cdd:cd14887 227 VGIGGGEQADIFK-LLAAILHLGnveFTtdqEPETSKKRKLTSVSVGCEETAADRshssEVKCLSSGLKVTEASRKhlkt 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 408 LCRLLGL--GVTDFSRALLTPRIKVGRDyVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPR--------- 476
Cdd:cd14887 306 VARLLGLppGVEGEEMLRLALVSRSVRE-TRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 477 ----QGASFLGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGI---------PWTF-LDFG 539
Cdd:cd14887 385 tpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqdcsafPFSFpLAST 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 540 LDLQP--CIDLIERP--------ANPPGL---------LALLDEECWFPKATDKSFVEKVAQEQGGHPKF--QRPRHLRD 598
Cdd:cd14887 465 LTSSPssTSPFSPTPsfrsssafATSPSLpsslsslssSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYknITPALSRE 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 599 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQstdrltaeiwkdehggfqqfsflgsfppsppgsaerCSSAIS 678
Cdd:cd14887 545 NLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA------------------------------------CSTYTR 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 679 PPGVEGIVGLEQVSSlgdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLR 758
Cdd:cd14887 589 LVGSKKNSGVRAISS-------------RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLR 655
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743142585 759 CNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 829
Cdd:cd14887 656 CSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
119-829 |
9.49e-88 |
|
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: 301.73 E-value: 9.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR---GKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 195
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 196 CTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 275
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS----------------SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 276 INF-DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-PSSSPGQERELF 353
Cdd:cd14878 145 LQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmREDVSTAERSLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 354 QETL----ESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd14878 225 REKLavlkQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS---FLGILDIAGFEIFQLNSFEQLCINYT 506
Cdd:cd14878 305 FKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 507 NEKLQQLFNHTMFVLEQEEYQREGIPW----------TFLDFGLDlqpcidlierpaNPPGLLALLDEEC---W-----F 568
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMetayspgnqtGVLDFFFQ------------KPSGFLSLLDEESqmiWsvepnL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 569 PK-------ATDKSFVEKVAQEQGGHPKFqrprhlRDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDR 640
Cdd:cd14878 453 PKklqslleSSNTNAVYSPMKDGNGNVAL------KDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENV 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 641 LTAEIwkdehggFQqfsflgsfppsppgsaercssaisppgvegivgleqvSSLGdgppggrprrgmfrTVGQLYKESLS 720
Cdd:cd14878 527 VINHL-------FQ-------------------------------------SKLV--------------TIASQLRKSLA 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 721 RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFM 799
Cdd:cd14878 549 DIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQ 628
|
730 740 750
....*....|....*....|....*....|
gi 1743142585 800 DGKQACEKMIQALELDPnlYRVGQSKIFFR 829
Cdd:cd14878 629 SAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
116-828 |
1.55e-87 |
|
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: 301.01 E-value: 1.55e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 116 LNEASVLHNLRERYYSGLIYTY---SGLfcVVINPYKQLPIYTEAIVEMYR-------GKKRHEVPPHVYAVTEGAYRSM 185
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 186 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSPKGRKepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKN 264
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK---------------LSSQISAAEFVLDSFGNAKTLTN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 265 DNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--- 341
Cdd:cd14879 144 PNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYgch 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 342 --PSSSPGQERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNI--ALKRERNTDqATMPDNTAA-QKLCRLLGLGV 416
Cdd:cd14879 224 plPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLefTYDHEGGEE-SAVVKNTDVlDIVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 417 TDFsRALLTPRIK-VGRD----YVQKAQTKEQADfaleALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFE 491
Cdd:cd14879 303 EDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 492 ifQL-----NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEEC 566
Cdd:cd14879 378 --NRsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQT 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 567 -WFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAD---FSVLHYAGKVDYKANEWLMKNmdplndnvaallhqstdrlt 642
Cdd:cd14879 453 rRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERN-------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 643 aeiwkdehggfqqfsflgsfppsppgsAERCSSAIsppgvegivgleqVSslgdgppggrprrgMFRTVGQLyKESLSRL 722
Cdd:cd14879 513 ---------------------------GDVLSPDF-------------VN--------------LLRGATQL-NAALSEL 537
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 723 MATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPnaipkgFMDGK 802
Cdd:cd14879 538 LDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAE 611
|
730 740
....*....|....*....|....*.
gi 1743142585 803 QACEKMIQALELDPNLYRVGQSKIFF 828
Cdd:cd14879 612 RIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
119-829 |
1.51e-79 |
|
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: 277.28 E-value: 1.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLpiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAhvasspKGRKEPGvpasvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN-----------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14937 140 DEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEiDDAKDFGNLM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 358 ESLRVLGFtHEEIISMLRMVSAVLQFGNI---ALKRERNTDQATMPDNT--AAQKLCRLLGLGVTDFSRALLTPRIKVGR 432
Cdd:cd14937 220 ISFDKMNM-HDMKDDLFLTLSGLLLLGNVeyqEIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIAN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 433 DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 512
Cdd:cd14937 299 QKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNN-KELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 513 LFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQR 592
Cdd:cd14937 378 IYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYAS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 593 PRhlRD-QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfppsppgsae 671
Cdd:cd14937 454 TK--KDiNKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED----------------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 672 rcssaisppgvegivgLEQVSSLGdgppggRPRRGMFRtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPR 751
Cdd:cd14937 509 ----------------VEVSESLG------RKNLITFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQK 561
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 752 LVLDQLRCNGVLEGIRIcRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQAlELDPNLYRVGQSKIFFR 829
Cdd:cd14937 562 KVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
119-781 |
8.83e-77 |
|
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: 270.62 E-value: 8.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQDRE 190
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 191 DQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstVSYGELERQLLQANPILEAFGNAKTVKNDNSSRF 270
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTD---------------SQMTERIDKLIYINNILESMSNATTIKNNNSSRC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 271 GKFIRINFD---------VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPCSHYRFL-- 338
Cdd:cd14884 146 GRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 339 ------------------TNGPSSSPGQEREL-FQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKrerntdqatm 399
Cdd:cd14884 226 deshqkrsvkgtlrlgsdSLDPSEEEKAKDEKnFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK---------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 400 pdntAAqklCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL-------- 471
Cdd:cd14884 296 ----AA---AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekde 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 472 ---DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFlDFGLDLQPCIDL 548
Cdd:cd14884 369 sdnEDIYSINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS-DVAPSYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 549 IERpanppgLLALLDE-----ECWFPKATDKSFV-----EKVAQEQGGHPKFQRPRHLRDQAD---------FSVLHYAG 609
Cdd:cd14884 448 IAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYGFVLNHDADGTAkkqnikkniFFIRHYAG 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 610 KVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdehggfqqfsflgsfppsppgSAERCSSaisppgvegivgle 689
Cdd:cd14884 522 LVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE------------------------ANNGGNK-------------- 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 690 qvsslgdgppggrprrGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIC 769
Cdd:cd14884 564 ----------------GNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKIL 627
|
730
....*....|..
gi 1743142585 770 RQGFPNRILFQE 781
Cdd:cd14884 628 NRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
120-828 |
1.67e-66 |
|
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: 238.86 E-value: 1.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYkqlpiyteaiveMYRGKKRHEVPPHVYA-------VTEGAYRSMLQDREDQ 192
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 193 SILCTGESGAGKTENTKKVIQYLAHVASspkgrkepGVPASvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGK 272
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPET-------DAFKHLAAAFTVLRSLGSAKTATNSESSRIGH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 273 FIRINFdVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNGPSSSPGQER 350
Cdd:cd14881 135 FIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAED 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 351 EL-FQETLESLRVLGFTHEEIIsmlRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd14881 214 AArFQAWKACLGILGIPFLDVV---RVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrspRQGAS--------FLGILDIAGFEIFQLNSFEQL 501
Cdd:cd14881 290 ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 502 CINYTNEKLQQLFNHTMFVLEQEEYQREGIPwTFLDFG-LDLQPCIDLIErpANPPGLLALLDEECwFPKATDKSFVEKV 580
Cdd:cd14881 366 CINLCAETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 581 AQEQGGHPKFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTdrltaeiwkdehggfqqfsflg 660
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 661 sfppsppgsaerCSSAisppgvegivgleqvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPN 740
Cdd:cd14881 499 ------------CNFG-------------------------------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSN 535
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 741 HEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQ--ALELDPNL 818
Cdd:cd14881 536 TTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPPSK 615
|
730
....*....|....*..
gi 1743142585 819 -------YRVGQSKIFF 828
Cdd:cd14881 616 lssvstsWALGKRHIFL 632
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
120-829 |
1.91e-65 |
|
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: 236.53 E-value: 1.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLahvasspkgrkepgVPASVSTVSYgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14905 80 ESGSGKSENTKIIIQYL--------------LTTDLSRSKY--LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ--ERELFQET 356
Cdd:cd14905 144 SLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 357 LESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNtdQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14905 224 KMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 437 KAqtkeqadfalEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14905 302 NR----------DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 517 TMFVLEQEEYQREGIPW-TFLDFGlDLQPCIDLIERPANppgllaLLDEECWFPKATDKSFVEKVAQEQGGHPKF-QRPR 594
Cdd:cd14905 370 TVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEKIIN------LLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPN 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 595 hlrdqaDFSVLHYAGKVDYKANEWLMKNMDPLNDNvAALLHQSTdrLTAEIWKDEhGGF----------QQFSFLGSFPP 664
Cdd:cd14905 443 ------KFGIEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNS--ITKYLFSRD-GVFninatvaelnQMFDAKNTAKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 665 SPPGSAE---RCSS-----AISPPGVEGIVGLEQVSSLGDGppggrprrgmfrTVGQLYKeSLSRLMATLSNTNPS--FV 734
Cdd:cd14905 513 SPLSIVKvllSCGSnnpnnVNNPNNNSGGGGGGGNSGGGSG------------SGGSTYT-TYSSTNKAINNSNCDfhFI 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 735 RCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFP----NRILFqefrQRYEILTPNAipKGFMD-GKQACEKMI 809
Cdd:cd14905 580 RCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFF----DRFSFFFQNQ--RNFQNlFEKLKENDI 653
|
730 740
....*....|....*....|
gi 1743142585 810 QALELDPNLYRVGQSKIFFR 829
Cdd:cd14905 654 NIDSILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
119-794 |
3.73e-64 |
|
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: 231.68 E-value: 3.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYrgkkrhevppHVYAVTEGAYRSMLQDRED-QSILCT 197
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 198 GESGAGKTENTKKVIQYLAhvaSSPKgrkepgvpASVSTVSYGELERqllqanpILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPK--------SKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 278 FDvAGYIVGANIE-TYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQE 355
Cdd:cd14874 133 YK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDvNHFKH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 356 TLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKRERNTD---QATMPDNTAAQKLCRLLgLGVtDFSR--ALLTPRIKV 430
Cdd:cd14874 212 LEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFL-LEV-DFDQlvNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 431 GrdyvqKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAsfLGILDIAGFEIFQLNSFEQLCINYTNEKL 510
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 511 QQLFNHTMFVLEQEEYQREGIPWTF-LDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK 589
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 590 FQRPRHlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehggFQQFSFlgsfppsppgs 669
Cdd:cd14874 441 YGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL-------FESYSS----------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 670 aercssaisppgvegivgleqvsslgdgppggrPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 749
Cdd:cd14874 502 ---------------------------------NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFD 548
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1743142585 750 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 794
Cdd:cd14874 549 IPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
120-789 |
9.59e-64 |
|
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: 230.78 E-value: 9.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 200 SGAGKTENTKKVIQYLAHVasspkGRKEPGVPASVstvsygelerqlLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRV------------ESSIKAILALVNAGTPLNADSTRCILQYQLTFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG--AGEQLKaDLLLEPCSHYRFLTNGPSSSPGQER------- 350
Cdd:cd14882 145 STGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSKLKyrrddpe 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 351 ---ELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIALKreRNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPR 427
Cdd:cd14882 224 gnvERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR--QNGGYAELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 428 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECwfPKATDKSFV-EKVAQEQ 584
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYImDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 585 GGHPKfqrprhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDehggfqqfsflgsfpp 664
Cdd:cd14882 457 SQFVK------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 665 sppgsaercssaisppgvegivglEQVSSLgdgppggrprrgmfRTVGQLYKESLSRLMATLS-NTNPS---FVRCIVPN 740
Cdd:cd14882 515 ------------------------SQVRNM--------------RTLAATFRATSLELLKMLSiGANSGgthFVRCIRSD 556
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1743142585 741 HEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 789
Cdd:cd14882 557 LEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
122-787 |
4.55e-62 |
|
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: 227.93 E-value: 4.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 122 LHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKR----------HEVPPHVYAVTEGAYRSMLQDRED 191
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 192 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEpGVPASVSTVSYGElerQLLQANPILEAFGNAKTVKNDNSSRFG 271
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD-SEGASGVLHPIGQ---QILHAFTILEAFGNAATRQNRNSSRFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 272 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQ--LKADLLLEPCSH-YRFLTNGP--SSSP 346
Cdd:cd14893 160 KMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVNeFVMLKQADplATNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 347 GQERELFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNIAL-------KRERNTDQATMPDNTAaqklCRLLGLGVTDF 419
Cdd:cd14893 240 ALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQS----CALKDPAQILL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 420 SRALLTPRIKVGRDYVQKAQ----------------TKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPR--- 476
Cdd:cd14893 316 AAKLLEVEPVVLDNYFRTRQffskdgnktvsslkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKsni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 477 ----QGasfLGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IPWTFLDFGLDLQ 543
Cdd:cd14893 396 vinsQG---VHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 544 PCIDLIERPanPPGLLALLDEECWFPKATDKSFVEK---VAQEQGGhpkFQRPRHLRDQAD------------FSVLHYA 608
Cdd:cd14893 473 KCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKlfsGNEAVGG---LSRPNMGADTTNeylapskdwrllFIVQHHC 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 609 GKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIwkdehgGFQQFSFLGSfpPSPPGSAERCSSAISPPGvEGIVGL 688
Cdd:cd14893 548 GKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAV------GAAQMAAASS--EKAAKQTEERGSTSSKFR-KSASSA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 689 EQVSSLGDGppggrprrgmfrTVGQLYKESLSRLMAtLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRI 768
Cdd:cd14893 619 RESKNITDS------------AATDVYNQADALLHA-LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQA 685
|
730
....*....|....*....
gi 1743142585 769 CRQGFPNRILFQEFRQRYE 787
Cdd:cd14893 686 SRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
141-283 |
1.01e-58 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 200.26 E-value: 1.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 141 FCVVINPYKQLPIYTEAIV-EMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 219
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 220 SSPKGRKEPGVPASVsTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 283
Cdd:cd01363 81 FNGINKGETEGWVYL-TEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
120-827 |
6.65e-52 |
|
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: 196.98 E-value: 6.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR-GKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 199 ESGAGKTENTKKVIQYLAHVASSpkGRKEPGVPASVSTVSYGELERQ---------LLQANPILEAFGNAKTVKNDNSSR 269
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKG--SRRLPTNLNDQEEDNIHNEENTdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 270 FGKFIRINFDvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE 349
Cdd:cd14938 160 FSKFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 350 RE-LFQETLESLRVLGFTHEEIISMLRMVSAVLQFGNI---------ALKRERNTDQATMPDNTAAQKL----------- 408
Cdd:cd14938 239 YSgKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkafrkkSLLMGKNQCGQNINYETILSELensediglden 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 409 -------CRLLGLGVTDFSRALLTPRIkVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGA 479
Cdd:cd14938 319 vknlllaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTqlQNININT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 480 SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANpPGLL 559
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE-GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 560 ALLDEECwFPKATDKSFVEKVAQEQGGH-PKF-QRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQS 637
Cdd:cd14938 477 SLLENVS-TKTIFDKSNLHSSIIRKFSRnSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 638 tdrltaeiwkdEHGGFQQFSFLGSFPPSPPGSAERCSSAISppgvegivgleqvSSLGDGPPGGRPRRGMFRTvgqLYKE 717
Cdd:cd14938 556 -----------ENEYMRQFCMFYNYDNSGNIVEEKRRYSIQ-------------SALKLFKRRYDTKNQMAVS---LLRN 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 718 SLSRLMATLSNTNPSFVRCIVPNHEKRA-GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIltPNAipk 796
Cdd:cd14938 609 NLTELEKLQETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE--- 683
|
730 740 750
....*....|....*....|....*....|.
gi 1743142585 797 gfmDGKQACEKMIQALELDPNLYRVGQSKIF 827
Cdd:cd14938 684 ---DLKEKVEALIKSYQISNYEWMIGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1192-1770 |
1.08e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 119.27 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1192 RTKAEKqRRDLGEELEALRGELE-DTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQL 1270
Cdd:COG1196 209 AEKAER-YRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1271 EQARRgkgawektrlaLEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENV 1350
Cdd:COG1196 288 AEEYE-----------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1351 SGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQ 1430
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1431 LSEWRRRQEEEAGALeageearrraareaEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRK 1510
Cdd:COG1196 437 EEEEEEALEEAAEEE--------------AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1511 FDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDdvGKSVHELER 1590
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--GRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1591 ACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQR 1670
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1671 ALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRL 1750
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580
....*....|....*....|
gi 1743142585 1751 QEELAASDRARRQAQQDRDE 1770
Cdd:COG1196 741 LLEEEELLEEEALEELPEPP 760
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1035-1574 |
1.38e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1035 EAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKL 1114
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1115 KRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALAraedeggARAQLLKSLREAQAALAEAQEDLEAERVARTK 1194
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-------ELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1195 AEKQRRDLGEELEALRGELED---TLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLE 1271
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEAlleRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1272 QARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQ--RAQAELEN 1349
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1350 VSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQA 1429
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1430 QLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQR 1509
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743142585 1510 KFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRA----LRAELEAL 1574
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERelerLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1026-1931 |
4.44e-24 |
|
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: 111.30 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1026 KLQLEKVTTEAKMKKFEEDLLLLEDQNSKLskERKLleDRLAEFSSQAAEEEEKVKSLNKLRLKYEAtitdmeDRLRKEE 1105
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNEL--ERQL--KSLERQAEKAERYKELKAELRELELALLV------LRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1106 KGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDL 1185
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1186 EAERVARTKAEKQRRDLGEELEALRGELEDTldstnaqqelrskrEQEVTELKKTLEEEtrihEAAVQELRQRhgqaLGE 1265
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEEL--------------KEELESLEAELEEL----EAELEELESR----LEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1266 LAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQ-----TARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKL 1340
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrerLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1341 QRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEetraKLALGSRVRAMEAEA---AGLREQLEEEAAAR 1417
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQsglSGILGVLSELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1418 ERAGRELQTA-----QAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASV 1492
Cdd:TIGR02168 533 EGYEAAIEAAlggrlQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1493 DLE-------QQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRaleeeqeareelerqnr 1565
Cdd:TIGR02168 613 KLRkalsyllGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILER----------------- 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1566 alRAELEallsskdDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERdLQGRDEAG 1645
Cdd:TIGR02168 676 --RREIE-------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1646 EERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSS 1725
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1726 REEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVAngnlskaAILEEKRQLEGRLgqleeelee 1805
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE-------ALLNERASLEEAL--------- 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1806 eqsnsELLNDRYRKLLLQVESLttelsaersfsakaESGRQQLERQIQELRGRLGEEDAgARARHKMTIAALESKLAqAE 1885
Cdd:TIGR02168 890 -----ALLRSELEELSEELREL--------------ESKRSELRRELEELREKLAQLEL-RLEGLEVRIDNLQERLS-EE 948
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 1743142585 1886 EQLEQETrerilsgklvrrAEKRLKEVVLQVEEERRVADQLRDQLE 1931
Cdd:TIGR02168 949 YSLTLEE------------AEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
125-770 |
9.43e-24 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 109.83 E-value: 9.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 125 LRERYYSGLIYTYSGLFCV-VINPYKQL------PIYTEAIVEMYRGKKRHE--VPPHVYAV------------------ 177
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 178 --TEGAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVASSP--KGRKE----------PGVPASVST------- 236
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPAlsKGSEEtckvsgstrqPKIKLFTSStkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 237 ----------------------------------------------------------VSYGELERQL------------ 246
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyekLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 247 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRAIRQA------KDECSFHI 311
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 312 FYQLLGGAG-----EQLKADLLLE--PCSHYRFLTNGPSSSPG---------QERELFQETLESLRVLGFTHEEIISMLR 375
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDgiDCSALTYLGRSDHKLAGfvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 376 MVSAVLQFGNIALKRERNTDQATMPDN---TAAQKLCRLLGLG-VTDFSRALLTPRIKV--GRDYVQKAQTKEQADFALE 449
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGsVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 450 ALAKATYERLFRWLVLRLNRAL----------------DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQql 513
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY-- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 514 fnhtmfvleQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKAT----------DKSFVEKVAQE 583
Cdd:cd14894 564 ---------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 584 QGGH-PKFQR-----PRH---LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDEhggfQ 654
Cdd:cd14894 635 NSSRlPEPPRvlsnaKRHtpvLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNES----S 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 655 QFSFLGSFPPSPPGSAErcsSAISppGVEGIVGleqvsslgdgppggrprrgmfrtvgqLYKESLSRLMATLSNTNPSFV 734
Cdd:cd14894 711 QLGWSPNTNRSMLGSAE---SRLS--GTKSFVG--------------------------QFRSHVNVLTSQDDKNMPFYF 759
|
810 820 830
....*....|....*....|....*....|....*.
gi 1743142585 735 RCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICR 770
Cdd:cd14894 760 HCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1226-1988 |
1.92e-23 |
|
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: 108.99 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1226 LRSKREQEVTELKKTLEEETRIhEAAVQELRqRHGQALGELAEQLEQARRGKGAWEKTRLALEA-EVSELRAELSSLQTA 1304
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRL-EDILNELE-RQLKSLERQAEKAERYKELKAELRELELALLVlRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1305 RQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQE 1384
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1385 ETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQ 1464
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1465 RLAEKTEAVDRLERGRRRLQQELDDASVD-----LEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGRER 1539
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1540 EARALSLTRALEEEQ--EAREELERQNRALRAELEALLSSKDDVGKsvhELERACRVAeqAANDLRAQVTELEDELTAAE 1617
Cdd:TIGR02168 488 QARLDSLERLQENLEgfSEGVKALLKNQSGLSGILGVLSELISVDE---GYEAAIEAA--LGGRLQAVVVENLNAAKKAI 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1618 DA---KLRLEVTVQALKTQHERDLQGRDE---AGEERRRQLAKQLRDAEVERDE------------ERKQRALAVAARKK 1679
Cdd:TIGR02168 563 AFlkqNELGRVTFLPLDSIKGTEIQGNDReilKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvDDLDNALELAKKLR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1680 -------LEGEL-----------EELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLK 1741
Cdd:TIGR02168 643 pgyrivtLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1742 GLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLL 1821
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1822 LQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGE-EDAGARARHKMT-----IAALESKLAQAEEQLEQETRER 1895
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDlEEQIEELSEDIEslaaeIEELEELIEELESELEALLNER 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1896 ILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASR-AQAGRRRLQRELEDVTESAES 1974
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENK 962
|
810
....*....|....
gi 1743142585 1975 MNREVTTLRNRLRR 1988
Cdd:TIGR02168 963 IEDDEEEARRRLKR 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1062-1919 |
3.01e-23 |
|
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: 108.22 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1062 LEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRS 1141
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1142 QLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRG---ELEDTLD 1218
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1219 STNAQQELRSKREQEVTELKKTLEEETRIHEAAVQEL-RQRHGQALGELAEQLEQarrgkgawektrlaLEAEVSELRAE 1297
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEE--------------LQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1298 LSSLQTARQEGEQRRRRLESQLQEVQGRagdgeraraeaAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHD 1377
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQAR-----------LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1378 AQELlqeETRAKLALGSRVRAMEAEaaglreqleeeaaareragrelqTAQAQLSEWRRRQEEEAGALEAGEEARRRAAR 1457
Cdd:TIGR02168 532 DEGY---EAAIEAALGGRLQAVVVE-----------------------NLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1458 EAEALTQRLAEKTEAVDRLERgRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGR 1537
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKD-LVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1538 EREARALSLTRaleeeqeareelerqnralRAELEallsskdDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAE 1617
Cdd:TIGR02168 665 SAKTNSSILER-------------------RREIE-------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1618 DAKLRLEVTVQALKTQHERdLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQG 1697
Cdd:TIGR02168 719 KELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1698 KEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVan 1777
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-- 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1778 gnlskAAILEEKRQLEGRLgqleeeleeeqsnsELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRG 1857
Cdd:TIGR02168 876 -----EALLNERASLEEAL--------------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743142585 1858 RLGEEDAGARARHKMTIAALESKLAQAEEQlEQETRERIlsgKLVRRAEKRLKEVVLQVEEE 1919
Cdd:TIGR02168 937 RIDNLQERLSEEYSLTLEEAEALENKIEDD-EEEARRRL---KRLENKIKELGPVNLAAIEE 994
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1333-1945 |
5.85e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1333 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKElsstEAQLHDAQELLQEETRAKLAL-GSRVRAMEAEAAGLREQle 1411
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLERQ----AEKAERYRELKEELKELEAELlLLKLRELEAELEELEAE-- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1412 eeaaareragreLQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDAS 1491
Cdd:COG1196 248 ------------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1492 VDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1571
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1572 EALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRrQ 1651
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA-L 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1652 LAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFS 1731
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1732 QNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDE--MADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSN 1809
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1810 SELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLE 1889
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1890 QETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLE 1945
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
907-1756 |
6.67e-23 |
|
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: 107.45 E-value: 6.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 907 RQDEVLQARAQELQKVQELQQqsarEVRELQGRVAQLEEERARlaEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 986
Cdd:TIGR02168 200 RQLKSLERQAEKAERYKELKA----ELRELELALLVLRLEELR--EELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 987 ARVGEEEECSRQMQT-------EKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKER 1059
Cdd:TIGR02168 274 LEVSELEEEIEELQKelyalanEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1060 KLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEEL 1139
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1140 RSQ-LGRKEEELQAALARAEDEGGARAQLLKSLREaqaalaeaqedleaervARTKAEKQRRDLGEELEALRGEledtLD 1218
Cdd:TIGR02168 434 ELKeLQAELEELEEELEELQEELERLEEALEELRE-----------------ELEEAEQALDAAERELAQLQAR----LD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1219 STNAQQELRSKREQEVTELKKTleeetriheaavqelRQRHGQALGELAEQLEQArrgkgawEKTRLALEAEVSELRAEL 1298
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKALLKN---------------QSGLSGILGVLSELISVD-------EGYEAAIEAALGGRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1299 --SSLQTArqegeqrRRRLESQLQEVQGRAG----DGERARAEAAEKLQRAQaELENVSGALNEAESKTIRLSKELSSTE 1372
Cdd:TIGR02168 551 vvENLNAA-------KKAIAFLKQNELGRVTflplDSIKGTEIQGNDREILK-NIEGFLGVAKDLVKFDPKLRKALSYLL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1373 AQLHDAQELLQE-ETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAgaleageea 1451
Cdd:TIGR02168 623 GGVLVVDDLDNAlELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKI--------- 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1452 rrraareaEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERER 1531
Cdd:TIGR02168 694 --------AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1532 AEAEGRErearalsltraleeeqeareelerqnraLRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELED 1611
Cdd:TIGR02168 766 LEERLEE----------------------------AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1612 ELTAAEDAKLRLEVTVQALKTQHErDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQM 1691
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLE-DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743142585 1692 asagqgkEEAVKQLRKMQAQMKELWREVEETRSSREEIfsqnresEKRLKGLEAEVLRLQEELAA 1756
Cdd:TIGR02168 897 -------EELSEELRELESKRSELRRELEELREKLAQL-------ELRLEGLEVRIDNLQERLSE 947
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
860-1440 |
2.24e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.40 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 860 ARRAfQKRQQQQSALRVMQrncaAYLKLRHWQWWRLfTKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVRELQGR 939
Cdd:COG1196 209 AEKA-ERYRELKEELKELE----AELLLLKLRELEA-ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 940 VAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEA 1019
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1020 EEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMED 1099
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1100 RLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALA 1179
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1180 EAQEDLEAERVARtkaekQRRDLGEELEALRGEL--EDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQ 1257
Cdd:COG1196 523 AGAVAVLIGVEAA-----YEAALEAALAAALQNIvvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1258 RHGQALGELAEQLEQARrgkgawektRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAA 1337
Cdd:COG1196 598 GAAVDLVASDLREADAR---------YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1338 EKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAAR 1417
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580
....*....|....*....|...
gi 1743142585 1418 ERAGRELQTAQAQLSEWRRRQEE 1440
Cdd:COG1196 749 EEEALEELPEPPDLEELERELER 771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1025-1777 |
4.75e-21 |
|
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: 101.29 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1025 QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKE 1104
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1105 EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLReaqaalaeaqed 1184
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA------------ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1185 LEAERVARTKAEKQRrdLGEELEALRGELEDTLDSTNAQQelRSKREQEVTELKKTLEEETRIHEAAVQELRQrhgqaLG 1264
Cdd:TIGR02168 397 SLNNEIERLEARLER--LEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEE-----LR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1265 ELAEQLEQARRgkgawektrlALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERA--RAEAAEKLQR 1342
Cdd:TIGR02168 468 EELEEAEQALD----------AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLseLISVDEGYEA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1343 AqaeLENVSGAlneaesktiRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGR 1422
Cdd:TIGR02168 538 A---IEAALGG---------RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAK 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1423 ELQTAQAQLSEW-------RRRQEEEAGALeageearrraaREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLE 1495
Cdd:TIGR02168 606 DLVKFDPKLRKAlsyllggVLVVDDLDNAL-----------ELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1496 QQRQLvSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRaleeeqeareelerQNRALRAELEALL 1575
Cdd:TIGR02168 675 RRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR--------------QISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1576 SSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQH---ERDLQG-RDEAGEERRRQ 1651
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDElRAELTLLNEEA 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1652 LAKQLRDAEVERDEERKQRALAVAAR--KKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEI 1729
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1743142585 1730 FSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVAN 1777
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1563-1988 |
3.43e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1563 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERdLQGRD 1642
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-LEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1643 EAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEET 1722
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1723 RSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEE 1802
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1803 LEEEQSNSELLNDRYRKLLLQVESLT----TELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALE 1878
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAarllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1879 SKLAQaEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVkqlkrQLEEAEEEASRAQAGR 1958
Cdd:COG1196 545 AAALQ-NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD-----LVASDLREADARYYVL 618
|
410 420 430
....*....|....*....|....*....|
gi 1743142585 1959 RRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1063-1793 |
4.32e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 94.75 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1063 EDRLAEFSSQAAEEEEKVKSLNKLRLKYEaTITDMEDRLRKEE-----KGRQELEKLKRRLDGESSELQEQMVEQQQRAE 1137
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1138 ELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTK-AEKQRRDLGEELEALRGELEDT 1216
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1217 LDSTNAQQELRSKREQEVTELKKTLEE-ETRIHE--AAVQELRQRHGQalgeLAEQLEQARRGKGAWEKTRLALEAEVSE 1293
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDlRAELEEvdKEFAETRDELKD----YREKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1294 LRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEA 1373
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1374 QLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEE-EAAARERAGRELQ--------TAQAQLSEWRRRQEEEAGA 1444
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyATAIEVAAGNRLNnvvveddaVAKEAIELLKRRKAGRATF 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1445 LEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASV--DLEQQRQLVS-----TLEKKqrkfdqlLAE 1517
Cdd:TIGR02169 578 LPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRLMGkyrmvTLEGE-------LFE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1518 EKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQ 1597
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1598 AANDLRAQVTELEDELTAAEDAKLRLEVTVQAL---KTQHERDL-QGRDEAGEERRRQLAKQLRDAEVERDEERKQRALA 1673
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELearIEELEEDLhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1674 VAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQ-------NRESEKRLKGLEAE 1746
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleeleaaLRDLESRLGDLKKE 890
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1743142585 1747 VLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLE 1793
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1646-1956 |
1.93e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1646 EERRRQLAKQLRDA----EVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEE 1721
Cdd:COG1196 199 ERQLEPLERQAEKAeryrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1722 TRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEE 1801
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1802 ELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRlgeedagaRARHKMTIAALESKL 1881
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER--------LERLEEELEELEEAL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743142585 1882 AQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQA 1956
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
903-1514 |
2.26e-17 |
|
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: 88.97 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 903 LQVTRQDEVLQAraqELQKVQELQQQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVV 982
Cdd:TIGR02169 290 LRVKEKIGELEA---EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 983 SELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLL 1062
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1063 EDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLD---GESSELQEQMVEQQQRAEEL 1139
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervRGGRAVEEVLKASIQGVHGT 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1140 RSQLGRKEEELQAALARA----------EDEGGARA--QLLKSLREAQAA----LAEAQEDLEAERVARTKAEKQRRDLG 1203
Cdd:TIGR02169 527 VAQLGSVGERYATAIEVAagnrlnnvvvEDDAVAKEaiELLKRRKAGRATflplNKMRDERRDLSILSEDGVIGFAVDLV 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1204 EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV----QELRQRHGQALGELAEqLEQARRGKGA 1279
Cdd:TIGR02169 607 EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggsRAPRGGILFSRSEPAE-LQRLRERLEG 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1280 WEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAES 1359
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1360 KTIRLSKELSSTEAQL-----HDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEW 1434
Cdd:TIGR02169 766 RIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1435 -------RRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTL-EK 1506
Cdd:TIGR02169 846 keqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkAK 925
|
....*...
gi 1743142585 1507 KQRKFDQL 1514
Cdd:TIGR02169 926 LEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
917-1518 |
5.62e-17 |
|
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: 87.80 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 917 QELQKVQELQQQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECS 996
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 997 RQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRL--AEFSSQAA 1074
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeAELKELQA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1075 EEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSE---LQEQMVEQQQRAEELR----------- 1140
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENLEGFSEGVKallknqsglsg 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1141 -----SQLGRKEEELQAALARA----------EDEGGARA--QLLKSLREAQAA----LAEAQEDLEAERVARTKAEKQR 1199
Cdd:TIGR02168 521 ilgvlSELISVDEGYEAAIEAAlggrlqavvvENLNAAKKaiAFLKQNELGRVTflplDSIKGTEIQGNDREILKNIEGF 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1200 RDLGEELEALRGELE-------------DTLDSTNAQQEL----------------------------------RSKREQ 1232
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssileRRREIE 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1233 EVTELKKTLEEETRIHEAAVQELRQrhgqALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRR 1312
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRK----ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1313 RRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLAL 1392
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1393 GSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEW--RRRQEEEAGALEAGEEARrraareaeaLTQRLAEKT 1470
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnERASLEEALALLRSELEE---------LSEELRELE 907
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1743142585 1471 EAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEE 1518
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
915-1523 |
4.44e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.19 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 915 RAQELQKVQELQQqsAREVRELQgrvAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQElelvvselEARVGEEEE 994
Cdd:PTZ00121 1183 KAEEVRKAEELRK--AEDARKAE---AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE--------EAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 995 CSRQMQTEKKRLQQHIQELEAHLEaeegARQKLQLEKVTTEAKMKKFEEdLLLLEDQNSKLSKERKLLEDRLAEFSSQAA 1074
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIK----AEEARKADELKKAEEKKKADE-AKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1075 EEEEKvkSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDG---ESSELQEQMVEQQQRAEELRS--QLGRKEEE 1149
Cdd:PTZ00121 1325 EEAKK--KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaekKKEEAKKKADAAKKKAEEKKKadEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1150 LQAA---LARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERV--ARTKAEKQRR--DLGEELEALRG--ELEDTLDST 1220
Cdd:PTZ00121 1403 DKKKadeLKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAdeAKKKAEEAKKaeEAKKKAEEAKKadEAKKKAEEA 1482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1221 NAQQELRSKREQ---EVTELKKTLEEETRIHEA-------AVQELRQRHGQALGELAEQLEQARRG---KGAWEKTRLAL 1287
Cdd:PTZ00121 1483 KKADEAKKKAEEakkKADEAKKAAEAKKKADEAkkaeeakKADEAKKAEEAKKADEAKKAEEKKKAdelKKAEELKKAEE 1562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1288 EAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGAlnEAESKTIRLSKE 1367
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1368 LSSTEAQlhDAQELLQEETRAKLALGSRVRAMEAEaaglreqleeeaAARERAGRELQTAQAQLSEWRRRQEEEAGALEA 1447
Cdd:PTZ00121 1641 KEAEEKK--KAEELKKAEEENKIKAAEEAKKAEED------------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1448 GEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDlEQQRQLVSTLEKKQRKFDQLLAEEKAAVL 1523
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1602-1993 |
7.15e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 7.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1602 LRAQVTELEDEltaAEDAKLRLEVTVQALKTQHERDLQgrdeageeRRRQLAKQLRDAEVERDEERKQRALAVAARKKLE 1681
Cdd:COG1196 198 LERQLEPLERQ---AEKAERYRELKEELKELEAELLLL--------KLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1682 GELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRAR 1761
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1762 RQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKA 1841
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1842 ESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERR 1921
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743142585 1922 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAqAGRRRLQRELEDVTESAESMNREVTTLRNRlRRGPLTF 1993
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-LEAALAAALQNIVVEDDEVAAAAIEYLKAA-KAGRATF 576
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
911-1294 |
9.02e-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: 80.49 E-value: 9.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 911 VLQARAQELQKVQELQQQSAREVRELQGRVAQLEEERARLAEQLRAeaelcaeaeetrgrLAARKQELELVVSELEARVG 990
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ--------------LRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 991 EEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFS 1070
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1071 SQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEklkrrldGESSELQEQMVEQQQRAEELRSQLGRKEEEL 1150
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1151 QAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEEL-EALRGELEDTLDSTNAQQELRSK 1229
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEE 969
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743142585 1230 REQEVTELKKTLEEETRIHEAAVQELRQRHGQaLGELAEQLEQARRGKGAWEKTRLALEAEVSEL 1294
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEELKER-YDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1583-1988 |
9.63e-15 |
|
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: 80.60 E-value: 9.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1583 KSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAgEERRRQLAKQLRDAEVE 1662
Cdd:pfam01576 201 KGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA-LKKIRELEAQISELQED 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1663 RDEERKQRALAVAARKKLEGELEELKAQMASAgQGKEEAVKQLR-KMQAQMKELWREVEETRSSREEIFSQNRESEKR-L 1740
Cdd:pfam01576 280 LESERAARNKAEKQRRDLGEELEALKTELEDT-LDTTAAQQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1741 KGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKL 1820
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1821 LLQVESLTTELSAERSFSAKAESGRQQLERQIQELRgRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGK 1900
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ-ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1901 LVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVT 1980
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
....*...
gi 1743142585 1981 TLRNRLRR 1988
Cdd:pfam01576 598 NLEKKQKK 605
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
908-1793 |
1.22e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 908 QDEVLQARAQELQKVQELQQQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQElelvvselEA 987
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE--------DA 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 988 RVGEEEecsrqmqtekkrlqqhiqeleahleaeegarqklqlekvtteakmKKFEEDlllledqnSKLSKERKLLEDRLA 1067
Cdd:PTZ00121 1140 RKAEEA---------------------------------------------RKAEDA--------KRVEIARKAEDARKA 1166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1068 EFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEklkRRLDGESSELQEQMVEQQQRAEELRsqlgRKE 1147
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEE---RKAEEARKAEDAKKAEAVKKAEEAK----KDA 1239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1148 EELQaalaRAEDEggaraqllkSLREAQAALAEAQEDLEAERVARTKAEKQRRdlgeelealRGELEDTLDSTNAQQELR 1227
Cdd:PTZ00121 1240 EEAK----KAEEE---------RNNEEIRKFEEARMAHFARRQAAIKAEEARK---------ADELKKAEEKKKADEAKK 1297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1228 SKREQEVTELKKTLEEETRIHEAAVQ-ELRQRHGQALGELAEQLEQARRGKGAWEKTRlALEAEVSELRAELSSLQTArq 1306
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA-ADEAEAAEEKAEAAEKKKE-- 1374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1307 EGEQRRRRLESQLQEVqgRAGDGERARAE----AAEKLQRAQAELENVSGALNEAESKtiRLSKELSSTEAQLHDAQELL 1382
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEK--KKADEAKKKAEedkkKADELKKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKADEAK 1450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1383 QEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAeal 1462
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA--- 1527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1463 tqRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLraveereraEAEGREREAR 1542
Cdd:PTZ00121 1528 --KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA---------KKAEEARIEE 1596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1543 ALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLR 1622
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1623 LEVTVQALKTQHERDLQGRDEAGEER-----RRQLAKQLRDAEVERDEERKQRALAVAARKklEGELEELKAQMASAGQG 1697
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKkaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKK--EAEEDKKKAEEAKKDEE 1754
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1698 KEEAVKQLRKMQAQMKELWREVEET---RSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADE 1774
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKE 1834
|
890
....*....|....*....
gi 1743142585 1775 VAngnLSKAAILEEKRQLE 1793
Cdd:PTZ00121 1835 VA---DSKNMQLEEADAFE 1850
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1031-1911 |
1.62e-14 |
|
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: 79.63 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1031 KVTTEAKMKKFEEDLLLLEDqnSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQE 1110
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEE--AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1111 -LEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAER 1189
Cdd:pfam02463 220 eLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1190 VARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEtrihEAAVQELRQRHGQALgELAEQ 1269
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKLQEKLE-QLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1270 LEQARRGKGAWEKTRLALEAEVSELRAELSSlqtarqEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELEN 1349
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEK------EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1350 VSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEA-----------EAAGLREQLEEEAAARE 1418
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkeskarsglkvLLALIKDGVGGRIISAH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1419 RAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLE--- 1495
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaql 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1496 QQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALL 1575
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1576 SSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELT------AAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERR 1649
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVqeaqdkINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1650 RQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMasagqgKEEAVKQLRKMQAQMKELWREVEETRSSREEI 1729
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL------KEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1730 FsqnrESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSN 1809
Cdd:pfam02463 843 K----EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1810 SELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLE 1889
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900
....*....|....*....|...
gi 1743142585 1890 QETRERI-LSGKLVRRAEKRLKE 1911
Cdd:pfam02463 999 RLEEEKKkLIRAIIEETCQRLKE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1102-1982 |
1.64e-14 |
|
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: 79.73 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1102 RKEEKGRQELEKLKRRLDgessELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEA 1181
Cdd:TIGR02169 170 RKKEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1182 QEDLEAERvarTKAEKQRRDLGEELEALRGELEDtldstnAQQELRSKREQEVTELKKTLEE---ETRIHEAAVQELRQR 1258
Cdd:TIGR02169 246 LASLEEEL---EKLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGEleaEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1259 HGQALGELAEQLEQARRGKGAWEKtrlaLEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAE 1338
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEE----LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1339 KLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEaaglreqleeeaaare 1418
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK---------------- 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1419 ragreLQTAQAQLSEWRrrqeeeagaleageearrraareaealtQRLAEKTEAVDRLERGRRRLQQELDDAsvdlEQQR 1498
Cdd:TIGR02169 457 -----LEQLAADLSKYE----------------------------QELYDLKEEYDRVEKELSKLQRELAEA----EAQA 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1499 QLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARalsltraleeeqeareelerqnrALRAELEALLSSK 1578
Cdd:TIGR02169 500 RASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEV-----------------------AAGNRLNNVVVED 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1579 DDVGKSVHELERACRV---------------------AEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTqherd 1637
Cdd:TIGR02169 557 DAVAKEAIELLKRRKAgratflplnkmrderrdlsilSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEA----- 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1638 lqGRDEAGEERRRQLAKQLRD--------AEVERDEERKQRALAVAARkKLEGELEELKAQMASAGQGKEEAVKQLRKMQ 1709
Cdd:TIGR02169 632 --ARRLMGKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAELQ-RLRERLEGLKRELSSLQSELRRIENRLDELS 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1710 AQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAAsdrarrqAQQDRDEMADEVANGNLSKAAILEEK 1789
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN-------VKSELKELEARIEELEEDLHKLEEAL 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1790 RQLEGRLGQLEEELEEEQSNSelLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAgarar 1869
Cdd:TIGR02169 782 NDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK----- 854
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1870 hkmTIAALESKLAQAEEQLEQ-ETRERILSGKLVRRAEKRlKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAE 1948
Cdd:TIGR02169 855 ---EIENLNGKKEELEEELEElEAALRDLESRLGDLKKER-DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1743142585 1949 EEASRAQAGRRRLQRE------LEDVTESAESMNREVTTL 1982
Cdd:TIGR02169 931 EELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
904-1150 |
5.03e-13 |
|
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: 74.71 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 904 QVTRQDEVLQARAQELQKVQELQQQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVS 983
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 984 ELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLE 1063
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1064 DRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQL 1143
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
....*..
gi 1743142585 1144 GRKEEEL 1150
Cdd:TIGR02168 939 DNLQERL 945
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
907-1368 |
6.82e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 6.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 907 RQDEVLQARAQELQKVQELQQQsAREVRELQGRVAQLEEERARlAEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 986
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKK-AEEDKKKADELKKAAAAKKK-ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 987 ARVGEE----EECSRQMQTEKKRLQQhiqeleahleaeegARQKLQLEKVTTEAKMKKfeEDLLLLEDQNSKLSKERKLL 1062
Cdd:PTZ00121 1456 AKKAEEakkkAEEAKKADEAKKKAEE--------------AKKADEAKKKAEEAKKKA--DEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1063 EDRLAEfSSQAAEEEEKVKSLNKLRLKYEAtitdmeDRLRKEEKGRQELEKLKrrldgesselqeqmVEQQQRAEELRSQ 1142
Cdd:PTZ00121 1520 EAKKAD-EAKKAEEAKKADEAKKAEEKKKA------DELKKAEELKKAEEKKK--------------AEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1143 LGRKEEELQAAlaraedeggARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNA 1222
Cdd:PTZ00121 1579 ALRKAEEAKKA---------EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1223 QQELRSKREQEV--TELKKTLEEETRIHEAAVQELRQRHGQalgelAEQLEQARRGKGAWEKTRLALEAEVSelRAElsS 1300
Cdd:PTZ00121 1650 EELKKAEEENKIkaAEEAKKAEEDKKKAEEAKKAEEDEKKA-----AEALKKEAEEAKKAEELKKKEAEEKK--KAE--E 1720
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1301 LQTARQEGEQRRRRLESQLQEVQGRAgdgERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKEL 1368
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
922-1384 |
9.15e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 922 VQELQQQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELV---VSELEARVGEEEECSRQ 998
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegsKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 999 MQTEKKRLQQHIQELEAHleaeegarQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEE 1078
Cdd:PRK03918 271 LKKEIEELEEKVKELKEL--------KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1079 KVKSLNKLRLKYEAtitdMEDRLRKEEKGRQ---ELEKLKRRLDGESSELQEQMVEQQQRAEElrsQLGRKEEELQAALA 1155
Cdd:PRK03918 343 LKKKLKELEKRLEE----LEERHELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKE---EIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1156 RAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAE---------KQRRDLGEELEALRGELEDTLDSTNAQQEL 1226
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEytaelkrieKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1227 RskREQEVTELKKTLEEETRIH-----EAAVQELRQRHGQALGELAEQ--LEQARRGKGAWEKTRLALEAEVSELRAELS 1299
Cdd:PRK03918 496 I--KLKELAEQLKELEEKLKKYnleelEKKAEEYEKLKEKLIKLKGEIksLKKELEKLEELKKKLAELEKKLDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1300 SLQTARQEGEQRRRR---------------------LESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAE 1358
Cdd:PRK03918 574 ELLKELEELGFESVEeleerlkelepfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
490 500 510
....*....|....*....|....*....|....*...
gi 1743142585 1359 S------------KTIRLSKELSSTEAQLHDAQELLQE 1384
Cdd:PRK03918 654 KkyseeeyeelreEYLELSRELAGLRAELEELEKRREE 691
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1028-1774 |
9.36e-13 |
|
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: 73.95 E-value: 9.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1028 QLEKVTTEaKMKKFEEDLLLLEDQNSK---LSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKE 1104
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1105 EKgrqeleKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARaedeggaRAQLLKSLREAQAALAEAQED 1184
Cdd:TIGR02169 278 NK------KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER-------LAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1185 LEAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQaLG 1264
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE-LA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1265 ELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGER------ARAEAAE 1338
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelaeaeAQARASE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1339 KLQRAQAELENVSGALNEAESKTI--------------------RLSKELSSTEAQLHDAQELLQEET--RAKLALGSRV 1396
Cdd:TIGR02169 504 ERVRGGRAVEEVLKASIQGVHGTVaqlgsvgeryataievaagnRLNNVVVEDDAVAKEAIELLKRRKagRATFLPLNKM 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1397 RAMEAEAAGLREQLEEEAA------------------ARERAGRELQTAQAQLSEWRR-----RQEEEAGALEAGEEARR 1453
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAvdlvefdpkyepafkyvfGDTLVVEDIEAARRLMGKYRMvtlegELFEKSGAMTGGSRAPR 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1454 RAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVS--------------TLEKKQRKFDQLLAEEK 1519
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSdasrkigeiekeieQLEQEEEKLKERLEELE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1520 AAVLRAVEERERAEAEGREREARALSLTRALEEEQEAReelerqnralrAELEALLSskddvgksvheleracrvaeqaa 1599
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----------NDLEARLS----------------------- 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1600 ndlRAQVTELEDELTAAEDAKLRLEVTVQALKtQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKK 1679
Cdd:TIGR02169 790 ---HSRIPEIQAELSKLEEEVSRIEARLREIE-QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1680 LEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREeifsqnrESEKRLKGLEAEVLRLQEELAASDR 1759
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEIED 938
|
810
....*....|....*
gi 1743142585 1760 ARRQAQQDRDEMADE 1774
Cdd:TIGR02169 939 PKGEDEEIPEEELSL 953
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1326-1983 |
4.84e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1326 AGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTE-AQLHDAQELLQEETRAKLALgsrvRAMEAEAA 1404
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEAR----KAEDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1405 glreQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGAlEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQ 1484
Cdd:PTZ00121 1179 ----EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKA-EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1485 QELDDASVDLEQQRQLVSTLEKKQRKFDQLL-AEEKAAVLRAVEERERAEAEGREREARAlslTRALEEEQEAREELERQ 1563
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKkAEEKKKADEAKKAEEKKKADEAKKKAEE---AKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1564 NRALRAELEALlSSKDDVGKSvhELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQA--LKTQHERDLQGR 1641
Cdd:PTZ00121 1331 ADAAKKKAEEA-KKAAEAAKA--EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKA 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1642 DE---AGEERRRQLAKQLRDAEVERDEERKQRA----LAVAARKKLE--GELEELKAQMASAGQGKEEAVKQLRKMQAQm 1712
Cdd:PTZ00121 1408 DElkkAAAAKKKADEAKKKAEEKKKADEAKKKAeeakKADEAKKKAEeaKKAEEAKKKAEEAKKADEAKKKAEEAKKAD- 1486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1713 kELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDE---MADEVANGNLSKAAilEEK 1789
Cdd:PTZ00121 1487 -EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekkKADELKKAEELKKA--EEK 1563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1790 RQLEgrlgqleeeLEEEQSNSELLNDRYRKLLLQVESLTTELSA---ERSFSAKAESGRQQLERQIQELRGRLGEEDaga 1866
Cdd:PTZ00121 1564 KKAE---------EAKKAEEDKNMALRKAEEAKKAEEARIEEVMklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--- 1631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1867 RARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAE---KRLKEVVLQVEEERRVADQLRDQLEKGNlRVKQLKRQ 1943
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKK 1710
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1743142585 1944 LEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLR 1983
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1184-1943 |
8.22e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1184 DLEAERVARTKAEkqRRDLGEELEALRGELEDtldstNAQQELRSKREQEVTELKKTLEEETRIHEA--AVQELRQRHGQ 1261
Cdd:PTZ00121 1049 DEDIDGNHEGKAE--AKAHVGQDEGLKPSYKD-----FDFDAKEDNRADEATEEAFGKAEEAKKTETgkAEEARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1262 ALGELAEQLEQARRGkgawEKTRLALEAEVSELRAELSSLQTARqegeqrrrrlESQLQEVQGRAGDGERAR-AEAAEKL 1340
Cdd:PTZ00121 1122 KKAEDARKAEEARKA----EDARKAEEARKAEDAKRVEIARKAE----------DARKAEEARKAEDAKKAEaARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1341 QRAQaELENVSGALNEAESKtiRLSKELSSTEAQLHDAQELLQEETRAKLAlgsRVRAMEAEAAGLREQLEEEAAARERA 1420
Cdd:PTZ00121 1188 RKAE-ELRKAEDARKAEAAR--KAEEERKAEEARKAEDAKKAEAVKKAEEA---KKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1421 GRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASvdleqqrQL 1500
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD-------AA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1501 VSTLEKKQRKFDQLLAEEKAAvlravEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDD 1580
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAA-----ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1581 VGKSVHELERACRVAEQAANDLRA-QVTELEDELTAAEDAKLRLEVTVQA----LKTQHERDLQGRDEAGEERRR--QLA 1653
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKAeeakKKAEEAKKADEAKKKAEEAKKadEAK 1489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1654 KQLRDAEVERDEERKqralAVAARKKLEGELEELKAQMASAGQGKEEAVK--QLRKMQAQMK-ELWREVEETRSSREEif 1730
Cdd:PTZ00121 1490 KKAEEAKKKADEAKK----AAEAKKKADEAKKAEEAKKADEAKKAEEAKKadEAKKAEEKKKaDELKKAEELKKAEEK-- 1563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1731 sQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAailEEKRQLEGRLGQLEEELEEEQSNS 1810
Cdd:PTZ00121 1564 -KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA---EEAKIKAEELKKAEEEKKKVEQLK 1639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1811 ELLNDRYRKlllqVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKmtiaalESKLAQAEEQLEQ 1890
Cdd:PTZ00121 1640 KKEAEEKKK----AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK------EAEEAKKAEELKK 1709
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1743142585 1891 ETRERILSGKLVRRAEK----RLKEVVLQVEEERRVADQLRDQLEKGNlRVKQLKRQ 1943
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEenkiKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKE 1765
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
907-1243 |
3.39e-11 |
|
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: 68.94 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 907 RQDEVLQARAQELQKVQELQqqsaREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 986
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 987 ARVGEEEECSRQMqtEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDqnsklskERKLLEDRL 1066
Cdd:TIGR02169 772 EDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK-------EIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1067 AEFSSQAAEEEEKVKSLNklrlkyeATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRK 1146
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLN-------GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1147 EE---ELQAALARAEDEggaraqllksLREAQAALAEAQEDLEAERVARtKAEKQRRDLGEELEALRG-------ELEDT 1216
Cdd:TIGR02169 916 RKrlsELKAKLEALEEE----------LSEIEDPKGEDEEIPEEELSLE-DVQAELQRVEEEIRALEPvnmlaiqEYEEV 984
|
330 340
....*....|....*....|....*..
gi 1743142585 1217 LDSTNAQQELRSKREQEVTELKKTLEE 1243
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
970-1373 |
5.05e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 970 RLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLqlEKVTTEAK-MKKFEEDLLLL 1048
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--EKLEKEVKeLEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1049 EDQNSKLSKERKLLEDRLAEFSSQAAEE-------EEKVKSLNKLRLKYEATITdMEDRLRKEEKGRQELEKLKRRLDGE 1121
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELkkeieelEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1122 SSELQEQMVEQQQRAEELRsQLGRKEEELQAALARAEDeggaRAQLLKSLREAQAalaeaqedlEAERVARTKAEKQRRD 1201
Cdd:PRK03918 323 INGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEE----RHELYEEAKAKKE---------ELERLKKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1202 LGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEE---ETRIHEAAVQELRQRH-GQALGELAEQLEQArrgk 1277
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkAKGKCPVCGRELTEEHrKELLEEYTAELKRI---- 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1278 gawEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLE--SQLQEVQgragdgERARAEAAEKLQRAQAELENVSGALN 1355
Cdd:PRK03918 465 ---EKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELE------EKLKKYNLEELEKKAEEYEKLKEKLI 535
|
410
....*....|....*...
gi 1743142585 1356 EAESKTIRLSKELSSTEA 1373
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEE 553
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1594-1988 |
8.95e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 8.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1594 VAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDeERKQRala 1673
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERR--- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1674 vaaRKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSsreEIFSQNRESEKRLKGLEAEVLRLQ-- 1751
Cdd:COG4913 361 ---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLErr 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1752 ------EELAASDRARRQAQQDRDEM----------ADE-------------------VANGNLSKAAILEEKRQLEGRL 1796
Cdd:COG4913 435 ksnipaRLLALRDALAEALGLDEAELpfvgelievrPEEerwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1797 GQLEEELEEEQSNSELLNDR--YRKLLLQVESLTTELSAE--RSFS-AKAESGRQ--QLERQIQE-----LRGRLGEEDA 1864
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAElgRRFDyVCVDSPEElrRHPRAITRagqvkGNGTRHEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1865 ----------GARARHKmtIAALESKLAQAEEQLEQ-ETRERILSGKL-----VRRAEKRLKEV------VLQVEEERRV 1922
Cdd:COG4913 595 rrrirsryvlGFDNRAK--LAALEAELAELEEELAEaEERLEALEAELdalqeRREALQRLAEYswdeidVASAEREIAE 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1923 ADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1107-1917 |
4.75e-10 |
|
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: 65.14 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1107 GRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSlreaqaalaeaqedle 1186
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRR---------------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1187 aERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQElrskreqevtELKKTLEEetriHEAAVQELRQrhgqalgeL 1266
Cdd:pfam15921 136 -ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIE----------QLRKMMLS----HEGVLQEIRS--------I 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1267 AEQLEQARrGKGAWEKTRLA------LEAEVSELraeLSSLQTARQEGEQRRRRLESQLqevqgragdgERARAEAAEK- 1339
Cdd:pfam15921 193 LVDFEEAS-GKKIYEHDSMStmhfrsLGSAISKI---LRELDTEISYLKGRIFPVEDQL----------EALKSESQNKi 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1340 ---LQRAQAELENVsgaLNEAESKTIRLSKELSSTEAQLHDAQ---ELLQEETRAKLALGSR-VRAMEAEAAGLREQLEE 1412
Cdd:pfam15921 259 ellLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQsqlEIIQEQARNQNSMYMRqLSDLESTVSQLRSELRE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1413 EAAARERAGRELQT----AQAQLSEWRRRQEE---EAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRR---- 1481
Cdd:pfam15921 336 AKRMYEDKIEELEKqlvlANSELTEARTERDQfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSitid 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1482 RLQQELDDASVDLEQQRQLVSTLEKK-QRKFDQLLAEEKAavlraveereraeaegrerearalsltraleeeqeaREEL 1560
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQG------------------------------------KNES 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1561 ERQNRALRAELEallSSKDDVGKSVHEL---ERACRVAEQAANDLRAQVTELED--ELTAAEDAKLRLEVTVQALKTQHe 1635
Cdd:pfam15921 460 LEKVSSLTAQLE---STKEMLRKVVEELtakKMTLESSERTVSDLTASLQEKERaiEATNAEITKLRSRVDLKLQELQH- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1636 rdLQGRDEageerrrqlakQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKEL 1715
Cdd:pfam15921 536 --LKNEGD-----------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDR 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1716 WREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGR 1795
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1796 LGQLEEELEEEQsnsellndryRKLLLQVESLTTELSAERSFSAKAESGRQQ-------LERQIQELRGRLG-------- 1860
Cdd:pfam15921 683 FRNKSEEMETTT----------NKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQIDalqskiqf 752
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1861 -EEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVE 1917
Cdd:pfam15921 753 lEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1098-1941 |
5.07e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1098 EDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEElqaALARAED----EGGARAQLLKSLRE 1173
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEE---AKKKAEDarkaEEARKAEDARKAEE 1144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1174 AQAALAEAQEDLEAERVARTKAEKQRRdlgeELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQ 1253
Cdd:PTZ00121 1145 ARKAEDAKRVEIARKAEDARKAEEARK----AEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1254 ELRQRhgqalgelAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDgERAR 1333
Cdd:PTZ00121 1221 EDAKK--------AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE-EKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1334 AEAAEKLQraqaELENVSGALNEAESKtiRLSKELSS-TEAQLHDAQELLQEETRAKLAlgSRVRAMEAEAAglreqlee 1412
Cdd:PTZ00121 1292 ADEAKKAE----EKKKADEAKKKAEEA--KKADEAKKkAEEAKKKADAAKKKAEEAKKA--AEAAKAEAEAA-------- 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1413 eAAARERAGRELQTAQAQLSEWRRRQEEeagaleageearrraareaealtqrLAEKTEAVDRLERGRRRLQQELDDASv 1492
Cdd:PTZ00121 1356 -ADEAEAAEEKAEAAEKKKEEAKKKADA-------------------------AKKKAEEKKKADEAKKKAEEDKKKAD- 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1493 DLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAEle 1572
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-- 1486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1573 ALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKlRLEVTVQALKTQHERDLQGRDEAGEERRRQL 1652
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK-KADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1653 AKQLRDAeverdEERKQRAL--AVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELwREVEETRSSREEIF 1730
Cdd:PTZ00121 1566 AEEAKKA-----EEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-KKAEEEKKKVEQLK 1639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1731 SQNRESEKRlkgleAEVLRLQEElaasDRARRQAQQDRDEMADEVANGNLSKAAilEEKRQLEGRLGQLEEELEEEQSNS 1810
Cdd:PTZ00121 1640 KKEAEEKKK-----AEELKKAEE----ENKIKAAEEAKKAEEDKKKAEEAKKAE--EDEKKAAEALKKEAEEAKKAEELK 1708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1811 ELLNDRYRKlllqVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEedagararhKMTIAALESKLAQAEEQLEQ 1890
Cdd:PTZ00121 1709 KKEAEEKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE---------KKKIAHLKKEEEKKAEEIRK 1775
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1743142585 1891 EtRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLK 1941
Cdd:PTZ00121 1776 E-KEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK 1825
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1462-1986 |
6.92e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1462 LTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKkqrkFDQLLAEEKAAVLRAVEERERAEAEGREREA 1541
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET----LEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1542 RALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHEleraCRVAEQAAND----LRAQVTELEDELTAAE 1617
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE----CRVAAQAHNEeaesLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1618 DAKLRLEVTVQALKTQhERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAgqg 1697
Cdd:PRK02224 363 EEAAELESELEEAREA-VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA--- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1698 kEEAVKQLRKMQAQMK--ELWREVEEtrssrEEIFSQNRESEKRLKGLEAEVLRLQEElaasdRARRQAQQDRDEMADEV 1775
Cdd:PRK02224 439 -RERVEEAEALLEAGKcpECGQPVEG-----SPHVETIEEDRERVEELEAELEDLEEE-----VEEVEERLERAEDLVEA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1776 AngnlSKAAILEEKRQ-LEGRLGQLEEELEEEQSNSELLNDRyrklllqVESLTTELSAERSFSAKAESGRQQLERQIQE 1854
Cdd:PRK02224 508 E----DRIERLEERREdLEELIAERRETIEEKRERAEELRER-------AAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1855 LRGRLGEEDAGARARHKmtIAALESKLAQAEEQLEqetrerilsgklvRRAEKRlkevvlqvEEERRVADQLRDQLEKGN 1934
Cdd:PRK02224 577 LNSKLAELKERIESLER--IRTLLAAIADAEDEIE-------------RLREKR--------EALAELNDERRERLAEKR 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1743142585 1935 LRVKQLKRQLeeAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1986
Cdd:PRK02224 634 ERKRELEAEF--DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1127-1694 |
9.86e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1127 EQMVEQQQRAEELRSQLgRKEEELQAALARAEDEGGARAQLLKSLREAqaalaeaqeDLEAERVARTKAEKQRRDLGEEL 1206
Cdd:COG4913 228 DALVEHFDDLERAHEAL-EDAREQIELLEPIRELAERYAAARERLAEL---------EYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1207 EALRGELEDTldstnaqqelrskrEQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLA 1286
Cdd:COG4913 298 EELRAELARL--------------EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1287 LEAEVSELRAEL----SSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENV-SGALN-EAESK 1360
Cdd:COG4913 364 LEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLeRRKSNiPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1361 TIR--LSKELSSTEAQLHDAQELLQ---EETR----AKLALGSRVRAM------EAEAAglreqleeEAAARERAGRELQ 1425
Cdd:COG4913 444 ALRdaLAEALGLDEAELPFVGELIEvrpEEERwrgaIERVLGGFALTLlvppehYAAAL--------RWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1426 TAQAQLS-EWRRRQEEEAGALEAGEEARRRAARE--AEALTQRLA-EKTEAVDRLERGRRRLQQ-----------ELDDA 1490
Cdd:COG4913 516 YERVRTGlPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDyVCVDSPEELRRHPRAITRagqvkgngtrhEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1491 SvDLEQQRQL-VSTLEKKQRKFDQL-LAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALR 1568
Cdd:COG4913 596 R-RIRSRYVLgFDNRAKLAALEAELaELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1569 AELEALLSSKDDVGksvhELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDlqgRDEAGEER 1648
Cdd:COG4913 675 AELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLEL 747
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1743142585 1649 RRQLAKQLRDAEVERDEERKQRALAvAARKKLEGELEELKAQMASA 1694
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLE-ERIDALRARLNRAEEELERA 792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
912-1349 |
9.97e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 9.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 912 LQARAQELQKVQELQQQSAREVRELQGRVAQLE---EERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEAR 988
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 989 VGEEEECSRqmqtEKKRLQQHIQELEAHLEAEEGARQKL----QLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLED 1064
Cdd:PRK03918 337 EERLEELKK----KLKELEKRLEELEERHELYEEAKAKKeeleRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1065 RLAEFSSQAAEEEEKVKSLNK-------------------LRLKYEATITDMEDRLR----KEEKGRQELEKLKRRLDGE 1121
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkeLLEEYTAELKRIEKELKeieeKERKLRKELRELEKVLKKE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1122 SSEL-QEQMVEQQQRAEELRSQLGRKEEELQAALARA--EDEGGARAQlLKSLREAQAALAEAQEDLEAERVARTKAEKQ 1198
Cdd:PRK03918 493 SELIkLKELAEQLKELEEKLKKYNLEELEKKAEEYEKlkEKLIKLKGE-IKSLKKELEKLEELKKKLAELEKKLDELEEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1199 RRDLGEELEALRGELEDTLDSTnaQQELRS---------KREQEVTELKKTLEEETRIHEAAVQELrQRHGQALGELAEQ 1269
Cdd:PRK03918 572 LAELLKELEELGFESVEELEER--LKELEPfyneylelkDAEKELEREEKELKKLEEELDKAFEEL-AETEKRLEELRKE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1270 LEQARRGKGawEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEaAEKLQRAQAELEN 1349
Cdd:PRK03918 649 LEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE-LEKLEKALERVEE 725
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
932-1295 |
1.20e-09 |
|
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: 63.93 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 932 EVRELQGRVAQLEEERARLAEQLRAEAELCAEAeetRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQ 1011
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDEL---SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1012 eleahleaeegarqklqlEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEfsSQAAEEEEKVKSLNKLRLKYE 1091
Cdd:TIGR02169 752 ------------------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1092 ATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAqllksl 1171
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------ 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1172 reaqaalaeaqeDLEAErvaRTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAA 1251
Cdd:TIGR02169 886 ------------DLKKE---RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1252 -----VQELRQRHGQALGELA-------EQLEQARRGKGAWEKTRLALEAEVSELR 1295
Cdd:TIGR02169 951 lsledVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
997-1295 |
3.22e-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: 62.06 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 997 RQMQTEKKRLQQH-IQELEAHLEAEEGARQKLQLEKVTTEAKMKKfeEDLLLLEDQNSKLSKERKL----LEDRLAEF-- 1069
Cdd:pfam17380 287 RQQQEKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKRELer 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1070 --SSQAAEEEEKVKSLNKLRLkyeatitdmeDRLRKEEKGRQELE---KLKRRLDGESSELQEQMVEQQQ---RAEELRS 1141
Cdd:pfam17380 365 irQEEIAMEISRMRELERLQM----------ERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQiraEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1142 -QLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEElealrgELEDTLDST 1220
Cdd:pfam17380 435 rEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAM 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1221 NAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRgkgawEKTRL-ALEAEVSELR 1295
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE-----ERSRLeAMEREREMMR 579
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
917-1220 |
3.25e-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: 62.06 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 917 QELQKVQELQQQSAREVRElQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAA-----------RKQELELVVSEL 985
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKME-QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeqermameRERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 986 EAR----VGEEE---ECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1058
Cdd:pfam17380 358 RKRelerIRQEEiamEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1059 RKLLEDRLAEFSSQAAEEEEKVKSLNKLRlKYEATITDMEDRLRKEEKGRQELEKLKRR-LDGESSELQEQMVEQQQRae 1137
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLR-QQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERK-- 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1138 elRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEEL---EALRGELE 1214
Cdd:pfam17380 515 --RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIvesEKARAEYE 592
|
....*.
gi 1743142585 1215 DTLDST 1220
Cdd:pfam17380 593 ATTPIT 598
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
907-1625 |
3.81e-09 |
|
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: 62.30 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 907 RQDEVLQARAQELQKVQELQQQSarevrelqgrVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 986
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEE----------IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 987 ARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLL-LEDQNSKLSKERKLLEDR 1065
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGkLTEEKEELEKQELKLLKD 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1066 LAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRL-DGESSELQEQMVEQQQRAEELRSQLG 1144
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIkDGVGGRIISAHGRLGDLGVAVENYKV 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1145 RKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLgEELEALRGELEDTLDSTNAQQ 1224
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDP-ILNLAQLDKATLEADEDDKRA 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1225 ELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTA 1304
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1305 RQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSgaLNEAESKTIRLSKELSSTEAQLHDAQELLQE 1384
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE--EEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1385 ETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEwrrRQEEEAGALEAGEEARRRAAREAEALTQ 1464
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK---IKEEELEELALELKEEQKLEKLAEEELE 857
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1465 RLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQL---LAEEKAAVLRAVEERERAEAEGREREA 1541
Cdd:pfam02463 858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQklnLLEEKENEIEERIKEEAEILLKYEEEP 937
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1542 RALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGksvheleracRVAEQAANDLRAQVTELEDELTAAEDAKL 1621
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLM----------AIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
....
gi 1743142585 1622 RLEV 1625
Cdd:pfam02463 1008 IRAI 1011
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1392-1940 |
5.61e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1392 LGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEA---GALEAGEEARRRAAREAEALTQRLAE 1468
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1469 KTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEEREraeaegrerearalSLTR 1548
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE--------------SLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1549 ALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQ 1628
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1629 ALKTqherDLQGRDEAGEERRRQLA--------KQLRDAE-VERDEERKQRalavaaRKKLEGELEELKAQMASAGQgKE 1699
Cdd:PRK02224 430 ELEA----TLRTARERVEEAEALLEagkcpecgQPVEGSPhVETIEEDRER------VEELEAELEDLEEEVEEVEE-RL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1700 EAVKQLRKMQAQMKELwrevEETRSSREEIFSQNRES--EKRLKgleAEVLRLQ-EELAASDRARRQAQQDRDEMADEVA 1776
Cdd:PRK02224 499 ERAEDLVEAEDRIERL----EERREDLEELIAERRETieEKRER---AEELRERaAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1777 ngnlskaailEEKRQLEGRLGQLEEELEEEqsnsellnDRYRKLLLQVESLTTELSAERS-FSAKAESGRQQLERqIQEL 1855
Cdd:PRK02224 572 ----------EEVAELNSKLAELKERIESL--------ERIRTLLAAIADAEDEIERLREkREALAELNDERRER-LAEK 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1856 RGR---LGEEDAGARarhkmtIAALESKLAQAEEQLEQetreriLSGKLVRRAEKR--LKEVVLQVEEERRVADQLRDQL 1930
Cdd:PRK02224 633 RERkreLEAEFDEAR------IEEAREDKERAEEYLEQ------VEEKLDELREERddLQAEIGAVENELEELEELRERR 700
|
570
....*....|
gi 1743142585 1931 EKGNLRVKQL 1940
Cdd:PRK02224 701 EALENRVEAL 710
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1056-1394 |
7.41e-09 |
|
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: 61.24 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1056 SKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQR 1135
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1136 AEELRSQLgrkeEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAeRVARTKAEKQRRDLgEELEALRGELED 1215
Cdd:TIGR02169 739 LEELEEDL----SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA-RLSHSRIPEIQAEL-SKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1216 TLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRgkgawektrlaLEAEVSELR 1295
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE-----------LEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1296 AELSSLQtarqegeQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAEsKTIRLSKELSSTEAQL 1375
Cdd:TIGR02169 882 SRLGDLK-------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSL 953
|
330
....*....|....*....
gi 1743142585 1376 HDAQELLQEETRAKLALGS 1394
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEP 972
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1600-1982 |
8.50e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1600 NDLRAQVTELEDELTAAEDAKLRLEVTVQALK---TQHERDLQGRDEAGEERRrQLAKQLRDAEVERDEERKQRALAVAA 1676
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIE-DLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1677 RKKLEGELEELKAQmASAGQGKEEAVKQLRKmqaqmkELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEElaa 1756
Cdd:PRK02224 288 LEELEEERDDLLAE-AGLDDADAEAVEARRE------ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER--- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1757 SDRARRQAQQDRDEMAD---EVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSA 1833
Cdd:PRK02224 358 AEELREEAAELESELEEareAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1834 ERSFSAKAESGR---------QQLERQ-----IQELRGRLGEEDAgARARHKMTIAALESKLAQAEEQLEQETRerilsg 1899
Cdd:PRK02224 438 ARERVEEAEALLeagkcpecgQPVEGSphvetIEEDRERVEELEA-ELEDLEEEVEEVEERLERAEDLVEAEDR------ 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1900 klVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEE----ASRAQAGRRR---LQRELEDVTESA 1972
Cdd:PRK02224 511 --IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAaaeaEEEAEEAREEvaeLNSKLAELKERI 588
|
410
....*....|
gi 1743142585 1973 ESMNREVTTL 1982
Cdd:PRK02224 589 ESLERIRTLL 598
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1050-1287 |
2.93e-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: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1050 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQM 1129
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1130 VEQQQR-AEELRSQLGRKEEELQAALARAEDEGGA--RAQLLKSL-REAQAALAEAQEDLEAERVARTKAEKQRrdlgEE 1205
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLaPARREQAEELRADLAELAALRAELEAER----AE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1206 LEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRL 1285
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
..
gi 1743142585 1286 AL 1287
Cdd:COG4942 256 PW 257
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
969-1367 |
9.40e-08 |
|
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: 57.77 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 969 GRLAARKQELELVVSELEARVGEEEECsrqmQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLL 1048
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1049 EDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKslnklrlKYEATITDMEDRLRKEEkgrqeleklKRRLDGESSELQEQ 1128
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLH-------KLEEALNDLEARLSHSR---------IPEIQAELSKLEEE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1129 MVEQQQRAEELRSQLGRKEEELQAalarAEDEggaraqllkslreaqaalaeaQEDLEAERVArtkAEKQRRDLGEELEA 1208
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEY----LEKE---------------------IQELQEQRID---LKEQIKSIEKEIEN 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1209 LRGELEDtldsTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRhgqaLGELAEQLEQARRGKGAWEKTRLALE 1288
Cdd:TIGR02169 859 LNGKKEE----LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRKRLSELKAKLEALE 930
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1289 AEVSELRAELSSLQTaRQEGEQRRRRLESQLQEVQgragdgerARAEAAEKLQ-RAQAELENVSGALNEAESKTIRLSKE 1367
Cdd:TIGR02169 931 EELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVE--------EEIRALEPVNmLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1062-1869 |
1.16e-07 |
|
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: 57.44 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1062 LEDRLAEFSSQAAEEEEKVKSLNKLRLKYE----ATITDMEDRLRKEEKGRQELEKLKRRldgesselqeqmveQQQRAE 1137
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAMADIRRR--------------ESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1138 ELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDL--------EAE---------------RVARTK 1194
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIrsilvdfeEASgkkiyehdsmstmhfRSLGSA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1195 AEKQRRDLGEELEALRGEL---EDTLDSTNAqqELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGE---LAE 1268
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIfpvEDQLEALKS--ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1269 QLE----QARRGKGAWEKTRLALEAEVSELRAELsslQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAE------ 1338
Cdd:pfam15921 300 QLEiiqeQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnld 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1339 -KLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAAR 1417
Cdd:pfam15921 377 dQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1418 ERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQ 1497
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1498 RQLVSTLEKKQRKFDQLLAE--EKAAVLRAVEERERAEAEGREREAralsltRALEEEQEAREELERQNRALRAELEALL 1575
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQmaEKDKVIEILRQQIENMTQLVGQHG------RTAGAMQVEKAQLEKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1576 SSKDDVGKSVHELEraCRVAE----------------QAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKtqheRDLQ 1639
Cdd:pfam15921 611 ILKDKKDAKIRELE--ARVSDlelekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK----RNFR 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1640 GRDEAGEERRRQLAKQLRDAEVERDEERKQ-----------RALAVAARKKLEGELEELKAqMASAGQGKEEAVKQLRKM 1708
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghaMKVAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKE 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1709 QAQMKElwrevEETRSSRE--EIFSQNRESEKRLKGLEAEVLRLQEELA----ASDRARRQAQQDRDEMADEVANGNLSK 1782
Cdd:pfam15921 764 KHFLKE-----EKNKLSQElsTVATEKNKMAGELEVLRSQERRLKEKVAnmevALDKASLQFAECQDIIQRQEQESVRLK 838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1783 AAILEEKRQLEGRlGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAE-RSFSAKAESGRQQLERQIQELRGRLGE 1861
Cdd:pfam15921 839 LQHTLDVKELQGP-GYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHsRKTNALKEDPTRDLKQLLQELRSVINE 917
|
....*...
gi 1743142585 1862 EDAGARAR 1869
Cdd:pfam15921 918 EPTVQLSK 925
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1024-1793 |
1.61e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1024 RQKLQLEKVTTEAK-MKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLR 1102
Cdd:PRK03918 152 RQILGLDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1103 KEEKGRQELEKLKRR---LDGESSELQEQMVEQQQRAEELRSqlgrKEEELQAALARaedeggaraqlLKSLREAQAALA 1179
Cdd:PRK03918 232 ELEELKEEIEELEKElesLEGSKRKLEEKIRELEERIEELKK----EIEELEEKVKE-----------LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1180 EAQEDLEAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQ---EVTELKKTLE--EETRIHEAAVQE 1254
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1255 LRQRH-GQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARqegeqrrrrleSQLQEVQGRAGDGERAR 1333
Cdd:PRK03918 377 LKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-----------EELKKAKGKCPVCGREL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1334 AEAAEK--LQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLalgsrVRAMEAEAAGLREqle 1411
Cdd:PRK03918 446 TEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-----LKELEEKLKKYNL--- 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1412 eeaaareragrelqtaqaqlsewrrrqeeeagaleageearrraareaealtQRLAEKTEAVDRLERGRRRLQQELDDAS 1491
Cdd:PRK03918 518 ----------------------------------------------------EELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1492 VDLEQQRQLVSTLEKKQRKFDQLlaEEKAAVLraveereraeaegrerearalsltraleeeqeareelerqnraLRAEL 1571
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDEL--EEELAEL-------------------------------------------LKELE 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1572 EALLSSKDDVGKSVHELERACRvaeqAANDLRAQVTELEDELTAAEDAKLRLEvtvqalktQHERDLQGRDEAGEERRrq 1651
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYN----EYLELKDAEKELEREEKELKKLEEELD--------KAFEELAETEKRLEELR-- 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1652 laKQLRDAEVERDEERkqralavaaRKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFS 1731
Cdd:PRK03918 647 --KELEELEKKYSEEE---------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743142585 1732 QNRESEkRLKGLEAEVLRLQEELAasDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLE 1793
Cdd:PRK03918 716 LEKALE-RVEELREKVKKYKALLK--ERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1064-1513 |
2.20e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1064 DRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMED-----------RLRKEEKGRQELEKLKRRLDGESSELQEQMVEQ 1132
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERlaeleylraalRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1133 QQRAEELRSQL-----------GRKEEELQAALARAEDEGGARAQLLKSL----------------------REAQAALA 1179
Cdd:COG4913 315 EARLDALREELdeleaqirgngGDRLEQLEREIERLERELEERERRRARLeallaalglplpasaeefaalrAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1180 EAQEDLEAERVARTKAEKQRRDLGEELEALRGELEdtldstnaqqELRSKR---EQEVTELKKTLEEETRIHEAAVQ--- 1253
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEAELPfvg 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1254 ---ELRQR------------HGQALGEL--AEQLEQARRgkgAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLE 1316
Cdd:COG4913 465 eliEVRPEeerwrgaiervlGGFALTLLvpPEHYAAALR---WVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1317 SQLQEVQG-----------------------------RAG-----------DGERARAE-------AAEKLQRAQAELEN 1349
Cdd:COG4913 542 FKPHPFRAwleaelgrrfdyvcvdspeelrrhpraitRAGqvkgngtrhekDDRRRIRSryvlgfdNRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1350 VSGALNEAESKTIRLSKELSSTEAQLHDAQELLQ------------------EETRAKLALGS-RVRAMEAEAAGLREQL 1410
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaereiaelEAELERLDASSdDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1411 EEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALeaGEEARRRAAREAEALTQRLAEktEAVDRLERG-RRRLQQELDD 1489
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEERFAA--ALGDAVERElRENLEERIDA 777
|
570 580
....*....|....*....|....
gi 1743142585 1490 ASvdlEQQRQLVSTLEKKQRKFDQ 1513
Cdd:COG4913 778 LR---ARLNRAEEELERAMRAFNR 798
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1647-1970 |
3.13e-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: 56.11 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1647 ERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMK------------- 1713
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRqqekieryqedle 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1714 ELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRArRQAQQDRdemadevangnlskaAIleEKRQLE 1793
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQA-LDVQQTR---------------AI--QYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1794 GRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGE---EDAGARARH 1870
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEverSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1871 KMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEkgnlrvkQLKRQLEEAEEE 1950
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQ 572
|
330 340
....*....|....*....|
gi 1743142585 1951 ASRAQAGRRRLQRELEDVTE 1970
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRA 592
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1062-1500 |
3.41e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1062 LEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRS 1141
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1142 QLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRGELEDTLdstn 1221
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR---- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1222 aqqELRSKREQEVTELKKTLEE-ETRIHEAavQELRQRH-----GQALGE--LAEQLEQARRGKGAWEKTRLALEAEVSE 1293
Cdd:PRK02224 419 ---EERDELREREAELEATLRTaRERVEEA--EALLEAGkcpecGQPVEGspHVETIEEDRERVEELEAELEDLEEEVEE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1294 LRAELSSLQTArqegeqrrRRLESQLQEVQGRAGDGER----ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELS 1369
Cdd:PRK02224 494 VEERLERAEDL--------VEAEDRIERLEERREDLEEliaeRRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1370 STEAQLHDAQELLQEETRAKLALGS--RVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALea 1447
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF-- 643
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1743142585 1448 GEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQL 1500
Cdd:PRK02224 644 DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1692-1932 |
3.82e-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: 54.77 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1692 ASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEM 1771
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1772 adevangnlsKAAILEEKRQLEGRLGQLEEELEEEqsnsellndrYRKLLLQVESLTTELSAERSFSAKAESGRQQLErQ 1851
Cdd:COG4942 96 ----------RAELEAQKEELAELLRALYRLGRQP----------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-E 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1852 IQELRGRLGEEDAGARARHKmTIAALESKLAQAEEQLEQETRERilsGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLE 1931
Cdd:COG4942 155 LRADLAELAALRAELEAERA-ELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
.
gi 1743142585 1932 K 1932
Cdd:COG4942 231 R 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
900-1295 |
3.91e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 900 KPLLQVTRQDEVLQARAQELQKVQELQQQSAREVRELQGRVAQLeEERARLAEQLRAEAELCAEAEETRGRLAARKQELE 979
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 980 LvvSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQL--EKVTTE----------AKMKKFEEDLLL 1047
Cdd:PRK03918 393 L--EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgRELTEEhrkelleeytAELKRIEKELKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1048 LEDQNSKLSKERKLLEDRLAEFSS---------QAAEEEEKVKSLNKLRLKYEAtitdmedrlRKEEKGRQELEKLKRRL 1118
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKYNLEELEKKA---------EEYEKLKEKLIKLKGEI 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1119 DGESSELqEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLK--------------SLREAQAALAEAQED 1184
Cdd:PRK03918 542 KSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEerlkelepfyneylELKDAEKELEREEKE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1185 LEAERVARTKAEKQRRDLGEELEALRGELEDtLDSTNAQQELRSKREqEVTELKKTLEE-ETRIHEAavQELRQRHGQAL 1263
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEE-LEKKYSEEEYEELRE-EYLELSRELAGlRAELEEL--EKRREEIKKTL 696
|
410 420 430
....*....|....*....|....*....|..
gi 1743142585 1264 GELAEQLEQARRGKGAWEKTRLALEaEVSELR 1295
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALE-RVEELR 727
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1567-1988 |
4.11e-07 |
|
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: 55.51 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1567 LRAELEALLSSKDDvgkSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQ------ALKTQHERDLQG 1640
Cdd:pfam15921 329 LRSELREAKRMYED---KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHkrekelSLEKEQNKRLWD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1641 RDEAGEERRRQLAKQL--RDAEVERDEerkqrALAVAARKKLEGELEElkaQMAsAGQGKEEAVKQLRKMQAQM---KEL 1715
Cdd:pfam15921 406 RDTGNSITIDHLRRELddRNMEVQRLE-----ALLKAMKSECQGQMER---QMA-AIQGKNESLEKVSSLTAQLestKEM 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1716 WREV-EETRSSREEIFSQNR----------ESEKRLKGLEAEV--------LRLQE-----------------------E 1753
Cdd:pfam15921 477 LRKVvEELTAKKMTLESSERtvsdltaslqEKERAIEATNAEItklrsrvdLKLQElqhlknegdhlrnvqtecealklQ 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1754 LAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQsnseLLNDRYRKLLLQVESLTTELSA 1833
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSDLEL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1834 ERSFSAKAESGRQQLERQIQELRGRLGEEDAGARA----------------RHK-----MTIAALESKLAQAEEQLEQeT 1892
Cdd:pfam15921 633 EKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNelnslsedyevlkrnfRNKseemeTTTNKLKMQLKSAQSELEQ-T 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1893 RERIlsgKLVRRAEKRLKEVVLQVEEERRVAdqlRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESA 1972
Cdd:pfam15921 712 RNTL---KSMEGSDGHAMKVAMGMQKQITAK---RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
490
....*....|....*.
gi 1743142585 1973 ESMNREVTTLRNRLRR 1988
Cdd:pfam15921 786 NKMAGELEVLRSQERR 801
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
944-1353 |
5.67e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 944 EEERARLAEQlraEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEEcsrqmqtekkrLQQHIQELEahleaeegA 1023
Cdd:PRK04863 278 ANERRVHLEE---ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD-----------LEQDYQAAS--------D 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1024 RQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRK 1103
Cdd:PRK04863 336 HLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1104 EEKGRQELEKLKRRLDGES------SELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEdeggARAQLLKSLREAQAA 1177
Cdd:PRK04863 416 YQQAVQALERAKQLCGLPDltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1178 LaeaqedlEAERVARTKAEKQR--RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEetrihEAAVQEL 1255
Cdd:PRK04863 492 S-------EAWDVARELLRRLReqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-----EDELEQL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1256 RQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAE----------LSSLQTARQEGEQRRRRLESQLQEVQGR 1325
Cdd:PRK04863 560 QEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaqdaLARLREQSGEEFEDSQDVTEYMQQLLER 639
|
410 420
....*....|....*....|....*...
gi 1743142585 1326 AGDGERARAEAAEKLQRAQAELENVSGA 1353
Cdd:PRK04863 640 ERELTVERDELAARKQALDEEIERLSQP 667
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1033-1275 |
9.70e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 9.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1033 TTEAKMKKFEEDLLLLED-------QNSKLSKERKLLEDRLAEFS--SQAAEEEEKVKSLnklrlkyEATITDMEDRLRK 1103
Cdd:COG4913 607 DNRAKLAALEAELAELEEelaeaeeRLEALEAELDALQERREALQrlAEYSWDEIDVASA-------EREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1104 EEKGRQELEKLKRRLDG---ESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLlksLREAQAALAE 1180
Cdd:COG4913 680 LDASSDDLAALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE---LRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1181 AQEDLEAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSK-------REQEVTELKKTLEEEtRIHEAAVQ 1253
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdldadleSLPEYLALLDRLEED-GLPEYEER 835
|
250 260
....*....|....*....|....*
gi 1743142585 1254 ELRQRH---GQALGELAEQLEQARR 1275
Cdd:COG4913 836 FKELLNensIEFVADLLSKLRRAIR 860
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1037-1775 |
1.00e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1037 KMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRK-EEKGRQELEKLK 1115
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQsHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1116 RRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKA 1195
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1196 EKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQevteLKKTLEEETRIHeaAVQELRQRHGQALGELAEQLEQARR 1275
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI----SCQQHTLTQHIH--TLQQQKTTLTQKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1276 GKGawekTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSG-AL 1354
Cdd:TIGR00618 408 EQA----TIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQiHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1355 NEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKL-----ALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQA 1429
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidnpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1430 QLSEWRrrqeEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELddasvdLEQQRQLVSTLEKK-- 1507
Cdd:TIGR00618 564 QMQEIQ----QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL------LRKLQPEQDLQDVRlh 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1508 QRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLtraleeeqeareELERQNRALRAELEALLSSKDDVGKSVHE 1587
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK------------ELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1588 LERACRVAEQAANDLRAQVTELEDELTAAedaklrlevtvqalktqhERDLQGRDEAGEERRRQLAKQLRDAEVERDEER 1667
Cdd:TIGR00618 702 CQTLLRELETHIEEYDREFNEIENASSSL------------------GSDLAAREDALNQSLKELMHQARTVLKARTEAH 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1668 KQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEK----RLKGL 1743
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSAT 843
|
730 740 750
....*....|....*....|....*....|..
gi 1743142585 1744 EAEVLRLQEELAASDRARRQAQQDRDEMADEV 1775
Cdd:TIGR00618 844 LGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1109-1399 |
1.48e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 52.76 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1109 QELEKLKRRLdgesSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAE 1188
Cdd:pfam19220 41 RELPQAKSRL----LELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1189 RVARTKAEKQ-------RRDLGEELEALRGEL----EDTLDSTNAQQELRSKR---EQEVTELKKTLEE---ETRIHEAA 1251
Cdd:pfam19220 117 TAQAEALERQlaaeteqNRALEEENKALREEAqaaeKALQRAEGELATARERLallEQENRRLQALSEEqaaELAELTRR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1252 VQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQtarqegeqrrrrleSQLQEVQGRAGDGER 1331
Cdd:pfam19220 197 LAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLR--------------MKLEALTARAAATEQ 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1332 ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAM 1399
Cdd:pfam19220 263 LLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
940-1300 |
2.32e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 940 VAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEE--CSRQMQTEKKRLQQHIQELEAhl 1017
Cdd:pfam02029 7 AARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEeaFLDRTAKREERRQKRLQEALE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1018 eaeegaRQKlQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLlEDRLAEfssqAAEEEEKVKSLNKLRLKYEATITDM 1097
Cdd:pfam02029 85 ------RQK-EFDPTIADEKESVAERKENNEEEENSSWEKEEKR-DSRLGR----YKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1098 EDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAA 1177
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1178 LAEAQEDLEAERVARTKAEKQRRDLGE----ELEALRGEledtldstnaQQElrskREQEVTELKKTLEEETRIHEAavQ 1253
Cdd:pfam02029 233 SQEREEEAEVFLEAEQKLEELRRRRQEkeseEFEKLRQK----------QQE----AELELEELKKKREERRKLLEE--E 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1743142585 1254 ELRQRHGQALGELAEQlEQARRGKGAWEKTRlaleAEVSELRAELSS 1300
Cdd:pfam02029 297 EQRRKQEEAERKLREE-EEKRRMKEEIERRR----AEAAEKRQKLPE 338
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1026-1385 |
2.85e-06 |
|
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: 52.27 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1026 KLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDME---DRLR 1102
Cdd:COG5185 177 KKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAqtsDKLE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1103 ---------KEEKGRQELEKLKR------RLDGESSELQEQMVEQQQRAEELRSQLgRKEEELQAALARAEDEGGARAQl 1167
Cdd:COG5185 257 klveqntdlRLEKLGENAESSKRlnenanNLIKQFENTKEKIAEYTKSIDIKKATE-SLEEQLAAAEAEQELEESKRET- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1168 LKSLREAQAALAEAQEDLEaERVARTKAEKQRRDLGEELEalrgELEDTLDSTNAQQElrSKREqEVTELKKTLEEETRI 1247
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLT-ENLEAIKEEIENIVGEVELS----KSSEELDSFKDTIE--STKE-SLDEIPQNQRGYAQE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1248 HEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlesqlQEVQGRAG 1327
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEIN-----RSVRSKKE 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1328 DGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEE 1385
Cdd:COG5185 482 DLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
932-1383 |
3.23e-06 |
|
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: 52.43 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 932 EVRELQGRVAQLEEERARLAEQLRAEAELCaeaeetrgrLAARKQELELVVSELEARVG--EEEECSRQMQTEKKRLQQH 1009
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKSESQNKIELL---------LQQHQDRIEQLISEHEVEITglTEKASSARSQANSIQSQLE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1010 IQELEAHLEAEEGARQKLQLEKVTTEAKmkkfeedlllledqnSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLK 1089
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLR---------------SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1090 YEATITDMEDRLRK------EEKGRQELEK-------------------LKRRLDGESSELQEQMVEQQQRAEELRSQLG 1144
Cdd:pfam15921 368 FSQESGNLDDQLQKlladlhKREKELSLEKeqnkrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQGQME 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1145 RKEEELQAALARAEDEGGARAQllksLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEalrgELEDTLDSTNAQ- 1223
Cdd:pfam15921 448 RQMAAIQGKNESLEKVSSLTAQ----LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ----EKERAIEATNAEi 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1224 QELRSKREQEVTELK--KTLEEETRIHEAAVQELRQRHG----------QALGELAEQLEQARRGKGAWEKTRLALEAEV 1291
Cdd:pfam15921 520 TKLRSRVDLKLQELQhlKNEGDHLRNVQTECEALKLQMAekdkvieilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1292 SELRAELSSLQTARQEGEQRRRRLES-----QLQEVQGRAGDGERARAEAAEKLQRAQA--ELENVSGALN--------- 1355
Cdd:pfam15921 600 NDRRLELQEFKILKDKKDAKIRELEArvsdlELEKVKLVNAGSERLRAVKDIKQERDQLlnEVKTSRNELNslsedyevl 679
|
490 500 510
....*....|....*....|....*....|....*..
gi 1743142585 1356 ---------EAESKTIRLSKELSSTEAQLHDAQELLQ 1383
Cdd:pfam15921 680 krnfrnkseEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
861-1127 |
3.35e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 861 RRAFQKRQQQQSALRVMQRNCAaylkLRHWQWWRLFTKVKPLLQVTRQDEVLQARAQELQKVQEL-----QQQSAREVRE 935
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMA----LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaeELKKAEEEKK 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 936 LQGRVAQLEEERARLAEQLRaeaelcaeaeetrgrlaaRKQELELVVSELEARVGEEE----ECSRQMQTEKKRLQQHIQ 1011
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELK------------------KAEEENKIKAAEEAKKAEEDkkkaEEAKKAEEDEKKAAEALK 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1012 ELEAHLEAEEGARQKLQLEKVTTEaKMKKFEEDLLLLEDQNSKLSKERKlledRLAEFSSQAAEEEEKVKSLNKLRLKYE 1091
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDK----KKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1743142585 1092 ATITDMEDRL------RKEEKGRQELEKLKRRLDGESSELQE 1127
Cdd:PTZ00121 1771 EEIRKEKEAVieeeldEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
847-1089 |
3.96e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 847 IIVSFQAAARGYLARRAFQKRQQQQSALRVMQRNCAAYLKlrhwqwwrlfTKVKPLLQVTRQDEVLQARAQELQKVQELQ 926
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKK----------EEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 927 QQSAREVRELQGRVAQLEEE----RARLAEQLRAEAELCAEAEETR-------GRLAARKQELELVVSELEARVGEEEEC 995
Cdd:COG4942 79 AALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 996 SRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAE 1075
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....
gi 1743142585 1076 EEEKVKSLNKLRLK 1089
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1565-1781 |
4.51e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1565 RALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEA 1644
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1645 GeerRRQLAKQLRDAEVERDEERKQRALAVAAR------KKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWRE 1718
Cdd:COG4942 117 G---RQPPLALLLSPEDFLDAVRRLQYLKYLAParreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743142585 1719 VEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLS 1781
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1668-1911 |
4.75e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1668 KQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEV 1747
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1748 LRLQEELAASDRAR-RQAQQDR-------DEMADEVANGNLSKAAILEEKRQLEgrlgqleeeleeeqsnsellndRYRK 1819
Cdd:COG4942 100 EAQKEELAELLRALyRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAE----------------------ELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1820 LLLQVESLTTELSAERsfsAKAESGRQQLERQIQELrgrlgeedAGARARHKMTIAALESKLAQAEEQLEQETRERILSG 1899
Cdd:COG4942 158 DLAELAALRAELEAER---AELEALLAELEEERAAL--------EALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|..
gi 1743142585 1900 KLVRRAEKRLKE 1911
Cdd:COG4942 227 ALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1565-1988 |
5.94e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1565 RALRAELEALLSSKDDVGKSVHELERAcrvaEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHE-RDLQGRDE 1643
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1644 AGEERRRQLAKQLRD-AEVERDEERKQRALAVAARK---KLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREV 1719
Cdd:COG4717 150 ELEERLEELRELEEElEELEAELAELQEELEELLEQlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1720 EETRSSREEIFSQNRESEKR-----------LKGLEAEVLRLQEELAA---------------SDRARRQAQQDRDEMAD 1773
Cdd:COG4717 230 EQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1774 EVANGNLSKAAILEEKRQLEgrlgqleeeleeeqSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAEsgRQQLERQIQ 1853
Cdd:COG4717 310 LPALEELEEEELEELLAALG--------------LPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1854 ELRGRLG---EEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSgkLVRRAEKRLKEVVLQVEEERRVADQLRDQL 1930
Cdd:COG4717 374 ALLAEAGvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL--LEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1931 EKGNLRVKQLKRQLeEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG4717 452 REELAELEAELEQL-EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1114-1928 |
5.95e-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: 51.51 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1114 LKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEG----------GARAQLLKSLREAQAALAEAQE 1183
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtftrvvllpqGEFAQFLKAKSKEKKELLMNLF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1184 DLEAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRhgQAL 1263
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK--REA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1264 GELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTAR--QEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQ 1341
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1342 RA---QAELENVSGALNEAESKTIRLskelssteAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARE 1418
Cdd:TIGR00618 332 AHvkqQSSIEEQRRLLQTLHSQEIHI--------RDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1419 RAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQqELDDASVDLEQQR 1498
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK-EREQQLQTKEQIH 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1499 QLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSK 1578
Cdd:TIGR00618 483 LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1579 DDVGKSVHELER--ACRVAEQA-ANDLRAQVTELEDELTAAEDAK--LRLEVTVQALKTQHERDLQgrDEAGEERRRQLA 1653
Cdd:TIGR00618 563 EQMQEIQQSFSIltQCDNRSKEdIPNLQNITVRLQDLTEKLSEAEdmLACEQHALLRKLQPEQDLQ--DVRLHLQQCSQE 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1654 KQLRDAEVERD------EERKQRALAVAARKKLEGELEELKAQMAsagQGKEEAVKQLRKMQAQMKELWRE----VEETR 1723
Cdd:TIGR00618 641 LALKLTALHALqltltqERVREHALSIRVLPKELLASRQLALQKM---QSEKEQLTYWKEMLAQCQTLLRElethIEEYD 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1724 SSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEekrQLEGRLGQLEEEL 1803
Cdd:TIGR00618 718 REFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS---HLAAEIQFFNRLR 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1804 EEEQSNSELLNDRYRK--------LLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMT-- 1873
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQeipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIql 874
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1874 ---IAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRD 1928
Cdd:TIGR00618 875 sdkLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1565-1714 |
6.14e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1565 RALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHE-RDLQGRDE 1643
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743142585 1644 AGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKE 1714
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
930-1441 |
6.22e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 930 AREVRELQGRVAQLEEERARLAEQLRAEAELcaeaeetrgRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQH 1009
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYL---------RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1010 IQELEAHLEAEEGARQKLQLEKVtteakmKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEkvkSLNKLRLK 1089
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1090 YEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRA-----------EELRSQLGRKEEELQAAlA--- 1155
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparllalrDALAEALGLDEAELPFV-Geli 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1156 --RAEDE----------GGAR----------AQLLKSLREAQAALAeaqedLEAERVARTKAEKQRRDLGEelEALRGEL 1213
Cdd:COG4913 468 evRPEEErwrgaiervlGGFAltllvppehyAAALRWVNRLHLRGR-----LVYERVRTGLPDPERPRLDP--DSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1214 EdtLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHG------------------------QALGELAEQ 1269
Cdd:COG4913 541 D--FKPHPFRAWLEAELGRRFDYVCVDSPEELRRHPRAITRAGQVKGngtrhekddrrrirsryvlgfdnrAKLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1270 LEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRR--RRLESQLQEVQgragdGERARAEAA-EKLQRAQAE 1346
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELE-----AELERLDASsDDLAALEEQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1347 LENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQT 1426
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
570
....*....|....*
gi 1743142585 1427 AQAQLSEWRRRQEEE 1441
Cdd:COG4913 774 RIDALRARLNRAEEE 788
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1195-1970 |
8.40e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1195 AEKQRRDLGEELEALRGELEDTLDSTNAQQELR---SKREQEVTELKKTLEEE---TRIHEAAVQE-LRQ-----RHGQA 1262
Cdd:PRK04863 277 HANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaASDHLNLVQTaLRQqekieRYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1263 LGELAEQLEQ-------ARRGKGAWEKTRLALEAEVSELRAELSSLQTArqegeqrrrrlesqLQEVQGRAG---DGERA 1332
Cdd:PRK04863 357 LEELEERLEEqnevveeADEQQEENEARAEAAEEEVDELKSQLADYQQA--------------LDVQQTRAIqyqQAVQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1333 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLR-EQLE 1411
Cdd:PRK04863 423 LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVaRELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1412 EEAAARERAGRELQTAQAQLSEWRRRQEEEAGAleageearrraAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDAS 1491
Cdd:PRK04863 503 RRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA-----------ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1492 VDLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraveereraeaegrerearalsltraleeeqeareeLERQNRALRAEL 1571
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLAA---------------------------------------RAPAWLAAQDAL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1572 EALLS-SKDDVGKSvheleracrvaeQAANDLRAQVTELEDELTAAEDaklRLEVTVQALKTQHERdLQGRDEAGEERRR 1650
Cdd:PRK04863 613 ARLREqSGEEFEDS------------QDVTEYMQQLLERERELTVERD---ELAARKQALDEEIER-LSQPGGSEDPRLN 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1651 QLAK---------------------------QLRDAEVERDEERKQRALAvaarkKLEGELEELKAqmasagqgKEEAVK 1703
Cdd:PRK04863 677 ALAErfggvllseiyddvsledapyfsalygPARHAIVVPDLSDAAEQLA-----GLEDCPEDLYL--------IEGDPD 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1704 QLRKMQAQMKELWREVEETRSSREEIFSQNRE--------SEKRLKGLEAEVLRLQEELAASDRaRRQAQQDRDEMADEV 1775
Cdd:PRK04863 744 SFDDSVFSVEELEKAVVVKIADRQWRYSRFPEvplfgraaREKRIEQLRAEREELAERYATLSF-DVQKLQRLHQAFSRF 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1776 ANGNLSKA------AILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELS--AERSFSAKAESGRQQ 1847
Cdd:PRK04863 823 IGSHLAVAfeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETLADRVEEIREQ 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1848 LERqiqelrgrlGEEDAGARARHKMTIAALE---SKLAQAEEQLEQETRERILSGKLVRRAEKR---LKEVVlqveeERR 1921
Cdd:PRK04863 903 LDE---------AEEAKRFVQQHGNALAQLEpivSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVV-----QRR 968
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1743142585 1922 VA---DQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTE 1970
Cdd:PRK04863 969 AHfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1751-1993 |
8.45e-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: 50.53 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1751 QEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTE 1830
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1831 LSAERSFSAKAESGRQQLERQiQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLK 1910
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1911 EVVLQVEEERRVADQLRDQLEKgnlRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGP 1990
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
...
gi 1743142585 1991 LTF 1993
Cdd:COG4942 255 LPW 257
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1633-1943 |
9.38e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1633 QHERDLQGRDEAGEERRRQL--AKQLRDAEVERDEE-RKQRALAVAARKKLEGELEELKAQMASAgQGKEEAVKQLRKMQ 1709
Cdd:PRK04863 276 RHANERRVHLEEALELRRELytSRRQLAAEQYRLVEmARELAELNEAESDLEQDYQAASDHLNLV-QTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1710 AQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRA----------RRQAQQDRDEM-----ADE 1774
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALERAkqlcgLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1775 VANGNLSkaAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSF-----------SAKAES 1843
Cdd:PRK04863 435 LTADNAE--DWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvarellrrlrEQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1844 GR-QQLERQIQELRGRLGEEdagararhkmtiAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRV 1922
Cdd:PRK04863 513 EQlQQLRMRLSELEQRLRQQ------------QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340
....*....|....*....|.
gi 1743142585 1923 ADQLRDQLEKGNLRVKQLKRQ 1943
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAAR 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1184-1404 |
9.38e-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: 50.15 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1184 DLEAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQAL 1263
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1264 GELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRA 1343
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743142585 1344 QAELENVSGALNEAESKTIRLSKELSSTEAQLhdaQELLQEETRAKLALGSRVRAMEAEAA 1404
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
997-1213 |
9.46e-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: 50.15 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 997 RQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEE 1076
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1077 EEKVKSLNKL------------------------RLKYEATITD-MEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVE 1131
Cdd:COG4942 103 KEELAELLRAlyrlgrqpplalllspedfldavrRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1132 QQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSlreaqaalaEAQEDLEAERVARTKAEKQRRDLGEELEALRG 1211
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQE---------AEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 1743142585 1212 EL 1213
Cdd:COG4942 254 KL 255
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
908-1300 |
1.07e-05 |
|
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: 50.28 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 908 QDEVLQARAQELQKVQELQQQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEA 987
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 988 RVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLA 1067
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1068 EFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEqMVEQQQR--AEELRSQLGR 1145
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSS-MAAQRDRtqAELHQARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1146 KEEELQAALAR-AEDEGGAR-AQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRdlgEELEALRGELEDTLDSTNAQ 1223
Cdd:pfam07888 282 AQLTLQLADASlALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER---MEREKLEVELGREKDCNRVQ 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743142585 1224 qelRSKREQEVTELKKTLEEETRiheaaVQELRQRHGQALGELAEQLEQaRRGKGAWEKTRLALEAEVSELRAELSS 1300
Cdd:pfam07888 359 ---LSESRRELQELKASLRVAQK-----EKEQLQAEKQELLEYIRQLEQ-RLETVADAKWSEAALTSTERPDSPLSD 426
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
912-1270 |
1.87e-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: 49.95 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 912 LQARAQELQKVQE-LQQQSArevreLQGRVAQLEEERARLAEQlraeAELCAEAEETRGRLAARKQELELVVSELEARVG 990
Cdd:COG3096 329 YQAASDHLNLVQTaLRQQEK-----IERYQEDLEELTERLEEQ----EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 991 EEEECSRQMQTEKKRLQQHIQELEAhleaeegARQKLQLEKVTTEAkmkkFEEDLLLLEDQNSKLSKERKLLEDRLAeFS 1070
Cdd:COG3096 400 DYQQALDVQQTRAIQYQQAVQALEK-------ARALCGLPDLTPEN----AEDYLAAFRAKEQQATEEVLELEQKLS-VA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1071 SQAAEEEEKVkslnklrlkYEA--TITDMEDRLRKEEKGRQ------ELEKLKRRLDGESSELQE--QMVEQQQRAEELR 1140
Cdd:COG3096 468 DAARRQFEKA---------YELvcKIAGEVERSQAWQTAREllrryrSQQALAQRLQQLRAQLAEleQRLRQQQNAERLL 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1141 SQLGRK-------EEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRGEL 1213
Cdd:COG3096 539 EEFCQRigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQS 618
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743142585 1214 EDTLDSTNAQQELRSK---REQEVTELKKTLEEETRIHEAAVQELRQRHGQA---LGELAEQL 1270
Cdd:COG3096 619 GEALADSQEVTAAMQQlleREREATVERDELAARKQALESQIERLSQPGGAEdprLLALAERL 681
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1133-1517 |
2.16e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1133 QQRAEELRSQLGRKE-------EELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEA--ERVARTKAEKQRRDLG 1203
Cdd:COG4717 52 EKEADELFKPQGRKPelnlkelKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1204 EELEALRGELEDT---LDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAW 1280
Cdd:COG4717 132 QELEALEAELAELperLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1281 EKTRLALEAEVSELRAELSSLQTARQEGEQR----------------------RRRLESQLQEVQGRAGDGERARAEAAE 1338
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1339 KLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARE 1418
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1419 RAGRELQTAQAQLSEWRRRQE---------------EEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRL 1483
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEqaeeyqelkeeleelEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430
....*....|....*....|....*....|....
gi 1743142585 1484 QQELDDASVDLEQQRQlVSTLEKKQRKFDQLLAE 1517
Cdd:COG4717 452 REELAELEAELEQLEE-DGELAELLQELEELKAE 484
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1126-1351 |
2.18e-05 |
|
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: 48.99 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1126 QEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEE 1205
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1206 LEALRGELEDTLDStnAQQELRSKREQEVTELKKTLEEETRIheAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRL 1285
Cdd:COG4942 99 LEAQKEELAELLRA--LYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1286 ALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVS 1351
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1132-1380 |
2.22e-05 |
|
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: 48.99 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1132 QQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRG 1211
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1212 ELEdtldstnaqqelrskreqevtELKKTLEEETRiheaAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEV 1291
Cdd:COG4942 98 ELE---------------------AQKEELAELLR----ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1292 SELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSST 1371
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
....*....
gi 1743142585 1372 EAQLHDAQE 1380
Cdd:COG4942 233 EAEAAAAAE 241
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
894-1517 |
2.63e-05 |
|
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: 49.58 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 894 RLFTKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVRELQGRVAQLEEER-------------------ARLAEQL 954
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRaqeavleetqerinrarkaAPLAAHI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 955 RAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQleKVTT 1034
Cdd:TIGR00618 300 KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1035 EAKMKKFEEDLLLLEDQ----NSKLSKERKLLEDRLAEFSSQAAEEEEKV--KSLNKLRLKYEATITDMEDRLRKEEKGR 1108
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKlqslCKELDILQREQATIDTRTSAFRDLQGQLAhaKKQQELQQRYAELCAAAITCTAQCEKLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1109 Q-ELEKLKRRLDGESSELQ--EQMVEQQQRAEELRSQLGRKEEELQ----------AALARAEDEGGARAQLLKSLREAQ 1175
Cdd:TIGR00618 458 KiHLQESAQSLKEREQQLQtkEQIHLQETRKKAVVLARLLELQEEPcplcgscihpNPARQDIDNPGPLTRRMQRGEQTY 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1176 AALAEAQEDLEAE------RVARTKAEKQRRD------------LGEELEALRGELEDTLDSTNAQQELRSKREQEVTEL 1237
Cdd:TIGR00618 538 AQLETSEEDVYHQltserkQRASLKEQMQEIQqsfsiltqcdnrSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1238 KKTLEE-----ETRIHEAAVQELRQRHGQALGELAEQLEQARRgKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRR 1312
Cdd:TIGR00618 618 LRKLQPeqdlqDVRLHLQQCSQELALKLTALHALQLTLTQERV-REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1313 RRLE---SQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKEL--SSTEAQLHDAQELLQEETR 1387
Cdd:TIGR00618 697 EMLAqcqTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNNNEEVTAALQT 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1388 AklalgsrvrameAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEagaleaGEEARRRAAREAEALTQRLA 1467
Cdd:TIGR00618 777 G------------AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI------LNLQCETLVQEEEQFLSRLE 838
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1468 EKTeavdrlergrrRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAE 1517
Cdd:TIGR00618 839 EKS-----------ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
856-1270 |
2.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 856 RGYLARRAFQKRQQQQSALRVMQRNCAAYLKLRHwqwwRLFTKVKPLLQVTRQDEVLQARAQELQKVQELQ------QQS 929
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELREELEKLEKLLQLLplyqelEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 930 AREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELV----VSELEARVGEEEECSRQMQTEKKR 1005
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1006 LQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL--------------------------LLEDQNSKLSKER 1059
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglggsllsliltiagvlflvlgLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1060 KLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRA--- 1136
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAlla 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1137 -------EELRSQLGRKEE--ELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERvARTKAEKQRRDLGEELE 1207
Cdd:COG4717 378 eagvedeEELRAALEQAEEyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEE-ELEELEEELEELREELA 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743142585 1208 ALRGELEDtLDSTNAQQELRSKREQEVTELKKTLEEETRIH------EAAVQELRQRHGQALGELAEQL 1270
Cdd:COG4717 457 ELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPPVLERASEY 524
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
927-1390 |
3.28e-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: 49.07 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 927 QQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEeeecsrqmqtekkrl 1006
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE--------------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1007 qqhiqeleahleaeegARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKER----KLLEDRLAEFSSQAAEEEEKVKS 1082
Cdd:pfam12128 302 ----------------KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1083 L----NKLRLKYEATI--------TDMEDRLRKEEKGRQELEKLKR----RLDGESSELQEQMVEQQQRAEELRSQLGRK 1146
Cdd:pfam12128 366 LtgkhQDVTAKYNRRRskikeqnnRDIAGIKDKLAKIREARDRQLAvaedDLQALESELREQLEAGKLEFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1147 EEELQAALARAEdeggARAQLLKSLREAQAAlaeaqedLEAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQEL 1226
Cdd:pfam12128 446 LGELKLRLNQAT----ATPELLLQLENFDER-------IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1227 RSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELA------------EQLEQARRGKGAWEKTRLALE------ 1288
Cdd:pfam12128 515 LEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVIspellhrtdldpEVWDGSVGGELNLYGVKLDLKridvpe 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1289 --AEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAA-------EKLQRAQAELENVSGALNEAES 1359
Cdd:pfam12128 595 waASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARtalknarLDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510
....*....|....*....|....*....|....*.
gi 1743142585 1360 KTIRLS-KELSSTEAQL----HDAQELLQEETRAKL 1390
Cdd:pfam12128 675 ERKDSAnERLNSLEAQLkqldKKHQAWLEEQKEQKR 710
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1596-1735 |
3.32e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1596 EQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALK-----TQHERD-LQGRDEAGEERRRQLAKQLRDAEVERDEERKQ 1669
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRaslsaAEAERSrLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 1670 RALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWR--------EVEETRSSREEIFSQNRE 1735
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRrlnvalaqRVQELNRYRSEFFGRLRE 205
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1049-1974 |
3.87e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.05 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1049 EDQNSKLSKERKLLEDRLAEfSSQAAEEEEKVKSLNKLRLKYEATITdmEDRLRKEekGRQELEKLKRRLDGESSELQEQ 1128
Cdd:NF041483 360 EDTAAQLAKAARTAEEVLTK-ASEDAKATTRAAAEEAERIRREAEAE--ADRLRGE--AADQAEQLKGAAKDDTKEYRAK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1129 MVEQQQRAEELRSQLG--RKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDL-EAERVARTKAEKQRRDLGEE 1205
Cdd:NF041483 435 TVELQEEARRLRGEAEqlRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAKADAdELRSTATAESERVRTEAIER 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1206 LEALRGELEDTLDSTnaqqelRSKREQEVTELKKTLEEETRIHEAAVQELRqrhgqalgELAEQLEQARRGKGAWEKTRL 1285
Cdd:NF041483 515 ATTLRRQAEETLERT------RAEAERLRAEAEEQAEEVRAAAERAARELR--------EETERAIAARQAEAAEELTRL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1286 ALEAEvselrAELSSLQTARQEGEQRRRRLESQLQEvqgragDGERARAEAAEKLQ--RAQAELE----------NVSGA 1353
Cdd:NF041483 581 HTEAE-----ERLTAAEEALADARAEAERIRREAAE------ETERLRTEAAERIRtlQAQAEQEaerlrteaaaDASAA 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1354 LNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAeAAGLREQLEEEAAARERAGRELQTAQAQLSE 1433
Cdd:NF041483 650 RAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEA-AEALAAAQEEAARRRREAEETLGSARAEADQ 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1434 WRRRQEEEAGALEAGEEarrraareaealtQRLAE-KTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKqrkfd 1512
Cdd:NF041483 729 ERERAREQSEELLASAR-------------KRVEEaQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQ----- 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1513 qllAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLS-SKDDVGKSVHELERA 1591
Cdd:NF041483 791 ---AEEEIAGLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKAlAERTVSEAIAEAERL 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1592 CRVAEQAANDLRaqvTELEDELTAAED--AKLRLEVTVQALKTQHERDLQGR---DEAGEERRRQLAKQLRDAEVERDEE 1666
Cdd:NF041483 868 RSDASEYAQRVR---TEASDTLASAEQdaARTRADAREDANRIRSDAAAQADrliGEATSEAERLTAEARAEAERLRDEA 944
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1667 RKQ----RALAVAARKKL----EGELEELKAQMASAGQGKEEAVKQLRKmqaqmkELWREVEETRSSREEIFSQNRESEK 1738
Cdd:NF041483 945 RAEaervRADAAAQAEQLiaeaTGEAERLRAEAAETVGSAQQHAERIRT------EAERVKAEAAAEAERLRTEAREEAD 1018
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1739 RLkgleaevlrLQEELAASDRARRQAQQDRDEMADEVANGN---LSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLND 1815
Cdd:NF041483 1019 RT---------LDEARKDANKRRSEAAEQADTLITEAAAEAdqlTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAE 1089
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1816 RYRKLLLQVESLTTE-----LSAERSFSA---KAESGRQQLERQIQELRGRLGEEDA----GARARHKMTIAALESKLAQ 1883
Cdd:NF041483 1090 ATVEGNSLVEKARTDadellVGARRDATAireRAEELRDRITGEIEELHERARRESAeqmkSAGERCDALVKAAEEQLAE 1169
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1884 AEEQLEQETRE--------RILSgklVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLR-VKQLKRQLEEAEEEASRA 1954
Cdd:NF041483 1170 AEAKAKELVSDanseaskvRIAA---VKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRtVEEGKRELDVLVRRREDI 1246
|
970 980
....*....|....*....|
gi 1743142585 1955 QAGRRRLQreleDVTESAES 1974
Cdd:NF041483 1247 NAEISRVQ----DVLEALES 1262
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1563-1754 |
4.50e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1563 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKtQHERDLQGRD 1642
Cdd:COG1340 51 QVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIE-RLEWRQQTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1643 EAGEERRR------QLAKQLRDAEVERDEERKQralavaarKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELW 1716
Cdd:COG1340 130 LSPEEEKElvekikELEKELEKAKKALEKNEKL--------KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELY 201
|
170 180 190
....*....|....*....|....*....|....*...
gi 1743142585 1717 REVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEEL 1754
Cdd:COG1340 202 KEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1366-1988 |
4.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1366 KELSSTEAQLHDAQEllQEETRAKL-ALGSRVRAMEAEAAGLREQLEEEAAARERAGRELqtAQAQLSEWRRRQEEEAGA 1444
Cdd:COG4913 235 DDLERAHEALEDARE--QIELLEPIrELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1445 LEAGEEARRRAAREAEALTQRLAE-KTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEkkqrkfdqLLAEEKAAVL 1523
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALG--------LPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1524 RAVEERERAEAEGREREARALSLTRALEEEQEAREELerQNRALRAELEALLSSKDDVGKSVHEL-ERACRVAEQAANDL 1602
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRR--ELRELEAEIASLERRKSNIPARLLALrDALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1603 RA-----QVTELEDE--------------------------LTAAEDAKLRLEVTVQALKTQHERDLQGRDEAG------ 1645
Cdd:COG4913 461 PFvgeliEVRPEEERwrgaiervlggfaltllvppehyaaaLRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkl 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1646 --------EERRRQLAKQLRDAEVERDEE--RKQRALAVA-------------ARKKLEGE----------LEELKAQMA 1692
Cdd:COG4913 541 dfkphpfrAWLEAELGRRFDYVCVDSPEElrRHPRAITRAgqvkgngtrhekdDRRRIRSRyvlgfdnrakLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1693 SAGQGKEEAVKQLRKMQAQMKELwreveETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRArrqaQQDRDEMA 1772
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDAL-----QERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS----SDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1773 DEVAngnlskaAILEEKRQLEGRLGQleeeleeeqsnselLNDRYRKLLLQVESLTTEL-SAERSFSAKAESGRQQLERQ 1851
Cdd:COG4913 692 EQLE-------ELEAELEELEEELDE--------------LKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRAL 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1852 IQELRGRLGEEDAGARARHKMT--IAALESKLAQAEEQLEQETRErilsgkLVRRAEKRLKEVVLQVEEERRVADQLrDQ 1929
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEerIDALRARLNRAEEELERAMRA------FNREWPAETADLDADLESLPEYLALL-DR 823
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1743142585 1930 LEKGNLRVKqlkrqleeaeeeasRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG4913 824 LEEDGLPEY--------------EERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1088-1209 |
5.35e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1088 LKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLgrkEEELQAALARAEDEGgarAQL 1167
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKEAKKEA---DEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1743142585 1168 LKSLReaqaalaeAQEDLEAERVARTKAEKQRRDLGEELEAL 1209
Cdd:PRK00409 590 IKELR--------QLQKGGYASVKAHELIEARKRLNKANEKK 623
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1096-1278 |
5.76e-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: 46.84 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1096 DMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDeggARAQL--LKSLRE 1173
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLgnVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1174 AQAALAeaqeDLEAERVARTKAEKQRRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKTLEEETRIHEAAVQ 1253
Cdd:COG1579 91 YEALQK----EIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|....*....
gi 1743142585 1254 ELRQRHGQALGELAEQL----EQARRGKG 1278
Cdd:COG1579 160 ELEAEREELAAKIPPELlalyERIRKRKN 188
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1261-1491 |
6.24e-05 |
|
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: 47.45 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1261 QALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKL 1340
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1341 QRAQAELENVSGALNEAESktirlskelSSTEAQLHDAQELLQEETRAKLaLGSRVRAMEAEAAGLREQLEEEAAARERA 1420
Cdd:COG4942 100 EAQKEELAELLRALYRLGR---------QPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743142585 1421 GRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDAS 1491
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1462-1695 |
8.83e-05 |
|
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: 47.07 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1462 LTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEekaavlraveereraeaegREREA 1541
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------------------LEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1542 RALSLTRALEEEQEAREELERQNRALRAELEALLSSKD--DVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDA 1619
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1620 KLRLEVTVQALKTQHERdLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAG 1695
Cdd:COG4942 173 RAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
903-1128 |
1.04e-04 |
|
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: 47.32 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 903 LQVTRQDEVLQARAQELQKVQELQQQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAAR-------- 974
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQlkvlsrsi 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 975 ---KQELELVVSELEARVGEEEECSRQmqteKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ 1051
Cdd:TIGR04523 478 nkiKQNLEQKQKELKSKEKELKKLNEE----KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1052 N----------------SKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLK 1115
Cdd:TIGR04523 554 LkkenlekeideknkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
250
....*....|...
gi 1743142585 1116 RRLDGESSELQEQ 1128
Cdd:TIGR04523 634 KNIKSKKNKLKQE 646
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1649-1794 |
1.16e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.79 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1649 RRQLAKQLRDAEVERDEERKQRALAVAARKKlEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKelwREVEETRSSREE 1728
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANR-EAEEAELEQEREIETARIAEAEAELAKKKAEER---REAETARAEAEA 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1729 IFSQNRESEKRLKGLEAEVLRLQE--ELAASDRARRQAQQDRDEMADEVANgnlSKAAILEEKRQLEG 1794
Cdd:COG2268 267 AYEIAEANAEREVQRQLEIAEREReiELQEKEAEREEAELEADVRKPAEAE---KQAAEAEAEAEAEA 331
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1731-1966 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1731 SQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEvangnlskaailEEKRQLEGRLGQLEEELEEEQSNS 1810
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1811 ELLNDRYRKLLLQVESLTTELSAersfsAKAESGRQQLERQIQELRGRLGEEDAGARARHKmTIAALESKLAQAEEQLEQ 1890
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPE-----LLQSPVIQQLRAQLAELEAELAELSARYTPNHP-DVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1891 ETRerilsgklvrraeKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLkrqleeaeeeaSRAQAGRRRLQRELE 1966
Cdd:COG3206 310 EAQ-------------RILASLEAELEALQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVE 361
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1072-1279 |
2.01e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 46.85 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1072 QAAEEEEKVKSLNKLRLKY---EATITDMEDRLRKE-EKGRQELEKLKRRLDGE---SSELQE----------QMVEQQQ 1134
Cdd:PLN03188 1038 PESTDESPEKKLEQERLRWteaESKWISLAEELRTElDASRALAEKQKHELDTEkrcAEELKEamqmameghaRMLEQYA 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1135 RAEELRSQLGRKEEELQ-------AALARAEDEGgARAQLLKSLreaqaalaeaQEDLEAERVARtkaEKQRRDLGEELE 1207
Cdd:PLN03188 1118 DLEEKHIQLLARHRRIQegiddvkKAAARAGVRG-AESKFINAL----------AAEISALKVER---EKERRYLRDENK 1183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1208 ALRGELEDTLDSTNAQQEL--RSKREQE--VTELKKTLEEETRIHEA--AVQELRQRHGQALGELAEQLEQARRGKGA 1279
Cdd:PLN03188 1184 SLQAQLRDTAEAVQAAGELlvRLKEAEEalTVAQKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPKEA 1261
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1025-1374 |
2.12e-04 |
|
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: 46.55 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1025 QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKE 1104
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1105 EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLgrkeEELQAALARAEDEGGARAQLLKSLREAqaalaeaqed 1184
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI----IKNNSEIKDLTNQDSVKELIIKNLDNT---------- 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1185 leaervaRTKAEKQRRDLGEELEALRGELEDTldstnaQQELRSKreqeVTELKKtLEEETRIHEAAVQELRQRHGQaLG 1264
Cdd:TIGR04523 463 -------RESLETQLKVLSRSINKIKQNLEQK------QKELKSK----EKELKK-LNEEKKELEEKVKDLTKKISS-LK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1265 ELAEQLEQarrgkgawEKTRlaLEAEVSELRAELSSLQTARQEGEQRRRRLESQ--LQEVQGRAGDGERARAEAAEKLQR 1342
Cdd:TIGR04523 524 EKIEKLES--------EKKE--KESKISDLEDELNKDDFELKKENLEKEIDEKNkeIEELKQTQKSLKKKQEEKQELIDQ 593
|
330 340 350
....*....|....*....|....*....|..
gi 1743142585 1343 AQAELENVSGALNEAESKTIRLSKELSSTEAQ 1374
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
715-739 |
2.36e-04 |
|
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: 43.87 E-value: 2.36e-04
10 20
....*....|....*....|....*
gi 1743142585 715 YKESLSRLMATLSNTNPSFVRCIVP 739
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1651-1939 |
2.40e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1651 QLAKQLRDAEVERDEERKQRAlAVAARKKLEGELEELKAQMASAgqgkEEAVKQLRKmqaqmkelwreveetrssREEIF 1730
Cdd:COG3206 152 AVANALAEAYLEQNLELRREE-ARKALEFLEEQLPELRKELEEA----EAALEEFRQ------------------KNGLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1731 SqnreSEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEekrqlegrlgqleeeleeeqsns 1810
Cdd:COG3206 209 D----LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1811 ellNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQ 1890
Cdd:COG3206 262 ---SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1743142585 1891 eTRERILSgklVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQ 1939
Cdd:COG3206 339 -LEARLAE---LPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
777-1258 |
2.41e-04 |
|
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: 46.50 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 777 ILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVSFQAAAR 856
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 857 GYLARRAFQKRQQQQSalrvmqRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVREL 936
Cdd:pfam02463 605 LAQLDKATLEADEDDK------RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEI 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 937 QGRVAQLEEERARLAEQLRAEAELcaeaeetrgrLAARKQELELVVSELEARVGEEEECSRQMqtekKRLQQHIQELEAH 1016
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIK----------KKEQREKEELKKLKLEAEELLADRVQEAQ----DKINEELKLLKQK 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1017 LEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQnsKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKL---RLKYEAT 1093
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE--REKTEKLKVEEEKEEKLKAQEEELRALEEELKEeaeLLEEEQL 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1094 ITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEG----GARAQLLK 1169
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESkeekEKEEKKEL 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1170 SLREAQAALAEAQEDLEAERVARTKAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIH 1248
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEERIKEEAEILLKyEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEE 982
|
490
....*....|
gi 1743142585 1249 EAAVQELRQR 1258
Cdd:pfam02463 983 FEEKEERYNK 992
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1338-1886 |
2.66e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1338 EKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRvramEAEAAGLREQLEEEAAAR 1417
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL----EGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1418 ERAGRELQtaqaQLSEWRRRQEEeagaLEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQ 1497
Cdd:PRK03918 269 EELKKEIE----ELEEKVKELKE----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1498 RQLVSTLEKKQRKFDQLlaeEKAAVLRAVEERERAEAEGREREARALSLTRaleeeqeareelerqnraLRAELEALLSS 1577
Cdd:PRK03918 341 EELKKKLKELEKRLEEL---EERHELYEEAKAKKEELERLKKRLTGLTPEK------------------LEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1578 KDDVGKSVHELERACRVAEQAANDLRAQVTELEDeltaaedAKLRLEVTVQALKTQHERDLQGRDEAG-----------E 1646
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKK-------AKGKCPVCGRELTEEHRKELLEEYTAElkriekelkeiE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1647 ERRRQLAKQLRDAEVERDEERKQRALAVAAR--KKLEGELEELKAQMASAGQGKEEAVKQ-LRKMQAQMKELWREVE--- 1720
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEEYEKLKEkLIKLKGEIKSLKKELEkle 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1721 ETRSSREEIFSQNRESEKRLKGLEAEVL------------RLQE---------ELAASDRARRQAQQDRDEMADEVANGN 1779
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEelgfesveeleeRLKElepfyneylELKDAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1780 LSKAAILEEKRQLEGRLGQLEEELEEeqsnsellnDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRL 1859
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSE---------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
570 580
....*....|....*....|....*..
gi 1743142585 1860 GEedagaRARHKMTIAALESKLAQAEE 1886
Cdd:PRK03918 704 EE-----REKAKKELEKLEKALERVEE 725
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1075-1348 |
2.75e-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: 45.88 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1075 EEEEKVKSLNKLRLKYEAtitdmEDRLRKEEKGRQELEKLKRRldgeSSELQEQMV---EQQQRAEELRSQLGR-KEEEL 1150
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEK-----EEKAREVERRRKLEEAEKAR----QAEMDRQAAiyaEQERMAMERERELERiRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1151 QAALARAEDEGGA----RAQLLKSLREAQAALAEA-QEDLEAERVARTKAEKQRRDLGE---ELEALRGELEDTldstnA 1222
Cdd:pfam17380 359 KRELERIRQEEIAmeisRMRELERLQMERQQKNERvRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-----R 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1223 QQELRSKREQEVTELKKTLEEETRiHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRaelsslq 1302
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQE-RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK------- 505
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1743142585 1303 TARQEGEQRRRRLESQLQEVQGRAGDGERARaeAAEKLQRAQAELE 1348
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEME 549
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
980-1433 |
2.76e-04 |
|
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: 46.25 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 980 LVVSELEARVGEEEECSRqmqTEKKRLQQHIQELEAHLEAEEgaRQKLQLEKVTTEAKMKKFE-EDLLLLEDQNSKLSKE 1058
Cdd:pfam05483 349 FVVTEFEATTCSLEELLR---TEQQRLEKNEDQLKIITMELQ--KKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1059 RKLLEDRLAEFSSQAAEE----EEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRR---LDGESSELQEQMVE 1131
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1132 QQQRAEELRSQLGRKEEELQAALARAEdeggaraQLLKSLREAQAALAEAQEDLEAERvartKAEKQRRDlgeELEALRG 1211
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRDELESVR----EEFIQKGD---EVKCKLD 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1212 ELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHgqalgelaeqleQARRGKGAWEKTRL-ALEAE 1290
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN------------KALKKKGSAENKQLnAYEIK 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1291 VSELRAELSSL-QTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAE--KLQ-----RAQAELENVSGALNEAESKTI 1362
Cdd:pfam05483 638 VNKLELELASAkQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavKLQkeidkRCQHKIAEMVALMEKHKHQYD 717
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1743142585 1363 RLSKELSStEAQLHDAQEllQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSE 1433
Cdd:pfam05483 718 KIIEERDS-ELGLYKNKE--QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1675-1939 |
2.77e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1675 AARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSsreeifsqNRESEKRLKGLEAEVLRLQEEL 1754
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLS--------LRQLESRLAQTLDQLQNAQNDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1755 A-----------ASDRARRQ---AQQDRDEMADEVANGNLSKAAILEEKRQLegrlgqleeeleeEQSNSELLN--DRYR 1818
Cdd:PRK11281 145 AeynsqlvslqtQPERAQAAlyaNSQRLQQIRNLLKGGKVGGKALRPSQRVL-------------LQAEQALLNaqNDLQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1819 KLLLQVESLTTELSAERSFSAKAESgrQQLERQIQELRGRLGEEDagararhkmtiaaLESKLAQAEEQLEQETRERILS 1898
Cdd:PRK11281 212 RKSLEGNTQLQDLLQKQRDYLTARI--QRLEHQLQLLQEAINSKR-------------LTLSEKTVQEAQSQDEAARIQA 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1743142585 1899 GKLVRRaekrlkevvlQVEEERRVADQLRDQLEKGN------LRVKQ 1939
Cdd:PRK11281 277 NPLVAQ----------ELEINLQLSQRLLKATEKLNtltqqnLRVKN 313
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1464-1988 |
2.90e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1464 QRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraVEERERAEAEGREREARA 1543
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-----LEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1544 LSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAE---QAANDLRAQVTELEDELTAAEDAK 1620
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1621 LRLEVTVQALKtqherdlqgRDEAGEERRRQLAKQLRDAEVERDEERKQraLAVAARKKLEGELEEL---KAQMASAGQG 1697
Cdd:PRK03918 355 EELEERHELYE---------EAKAKKEELERLKKRLTGLTPEKLEKELE--ELEKAKEEIEEEISKItarIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1698 KEEAVKQLRKMQAQMKELWREVEEtrSSREEIFsqnRESEKRLKGLEAEVLRLQEELaasDRARRQAQQDRDEMADEVAN 1777
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCGRELTE--EHRKELL---EEYTAELKRIEKELKEIEEKE---RKLRKELRELEKVLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1778 GNLSKaaILEEKRQLEGRLGQLEEELEEEQSNS-ELLNDRYRKLLLQVESLTTELSAERSFsakaESGRQQLERQIQELR 1856
Cdd:PRK03918 496 IKLKE--LAEQLKELEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKELEKLEEL----KKKLAELEKKLDELE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1857 GRLGEEDAGARARHKMTIAALESKLaqaeEQLEQETRERILsgklVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLR 1936
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERL----KELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1743142585 1937 VKQLKRQLEeaeeeasraQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:PRK03918 642 LEELRKELE---------ELEKKYSEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
914-1402 |
3.85e-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: 45.50 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 914 ARAQELQKVQELQQQSAREV---RELQGRVAQLEE----------ERARLAEQLRAEAELCAEAEETR------------ 968
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESdrnQELQKRIRLLEKreaeaeealrEQAELNRLKKKYLEALNKKLNEKesqladarevis 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 969 ---GRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHleaeegarQKLQLEKVTTEAKMKKFEEDL 1045
Cdd:pfam05557 108 clkNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNL--------EKQQSSLAEAEQRIKELEFEI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1046 LLLEDQNSKLSKERKLLEdRLAEFSSQAAEEEEKVKSLNKLR---LKYEATITDMEDRLRKEEKGRQELEKLKRRLDGES 1122
Cdd:pfam05557 180 QSQEQDSEIVKNSKSELA-RIPELEKELERLREHNKHLNENIenkLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1123 SELQEQMVEQQQRAEELRS--QLGRKEEELQAALARAEDEGGARAQLLKSLReaqaalaEAQEDLEAE-RVARTKAEKQR 1199
Cdd:pfam05557 259 QELQSWVKLAQDTGLNLRSpeDLSRRIEQLQQREIVLKEENSSLTSSARQLE-------KARRELEQElAQYLKKIEDLN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1200 RDLgEELEALRGELEDTLDSTNAQ----QELRSKREQEVTELKKTLEEETRIHEAAvqELRQRHGQALGELAEQLEQARR 1275
Cdd:pfam05557 332 KKL-KRHKALVRRLQRRVLLLTKErdgyRAILESYDKELTMSNYSPQLLERIEEAE--DMTQKMQAHNEEMEAQLSVAEE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1276 GKGAWEKTRLALEAEVSELRAelsslQTARQEGEQRRRRLESQLQEVQGRagDGERARAEAAEKLQRAQAELENVSGALN 1355
Cdd:pfam05557 409 ELGGYKQQAQTLERELQALRQ-----QESLADPSYSKEEVDSLRRKLETL--ELERQRLREQKNELEMELERRCLQGDYD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1743142585 1356 EAESKTIRLSKE-LSSTEAQLHDAQELLQEETRaklALGSRVRAMEAE 1402
Cdd:pfam05557 482 PKKTKVLHLSMNpAAEAYQQRKNQLEKLQAEIE---RLKRLLKKLEDD 526
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
935-1389 |
4.75e-04 |
|
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: 45.48 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 935 ELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSE----------LEARVGEEEECSRQMQTEKK 1004
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1005 RLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMK-KFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSL 1083
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1084 NKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMveqqQRAEELRSQLgrkEEELQAALARAEDEGGA 1163
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSL----QRSMSTQKAL---EEDLQIATKTICQLTEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1164 RAQLLKSLREAQAALAEAQEDLEA-----ERVARTkaEKQRRDLGE-ELEALRGELEDTLDSTNAQQELRSKREQEVTEL 1237
Cdd:pfam05483 333 KEAQMEELNKAKAAHSFVVTEFEAttcslEELLRT--EQQRLEKNEdQLKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1238 KKTLEEEtrihEAAVQELRQrhgqaLGELAEQLEQARRGKGAWEKTRlalEAEVSELRAELSSLQTARQEGEQRRRRLES 1317
Cdd:pfam05483 411 KKILAED----EKLLDEKKQ-----FEKIAEELKGKEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1318 QLQEVQGR----AGDGERARAEAAEKLQRAQ---AELENVSGALNEAESKTIRLSKE---LSSTEAQLHDAQELLQEETR 1387
Cdd:pfam05483 479 ELEKEKLKnielTAHCDKLLLENKELTQEASdmtLELKKHQEDIINCKKQEERMLKQienLEEKEMNLRDELESVREEFI 558
|
..
gi 1743142585 1388 AK 1389
Cdd:pfam05483 559 QK 560
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1585-1864 |
4.75e-04 |
|
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: 45.33 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1585 VHELERACRVAEQAANDLRAQVTELEDELTAAED----AKLRLEVTVQALKTQHERDLQ--------------------- 1639
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEevdsLKSQLADYQQALDVQQTRAIQyqqavqalekaralcglpdlt 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1640 ------------GRDEAGEERRRQLAKQLRDAeverDEERKQRALAVAARKKLEGE-------------LEELKAQMASA 1694
Cdd:COG3096 436 penaedylaafrAKEQQATEEVLELEQKLSVA----DAARRQFEKAYELVCKIAGEversqawqtarelLRRYRSQQALA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1695 GQGK---------EEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQ 1765
Cdd:COG3096 512 QRLQqlraqlaelEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1766 QDRDEMADeVANGNLSKAAILEekrQLEGRLGQLEEELEEEqsnsellnDRYRKLLLQVEsltTELSAERSFSAKAesgR 1845
Cdd:COG3096 592 ARIKELAA-RAPAWLAAQDALE---RLREQSGEALADSQEV--------TAAMQQLLERE---REATVERDELAAR---K 653
|
330
....*....|....*....
gi 1743142585 1846 QQLERQIQELRGRLGEEDA 1864
Cdd:COG3096 654 QALESQIERLSQPGGAEDP 672
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
903-1253 |
5.70e-04 |
|
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: 45.11 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 903 LQVTRQDEVLQARAQELQKVQELQ-------QQSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARK 975
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 976 QELELV-------VSELEARVGEEEECSRQMQTEKKRLqQHIQELEAHLEAEEGARQKL------QLEKVTT-------E 1035
Cdd:pfam15921 506 QEKERAieatnaeITKLRSRVDLKLQELQHLKNEGDHL-RNVQTECEALKLQMAEKDKVieilrqQIENMTQlvgqhgrT 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1036 AKMKKFEEDLLLLEDQNSKLS-KERKLLED----RLAEFSSQAAE-EEEKVKSLN--KLRLKYEATITDMEDRLRKEEK- 1106
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLElQEFKILKDkkdaKIRELEARVSDlELEKVKLVNagSERLRAVKDIKQERDQLLNEVKt 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1107 GRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLE 1186
Cdd:pfam15921 665 SRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID 744
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743142585 1187 AERV-------ARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQ-ELRSKREQEVTELKKTLEEETRIHEAAVQ 1253
Cdd:pfam15921 745 ALQSkiqfleeAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAgELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1048-1160 |
5.96e-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: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1048 LEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRK-----------------------E 1104
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvrnnkeyealqkeiesL 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1105 EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDE 1160
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
932-1200 |
5.96e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 932 EVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQ 1011
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1012 ELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERkllEDRLAEFSSQAAEEEEKVKSLNKLRLKye 1091
Cdd:COG1340 89 ELREELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKELEKAKKALEKNEK-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1092 atITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSL 1171
Cdd:COG1340 162 --LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260
....*....|....*....|....*....
gi 1743142585 1172 REAQAALAEAQEDLEAERVARTKAEKQRR 1200
Cdd:COG1340 240 RELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1627-1986 |
6.16e-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: 44.73 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1627 VQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERdeeRKQRALAVAARkklEGELEELKAQMASAGQGKEEAVKQLR 1706
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER---RRKLEEAEKAR---QAEMDRQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1707 KMQAQMKElwREVEETRssREEIFSQnresEKRLKGLEaevlRLQEElaasdrarRQAQQDRDEMADEVANgnlsKAAIL 1786
Cdd:pfam17380 352 RIRQEERK--RELERIR--QEEIAME----ISRMRELE----RLQME--------RQQKNERVRQELEAAR----KVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1787 EEKRQLEGRLGQLEEELEEEQSNsellNDRYRKLLLQVESLTTELSAERsfsakaesgRQQLERQIQELRGRLGEEDaga 1866
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQE----EARQREVRRLEEERAREMERVR---------LEEQERQQQVERLRQQEEE--- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1867 RARHKMTIAALESKLAQAEEQleqetRERILSGKLVRRAEKRLkevvlqvEEERRvadqlRDQLEKgnlrvKQLKRQLEE 1946
Cdd:pfam17380 472 RKRKKLELEKEKRDRKRAEEQ-----RRKILEKELEERKQAMI-------EEERK-----RKLLEK-----EMEERQKAI 529
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1743142585 1947 AEEEASRAQAGRRRLQRELEDVTESAESMnREVTTLRNRL 1986
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
915-1128 |
6.36e-04 |
|
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: 45.11 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 915 RAQELQKVQELQQQSAREVRELQGRVAQLEEERARL----AEQLRAEAELCAEA-------EETRGRLAARKQELELVVS 983
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERdqllnevKTSRNELNSLSEDYEVLKR 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 984 ELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGA-------RQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLS 1056
Cdd:pfam15921 682 NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdghamkvAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAN 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743142585 1057 KERKLLEDRLA----EFSSQAAEEEEKVKSLNKLR---LKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQ 1128
Cdd:pfam15921 762 KEKHFLKEEKNklsqELSTVATEKNKMAGELEVLRsqeRRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1783-1988 |
6.43e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1783 AAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEe 1862
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1863 dagARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR 1942
Cdd:COG4942 95 ---LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1743142585 1943 QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1059-1241 |
6.52e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1059 RKLLEdrLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEE 1138
Cdd:COG1579 7 RALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1139 LRSQlgrkeEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRGELEDTLD 1218
Cdd:COG1579 85 VRNN-----KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|...
gi 1743142585 1219 stnaqqELRSKREQEVTELKKTL 1241
Cdd:COG1579 160 ------ELEAEREELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1054-1486 |
8.03e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1054 KLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDME--DRLRKEEKGRQELEKLKRRLDgessELQEQMVE 1131
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELA----ELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1132 QQQRAEELRsQLGRKEEELQAALARAEDEggARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRG 1211
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEE--LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1212 ELEDTLDSTNAQQELRSKREQE-----------VTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAW 1280
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1281 EKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAA-EKLQRAQAELENVSGALNEAE- 1358
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQlEELEQEIAALLAEAGVEDEEEl 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1359 SKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRV--RAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWrr 1436
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREELAELEAELEQL-- 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1437 rqeEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQE 1486
Cdd:COG4717 466 ---EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1566-1965 |
8.86e-04 |
|
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: 44.44 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1566 ALRAELEALLSSKDD-VGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKL--------RLEVTVQALKTQHER 1636
Cdd:pfam12128 283 ETSAELNQLLRTLDDqWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIetaaadqeQLPSWQSELENLEER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1637 -----DLQGRDEAGEERRRQLAKQLRDAEVERDEER---------KQRALAVAARKKLEGEL-EELKAQMASAGQGK--- 1698
Cdd:pfam12128 363 lkaltGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKlakireardRQLAVAEDDLQALESELrEQLEAGKLEFNEEEyrl 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1699 EEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRlkglEAEVLRLQEELAASDRARRQAQqdrDEMADEVANG 1778
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAA----NAEVERLQSELRQARKRRDQAS---EALRQASRRL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1779 NLSKAAILEEKRQLEGRLGQLEEELEEEQSnseLLNDRYRKLLLQVESLTTELSAERSFSAKAESGR------------- 1845
Cdd:pfam12128 516 EERQSALDELELQLFPQAGTLLHFLRKEAP---DWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNlygvkldlkridv 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1846 ---QQLERQIQELRGRLGEEDAGARARHkmtiAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVE-EERR 1921
Cdd:pfam12128 593 pewAASEEELRERLDKAEEALQSAREKQ----AAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQsEKDK 668
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1743142585 1922 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQREL 1965
Cdd:pfam12128 669 KNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA 712
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1231-1406 |
8.93e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1231 EQEVTELKKTLEEetriHEAAVQELRQRHGqaLGELAEQLEQarrgkgawektrlaLEAEVSELRAELSSLQTARQEGEQ 1310
Cdd:COG3206 181 EEQLPELRKELEE----AEAALEEFRQKNG--LVDLSEEAKL--------------LLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1311 RRRRLESQLQEVQGRAGD--GERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA 1388
Cdd:COG3206 241 RLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170
....*....|....*....
gi 1743142585 1389 KL-ALGSRVRAMEAEAAGL 1406
Cdd:COG3206 321 ELeALQAREASLQAQLAQL 339
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
906-1164 |
9.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 906 TRQDEVLQARAQELQ----KVQELQQQSAREVRELQGR----------------VAQLEEERARLAEQLRAEAELCAEAE 965
Cdd:COG4913 609 RAKLAALEAELAELEeelaEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 966 ETRGRLAARKQELELVVSELEARVGEEEECSRQmQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDL 1045
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKE-LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1046 LL-LEDQNSKLSKERKLLEDRLaefssqaaeeeekVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRrldgesse 1124
Cdd:COG4913 768 REnLEERIDALRARLNRAEEEL-------------ERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE-------- 826
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1743142585 1125 lqEQMVEQQQRAEELR-SQLGRKEEELQAALARAEDEGGAR 1164
Cdd:COG4913 827 --DGLPEYEERFKELLnENSIEFVADLLSKLRRAIREIKER 865
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1126-1522 |
9.33e-04 |
|
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: 44.56 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1126 QEQMVEQQQRAEELRSQL---GRKEEELQAALARAEDEggaRAQLLKSLREaqaalaeaqedleAERVARTKAEKQrrDL 1202
Cdd:COG3096 298 RRQLAEEQYRLVEMARELeelSARESDLEQDYQAASDH---LNLVQTALRQ-------------QEKIERYQEDLE--EL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1203 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRiheaAVQELRQRHGQ------ALGELAEQLEQARRG 1276
Cdd:COG3096 360 TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ----ALDVQQTRAIQyqqavqALEKARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1277 KGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARA-EAAEKLQRAQAELENVSGaln 1355
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAwQTARELLRRYRSQQALAQ--- 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1356 eaesktirlskELSSTEAQLHDAQELLQEETRAklalgsrvramEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWR 1435
Cdd:COG3096 513 -----------RLQQLRAQLAELEQRLRQQQNA-----------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1436 RRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDaSVDLEQQRQLVSTLEKKQRKFDQLL 1515
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALAD-SQEVTAAMQQLLEREREATVERDEL 649
|
....*..
gi 1743142585 1516 AEEKAAV 1522
Cdd:COG3096 650 AARKQAL 656
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1242-1776 |
9.36e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.46 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1242 EEETRIHEAAVQELRQRHGQA----LGELAEQLEQARRGKGAWE---------KTRLALEAEVSELRAELSSLqtARQEG 1308
Cdd:COG3899 663 EERRALHRRIARALEARGPEPleerLFELAHHLNRAGERDRAARlllraarraLARGAYAEALRYLERALELL--PPDPE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1309 EQRRRRLESQLQEVQGRAGDGERARaEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA 1388
Cdd:COG3899 741 EEYRLALLLELAEALYLAGRFEEAE-ALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALAL 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1389 KLALGSRVR------------------------AMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEE-EAG 1443
Cdd:COG3899 820 AERLGDRRLearalfnlgfilhwlgplrealelLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARlLAA 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1444 ALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVL 1523
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAA 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1524 RAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLR 1603
Cdd:COG3899 980 AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAA 1059
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1604 AQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGE 1683
Cdd:COG3899 1060 AALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLA 1139
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1684 LEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQ 1763
Cdd:COG3899 1140 AALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEA 1219
|
570
....*....|...
gi 1743142585 1764 AQQDRDEMADEVA 1776
Cdd:COG3899 1220 AALLLLLLLAALA 1232
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1186-1383 |
9.58e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1186 EAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQelrsKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGE 1265
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1266 LAEQLeqarrgkgawEKTRLA-LEAEVSELRAELSSLQTArqegeqrRRRLESQLQEVQGRAgdgERARAEAAEKLQRAQ 1344
Cdd:PRK11281 114 TRETL----------STLSLRqLESRLAQTLDQLQNAQND-------LAEYNSQLVSLQTQP---ERAQAALYANSQRLQ 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1743142585 1345 aELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQ 1383
Cdd:PRK11281 174 -QIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQ 211
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1060-1382 |
9.72e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1060 KLLEDRLAEFSsqaaeeeEKVKSLNKLRLKYEATITDmedrlrKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEEL 1139
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFLEQQNKLLETKISE------LRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1140 RSQLGRKEEELQAALARAEDEGGARaqllkslREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRGEledtlds 1219
Cdd:pfam00038 74 QLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1220 tnaqqelrskREQEVTELKKTLEEETRIHE---AAVQELrqrhGQALGELAEQLE-QARRGKG---AWEKTRLA-LEAEV 1291
Cdd:pfam00038 140 ----------HEEEVRELQAQVSDTQVNVEmdaARKLDL----TSALAEIRAQYEeIAAKNREeaeEWYQSKLEeLQQAA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1292 SELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEklqRAQAELENVSGALNEAESKTIRLSKELsst 1371
Cdd:pfam00038 206 ARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEE---RYELQLADYQELISELEAELQETRQEM--- 279
|
330
....*....|.
gi 1743142585 1372 EAQLHDAQELL 1382
Cdd:pfam00038 280 ARQLREYQELL 290
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1043-1879 |
9.89e-04 |
|
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: 44.56 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1043 EDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLnklrlkyEATITDMEDRLRKEEKGRQELEKLKRRLDgES 1122
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDL-------EQDYQAASDHLNLVQTALRQQEKIERYQE-DL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1123 SELQEQMVEQQQRAEELRSQLgrkeEELQAALARAEDE-GGARAQLlkslreaqaalaeaqEDLE-AERVARTKAEKQRR 1200
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQL----AEAEARLEAAEEEvDSLKSQL---------------ADYQqALDVQQTRAIQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1201 DLG--EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHgQALGELAEQLEQARrgkg 1278
Cdd:COG3096 418 AVQalEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEVERSQ---- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1279 AWEKTRLALE---------AEVSELRAELSSLQtarqEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELEN 1349
Cdd:COG3096 493 AWQTARELLRryrsqqalaQRLQQLRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1350 VSGALNEAESKTIRLSKELSSTEAQ-------------LHDAQELLQEETRAKLALGSRVRAMEAEAAglreqleeeaaa 1416
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALERLREQSGEALADSQEVTAAMQQLL------------ 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1417 reRAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAreaealtQRLAEKTEA------------------------ 1472
Cdd:COG3096 637 --EREREATVERDELAARKQALESQIERLSQPGGAEDPRL-------LALAERLGGvllseiyddvtledapyfsalygp 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1473 ------VDRLERGRRRLQQeLDDASVDLeqqrqlvSTLEKKQRKFDQLL---AEEKAAVLRAVEEREraeaegrereara 1543
Cdd:COG3096 708 arhaivVPDLSAVKEQLAG-LEDCPEDL-------YLIEGDPDSFDDSVfdaEELEDAVVVKLSDRQ------------- 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1544 LSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERA-----------CRVA-----EQAANDLRAQVT 1607
Cdd:COG3096 767 WRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLhqafsqfvgghLAVAfapdpEAELAALRQRRS 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1608 ELEDELTAAEDAKLRLEVTVQALKTQHE--RDLQGR-----DEAGEERRRQLAKQLRDA-EVERDEERKQRALAvaarkK 1679
Cdd:COG3096 847 ELERELAQHRAQEQQLRQQLDQLKEQLQllNKLLPQanllaDETLADRLEELREELDAAqEAQAFIQQHGKALA-----Q 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1680 LEGELEELK---AQMASAGQGKEEAVKQLRKMQAQMKELwREVEETR-----SSREEIFSQNRESEKRLKgleAEVLRLQ 1751
Cdd:COG3096 922 LEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFAL-SEVVQRRphfsyEDAVGLLGENSDLNEKLR---ARLEQAE 997
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1752 EELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSEllndRYRKlllqvESLTTEL 1831
Cdd:COG3096 998 EARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERA----RIRR-----DELHEEL 1068
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1743142585 1832 SAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALES 1879
Cdd:COG3096 1069 SQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1059-1299 |
1.04e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1059 RKLLeDRLAEFSSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEE---KGRQELEKLKRRlDGESSELQEQmVEQQQR 1135
Cdd:COG0497 144 RELL-DAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDllrFQLEELEAAALQ-PGEEEELEEE-RRRLSN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1136 AEELRSQLGrkeeelQAALARAEDEGGArAQLLKSLREAQAALAEAQEDLE--AERVARTKAEKQrrDLGEELEALRGEL 1213
Cdd:COG0497 221 AEKLREALQ------EALEALSGGEGGA-LDLLGQALRALERLAEYDPSLAelAERLESALIELE--EAASELRRYLDSL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1214 E---DTLDSTNA-QQELRS-KR-----EQEVTELKKTLEEE--------TRIH--EAAVQELRQrhgqALGELAEQLEQA 1273
Cdd:COG0497 292 EfdpERLEEVEErLALLRRlARkygvtVEELLAYAEELRAElaelensdERLEelEAELAEAEA----ELLEAAEKLSAA 367
|
250 260
....*....|....*....|....*.
gi 1743142585 1274 RRgkgaweKTRLALEAEVSELRAELS 1299
Cdd:COG0497 368 RK------KAAKKLEKAVTAELADLG 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
860-1388 |
1.19e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 860 ARRAFQKRQQQQSALRVMQRNCAAYLKLR-----------HWQWWRLFTKV----KPLLQVTRQDEVLQARAQELQKVQE 924
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLWFAQRRLelleAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 925 LQQQSAREVR------------ELQGRVAQLEEERARLAEQLRAEAElcaeaeetrgRLAARKQELELVVSELEARVGEE 992
Cdd:COG4913 320 ALREELDELEaqirgnggdrleQLEREIERLERELEERERRRARLEA----------LLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 993 EECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQnskLSKERKLLEDRL---AEF 1069
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA---LAEALGLDEAELpfvGEL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1070 SSQAAEEE------EKVksLNKLRL------KYEATITDMEDRLrkeekgrqeleKLKRRLDGEssELQEQMVEQQQRAE 1137
Cdd:COG4913 467 IEVRPEEErwrgaiERV--LGGFALtllvppEHYAAALRWVNRL-----------HLRGRLVYE--RVRTGLPDPERPRL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1138 ELRSQLGRKEEELQAALARAEDEGGARAQLLKslreaqaalAEAQEDLEAERVARTKA----------EKQRRD------ 1201
Cdd:COG4913 532 DPDSLAGKLDFKPHPFRAWLEAELGRRFDYVC---------VDSPEELRRHPRAITRAgqvkgngtrhEKDDRRrirsry 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1202 -LG----EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELR-QRHGQALGELAEQLEQARR 1275
Cdd:COG4913 603 vLGfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1276 GKGAWEktrlALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAgDGERARAEAAEKLQRAQ--AELENVSGA 1353
Cdd:COG4913 683 SSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-DELQDRLEAAEDLARLElrALLEERFAA 757
|
570 580 590
....*....|....*....|....*....|....*...
gi 1743142585 1354 LNEAES-KTIR--LSKELSSTEAQLHDAQELLQEETRA 1388
Cdd:COG4913 758 ALGDAVeRELRenLEERIDALRARLNRAEEELERAMRA 795
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1110-1985 |
1.61e-03 |
|
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: 43.88 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1110 ELEKLKRRLDGESSelQEQMVEQQQRAEELRSQLGRKEEELQAALaraedeggaraQLLKSLREAQAALAEAQEDLEAER 1189
Cdd:TIGR00606 167 EGKALKQKFDEIFS--ATRYIKALETLRQVRQTQGQKVQEHQMEL-----------KYLKQYKEKACEIRDQITSKEAQL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1190 VARTKAEKQRRDLGEELEALRGELEDTL-------DSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQA 1262
Cdd:TIGR00606 234 ESSREIVKSYENELDPLKNRLKEIEHNLskimkldNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRT 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1263 LGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRA---------------- 1326
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgfergpfserqik 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1327 --------GDGERAR------AEAAEKLQRAQAELENV----SGALNEAESKTIRLSKELSSTEaqlHDAQELLQEETRA 1388
Cdd:TIGR00606 394 nfhtlvieRQEDEAKtaaqlcADLQSKERLKQEQADEIrdekKGLGRTIELKKEILEKKQEELK---FVIKELQQLEGSS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1389 KLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEaltqrlaE 1468
Cdd:TIGR00606 471 DRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK-------D 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1469 KTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLlaEEKAAVLRAVEEreraeaegrerearalSLTR 1548
Cdd:TIGR00606 544 KMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQT--RDRLAKLNKELA----------------SLEQ 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1549 ALEEEQEAREELERQNRALRAELEALLSSKD---DVGKSVHELERAC--RVAEQAANDLRAQ-VTELEDELTAAEDAKLR 1622
Cdd:TIGR00606 606 NKNHINNELESKEEQLSSYEDKLFDVCGSQDeesDLERLKEEIEKSSkqRAMLAGATAVYSQfITQLTDENQSCCPVCQR 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1623 LEVTVQALKtQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKaqmasagqgkeeav 1702
Cdd:TIGR00606 686 VFQTEAELQ-EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-------------- 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1703 KQLRKMQAQMKELWREVEETRSSREEIFSQnRESEKRLKGLEAEVLRLQEELaaSDRARRQAQQDRDEmadEVANGNLSK 1782
Cdd:TIGR00606 751 NKLQKVNRDIQRLKNDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMEL--KDVERKIAQQAAKL---QGSDLDRTV 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1783 AAILEEKRQLEGRLgqlEEELEEEQSNSELLNDRyRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGE- 1861
Cdd:TIGR00606 825 QQVNQEKQEKQHEL---DTVVSKIELNRKLIQDQ-QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSl 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1862 --EDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEE-ERRVADQLRDQLEKGNLRVK 1938
Cdd:TIGR00606 901 irEIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELN 980
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1743142585 1939 QLKRQLEEAEEEASRAQAGRRRLQRELeDVTESAESMNREVTTLRNR 1985
Cdd:TIGR00606 981 TVNAQLEECEKHQEKINEDMRLMRQDI-DTQKIQERWLQDNLTLRKR 1026
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1194-1430 |
1.68e-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: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1194 KAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEtrihEAAVQELRQRHGQALGELAEQLEQA 1273
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1274 RRGKGAWEKTRLALEAE-VSELRAELSSLQTARQEGEQRRRRLESQLQEVqgragdgERARAEAAEKLQRAQAELENVSG 1352
Cdd:COG3883 96 YRSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAEL-------EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1353 ALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQ 1430
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1036-1398 |
1.88e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1036 AKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSS--QAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEK 1113
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1114 LKRRLDGESSELQEqmvEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVART 1193
Cdd:COG4717 161 LEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1194 KAEKQRR-----------DLGEELEALRGELEDTLDS------------TNAQQELRSKREQEVTELKKT--LEEETRIH 1248
Cdd:COG4717 238 AAALEERlkearlllliaAALLALLGLGGSLLSLILTiagvlflvlgllALLFLLLAREKASLGKEAEELqaLPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1249 EAAVQELRQRHG-------QALGELAEQLEQARRGKGAWEKtrLALEAEVSELRAELSSLQT-----------ARQEGEQ 1310
Cdd:COG4717 318 EEELEELLAALGlppdlspEELLELLDRIEELQELLREAEE--LEEELQLEELEQEIAALLAeagvedeeelrAALEQAE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1311 RRRRLESQLQEVQGR--AGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDA------QELL 1382
Cdd:COG4717 396 EYQELKEELEELEEQleELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLeedgelAELL 475
|
410
....*....|....*.
gi 1743142585 1383 QEETRAKLALGSRVRA 1398
Cdd:COG4717 476 QELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1338-1796 |
2.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1338 EKLQRAQAELENVSGALNEAESKTIrlsKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEE--EAA 1415
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKEL---KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1416 ARERAGRELQTAQAQLSEWRRRQEEeagaLEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRR-RLQQELDDASVDL 1494
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEE----LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1495 EQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEAL 1574
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1575 LSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQAlktqherdlqgrDEAGEERRRqlAK 1654
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP------------EELLELLDR--IE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1655 QLRDAEVERDEERKQRalavaarkKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNR 1734
Cdd:COG4717 348 ELQELLREAEELEEEL--------QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 1735 ESEKRL--KGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANgnLSKAAILEEKRQLEGRL 1796
Cdd:COG4717 420 ELLEALdeEELEEELEELEEELEELEEELEELREELAELEAELEQ--LEEDGELAELLQELEEL 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1563-1778 |
2.44e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1563 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRD 1642
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1643 EAGEE-----------------RRRQLAKQLRDAEVER-DEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQ 1704
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdflDRLSALSKIADADADLlEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743142585 1705 LRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANG 1778
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1637-1791 |
2.58e-03 |
|
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: 41.83 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1637 DLQGRDEageeRRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKE-- 1714
Cdd:COG1579 11 DLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1715 -------LWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANgnlsKAAILE 1787
Cdd:COG1579 87 nnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA----ELEELE 162
|
....
gi 1743142585 1788 EKRQ 1791
Cdd:COG1579 163 AERE 166
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1654-1754 |
2.89e-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: 41.79 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1654 KQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLR-KMQAQMKELWREVEETRSSREeifsq 1732
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKeKMEEERENLLKEQERALESKL----- 265
|
90 100
....*....|....*....|...
gi 1743142585 1733 nRESEKRLK-GLEAEVLRLQEEL 1754
Cdd:cd16269 266 -KEQEALLEeGFKEQAELLQEEI 287
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1069-1405 |
3.27e-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: 42.90 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1069 FSSQAAEEEEKVKSLnklrlkyeaTITDMEDRLRKEEKGRQELEKLKRRLDG--ESSELQEQM------VEQQQRAEELR 1140
Cdd:NF012221 1491 FASSGDASAWQQKTL---------KLTAKAGSNRLEFKGTGHNDGLGYILDNvvATSESSQQAdavskhAKQDDAAQNAL 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1141 SQLGRKEEELQaalaRAEDEggaRAQLLKSLreaqaalAEAQEDLEA--ERVARTKAEKQRRDLGEELEALRGELED--- 1215
Cdd:NF012221 1562 ADKERAEADRQ----RLEQE---KQQQLAAI-------SGSQSQLEStdQNALETNGQAQRDAILEESRAVTKELTTlaq 1627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1216 TLDSTNAQQELRSKREQEVTE---------LKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLA 1286
Cdd:NF012221 1628 GLDALDSQATYAGESGDQWRNpfagglldrVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQAN 1707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1287 LEAEVSELRAelsslqtarqegeqrrrrlesqlqevqgragDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSK 1366
Cdd:NF012221 1708 AEQDIDDAKA-------------------------------DAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDAS 1756
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1743142585 1367 ELSSTEAQLH-DAQELLQEE----TRAKlALGSRV--RAMEAEAAG 1405
Cdd:NF012221 1757 AAENKANQAQaDAKGAKQDEsdkpNRQG-AAGSGLsgKAYSVEGVA 1801
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1261-1395 |
3.41e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1261 QALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKL 1340
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1341 QRAQAELEnvsgALNEAESKtirLSKELSSTEAQLhDAQELLQEETRAKLA-LGSR 1395
Cdd:PRK09039 133 ARALAQVE----LLNQQIAA---LRRQLAALEAAL-DASEKRDRESQAKIAdLGRR 180
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1605-1984 |
3.47e-03 |
|
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: 42.31 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1605 QVTELEDELTAAEDAKLRLEVTVQALKtqheRDLQGRDEAGEERRRQLAKQLRDAE-VERDEERKQRALavaarKKLEGE 1683
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLK----KELTNSESENSEKQRELEEKQNEIEkLKKENQSYKQEI-----KNLESQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1684 LEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRSSRE-------EIFSQNRESEKRLKGLEAEVLRLQEELAA 1756
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1757 SDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQleeeleeeqsnselLNDRYRKLLLQVESLTTELSaers 1836
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD--------------LTKKISSLKEKIEKLESEKK---- 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1837 fsakaesgrqQLERQIQELRGRLGEEDAGararhkMTIAALESKLAQAEEQLEQETRERilsgKLVRRAEKRLKEVVLQV 1916
Cdd:TIGR04523 535 ----------EKESKISDLEDELNKDDFE------LKKENLEKEIDEKNKEIEELKQTQ----KSLKKKQEEKQELIDQK 594
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743142585 1917 EEERrvaDQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRN 1984
Cdd:TIGR04523 595 EKEK---KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1660-1846 |
3.69e-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: 41.67 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1660 EVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKElwrEVEETRSSREEIfsqnresEKR 1739
Cdd:pfam09787 46 TLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEE---QLATERSARREA-------EAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1740 LKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRK 1819
Cdd:pfam09787 116 LERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNS 195
|
170 180
....*....|....*....|....*..
gi 1743142585 1820 LLLQVESLTTELSaersfSAKAESGRQ 1846
Cdd:pfam09787 196 LVLQLERMEQQIK-----ELQGEGSNG 217
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1249-1983 |
3.83e-03 |
|
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: 42.27 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1249 EAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGD 1328
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1329 GERARAEAAEKLQRAQAELENVSGALNEAESKTIRLS-KELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLR 1407
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1408 EQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEagaLEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQEL 1487
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAE---EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1488 DDASVDlEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLtraleeeqeareelerqnral 1567
Cdd:pfam02463 398 ELKSEE-EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK--------------------- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1568 raELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEE 1647
Cdd:pfam02463 456 --QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1648 RRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQ----AQMKELWREVEETR 1723
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleiDPILNLAQLDKATL 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1724 SSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEEL 1803
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1804 EEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRgrLGEEDAGARARHKMTIAALESKlaq 1883
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID--EEEEEEEKSRLKKEEKEEEKSE--- 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1884 aEEQLEQETRERILSgKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQR 1963
Cdd:pfam02463 769 -LSLKEKELAEEREK-TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
730 740
....*....|....*....|
gi 1743142585 1964 ELEDVTESAESMNREVTTLR 1983
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKE 866
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1131-1523 |
4.31e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.82 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1131 EQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALR 1210
Cdd:COG5278 104 EQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1211 GELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAE 1290
Cdd:COG5278 184 ALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1291 VSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSS 1370
Cdd:COG5278 264 AAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1371 TEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEE 1450
Cdd:COG5278 344 LALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743142585 1451 ARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVL 1523
Cdd:COG5278 424 LAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAA 496
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1085-1202 |
4.52e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1085 KLRLKYEATITDMEDRLRKEEKGRQELEKLKRrldgesselqEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEgGAR 1164
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAE-KEL 469
|
90 100 110
....*....|....*....|....*....|....*...
gi 1743142585 1165 AQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDL 1202
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPL 507
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
837-1223 |
4.73e-03 |
|
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: 42.03 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 837 EEERDLKVTDIIVSfQAAARGYLARRAFQKRQQQQSALRVMQRNCAAyLKLrhwqwwrlftkvkpllQVTRQDEVLQARA 916
Cdd:pfam15921 507 EKERAIEATNAEIT-KLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKL----------------QMAEKDKVIEILR 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 917 QELQKVQELQQQSAREVRELQGRVAQLEEERARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEeeecs 996
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ--------------EFKILKDKKDAKIRELEARVSD----- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 997 rqMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEE 1076
Cdd:pfam15921 630 --LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1077 EEKVKSLNKlrlkyeaTITDMEDRLRKEEKGRQELEKLKR-RLDGESSELQeQMVEQQQRAEELRSQLGRKEEELQAALA 1155
Cdd:pfam15921 708 LEQTRNTLK-------SMEGSDGHAMKVAMGMQKQITAKRgQIDALQSKIQ-FLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1156 RAEDEGGARAQLLKSLREAQAALAEAQEDLEA--ERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQ 1223
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEValDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1833-1928 |
4.80e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1833 AERSFSAKAESGRQQLERQIQELRGR--LGEEDAGARARHKMTIAALESKLAQAEEQLEQ-------ETRERILsgKLVR 1903
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSqaLAEAQQQELVALEGLAAELEEKQQELEAQLEQlqekaaeTSQERKQ--KRKE 220
|
90 100
....*....|....*....|....*.
gi 1743142585 1904 RAEKRLKEVVLQVEEERRVAD-QLRD 1928
Cdd:PRK11448 221 ITDQAAKRLELSEEETRILIDqQLRK 246
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1074-1406 |
5.15e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1074 AEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAA 1153
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1154 LARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQE 1233
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1234 VTELKKTLEEETRIH-EAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRR 1312
Cdd:COG4372 166 LAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1313 RRLESQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLAL 1392
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....
gi 1743142585 1393 GSRVRAMEAEAAGL 1406
Cdd:COG4372 326 KKLELALAILLAEL 339
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
898-1140 |
5.85e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 41.84 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 898 KVKPLLQVTRQDEVLQAraQELQKVQELQQQSAREVRElQGRVAQLEEERA--RLAEQLRAEAELcaeaeetrGRLAARK 975
Cdd:PLN03188 1015 KRNSLLKLTYSCEPSQA--PPLNTIPESTDESPEKKLE-QERLRWTEAESKwiSLAEELRTELDA--------SRALAEK 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 976 QELELvvsELEARVGEEEECSRQMQTE--KKRLQQ-------HIQELEAHLEAEEGARQklqLEKVTTEAKMKKFEEDLL 1046
Cdd:PLN03188 1084 QKHEL---DTEKRCAEELKEAMQMAMEghARMLEQyadleekHIQLLARHRRIQEGIDD---VKKAAARAGVRGAESKFI 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1047 -LLEDQNSKL----SKERKLLEDRLAEFSSQAAEEEEKVKSLNKL--RLK-YEATITDMEDRLRKEE----KGRQELEKL 1114
Cdd:PLN03188 1158 nALAAEISALkverEKERRYLRDENKSLQAQLRDTAEAVQAAGELlvRLKeAEEALTVAQKRAMDAEqeaaEAYKQIDKL 1237
|
250 260
....*....|....*....|....*.
gi 1743142585 1115 KRRLDGESSELQEQMVEQQQRAEELR 1140
Cdd:PLN03188 1238 KRKHENEISTLNQLVAESRLPKEAIR 1263
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1252-1630 |
6.33e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.54 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1252 VQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGER 1331
Cdd:COG3903 561 LREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAA 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1332 ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLE 1411
Cdd:COG3903 641 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1412 EEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGRRRLQQELDDAS 1491
Cdd:COG3903 721 AAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAA 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1492 VDLEQQRQLVSTLEkkqrkfDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1571
Cdd:COG3903 801 AAAAAAAAAAAAAA------ALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAA 874
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1743142585 1572 EALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQAL 1630
Cdd:COG3903 875 AAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1696-1988 |
6.42e-03 |
|
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: 41.48 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1696 QGKEEAVKQLRKMQAQMKELWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELaaSDRARRQAQQDRDEMADEV 1775
Cdd:COG5185 236 KGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENT--KEKIAEYTKSIDIKKATES 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1776 ANGNLSKAAILE--EKRQLEGRLGQLEEELEEEQSNSELLnDRYRKLLLQVESLTTELSAERSfSAKAESGRQQLERQIQ 1853
Cdd:COG5185 314 LEEQLAAAEAEQelEESKRETETGIQNLTAEIEQGQESLT-ENLEAIKEEIENIVGEVELSKS-SEELDSFKDTIESTKE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1854 ELRGRLGEedagARARHKMTIAALESKLAQAEEQLEQETRErilsgklvrraekrLKEVVLQVEEERRVADQLRDQLEKG 1933
Cdd:COG5185 392 SLDEIPQN----QRGYAQEILATLEDTLKAADRQIEELQRQ--------------IEQATSSNEEVSKLLNELISELNKV 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1743142585 1934 NLRVKQL--KRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1988
Cdd:COG5185 454 MREADEEsqSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1070-1214 |
6.74e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1070 SSQAAEEEEKVKSLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGR-KEE 1148
Cdd:COG2433 377 SIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEaRSE 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743142585 1149 ELQAALARAEdeggaraqlLKSLREaqaalaeaqedlEAERVartkaEKQRRDLGEELEALRGELE 1214
Cdd:COG2433 457 ERREIRKDRE---------ISRLDR------------EIERL-----ERELEEERERIEELKRKLE 496
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1048-1257 |
7.27e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1048 LEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVK---------SLNKLRLKYEATITDMEDRLRKEEKGRQELEKLKRRL 1118
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1119 DGESSELQEQMVEQQQraEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQ 1198
Cdd:COG3206 246 RAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1743142585 1199 rrdlgeELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQ 1257
Cdd:COG3206 324 ------ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
902-1266 |
7.57e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 902 LLQVTRQDEVLQARAQELQkvQELQQ-----QSAREVRELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQ 976
Cdd:PRK04863 309 LVEMARELAELNEAESDLE--QDYQAasdhlNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 977 ELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAhleaeegARQKLQLEKVTTEakmkKFEEDLLLLEDQNSKLS 1056
Cdd:PRK04863 387 AAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALER-------AKQLCGLPDLTAD----NAEDWLEEFQAKEQEAT 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1057 KERKLLEDRLAefSSQAAEE--EEKVKSLNKL-----RLKYEATITDMEDRLRKEEKGRQELEKLKRRLdgesSELqEQM 1129
Cdd:PRK04863 456 EELLSLEQKLS--VAQAAHSqfEQAYQLVRKIagevsRSEAWDVARELLRRLREQRHLAEQLQQLRMRL----SEL-EQR 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1130 VEQQQRAEELRSQLGRK-------EEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDL 1202
Cdd:PRK04863 529 LRQQQRAERLLAEFCKRlgknlddEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAA 608
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743142585 1203 GEELEALRGELEDTLDSTNA-----QQELRskREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGEL 1266
Cdd:PRK04863 609 QDALARLREQSGEEFEDSQDvteymQQLLE--RERELTVERDELAARKQALDEEIERLSQPGGSEDPRL 675
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
986-1212 |
7.71e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 986 EARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLlllEDQNSKLSKERKLLEDR 1065
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1066 LAefssQAAEEEEKVKSLNKL-----------RLKYEATITDMEDRLRKE-EKGRQELEKLKRRLDGESSELQEQMVEQQ 1133
Cdd:COG3883 92 AR----ALYRSGGSVSYLDVLlgsesfsdfldRLSALSKIADADADLLEElKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1743142585 1134 QRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEAERVARTKAEKQRRDLGEELEALRGE 1212
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1119-1374 |
8.27e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1119 DGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLEaERVARTKAE-K 1197
Cdd:pfam07888 12 ESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELE-SRVAELKEElR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1198 QRRDLGEELE-------ALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQL 1270
Cdd:pfam07888 91 QSREKHEELEekykelsASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1271 EQARRGKGAWEKTrlalEAEVSELRAELSSLQTARQEGEQRRRRLESQLQEVQGRAGDGERARAEaaekLQRAQAELENV 1350
Cdd:pfam07888 171 AERKQLQAKLQQT----EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE----NEALLEELRSL 242
|
250 260
....*....|....*....|....
gi 1743142585 1351 SGALNEAESKTIRLSKELSSTEAQ 1374
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSMAAQ 266
|
|
| DUF3498 |
pfam12004 |
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ... |
1075-1149 |
8.44e-03 |
|
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.
Pssm-ID: 463427 [Multi-domain] Cd Length: 511 Bit Score: 40.90 E-value: 8.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743142585 1075 EEEEKVKSLNKLRL--KYEATITDMEDRLRKEEKgrqELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEE 1149
Cdd:pfam12004 373 EESSGPESREELKQaeKYEQEISKLKERLRVSNR---KLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEE 446
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1325-1869 |
8.97e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.38 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1325 RAGDGERARAEAAEKLQRAQAelenvSGALNEAESkTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAA 1404
Cdd:COG3899 697 RAGERDRAARLLLRAARRALA-----RGAYAEALR-YLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLER 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1405 GLREQLEEEAAARERAGRELQ----TAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTEAVDRLERGR 1480
Cdd:COG3899 771 ALAARALAALAALRHGNPPASarayANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREAL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1481 RRLQQ------ELDDASVDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQ 1554
Cdd:COG3899 851 ELLREaleaglETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAA 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1555 EAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAAnDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQH 1634
Cdd:COG3899 931 LALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAA-AAAAAAAAAAAAAAALEAAAAALLALLAAAAAAA 1009
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1635 ERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRALAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKE 1714
Cdd:COG3899 1010 AAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALA 1089
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1715 LWREVEETRSSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEG 1794
Cdd:COG3899 1090 AALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAAL 1169
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743142585 1795 RLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARAR 1869
Cdd:COG3899 1170 ALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1093-1241 |
9.18e-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: 40.51 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1093 TITDME-DRLRKE-EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRSQLGRKEEELQAALARAEDEGGARAQLLKS 1170
Cdd:pfam09787 43 TALTLElEELRQErDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1743142585 1171 LREAQaalaeaqedleaERVARTKAEKQRR--DLGEELEALRGELEDTLDSTNAQQELrskrEQEVTELKKTL 1241
Cdd:pfam09787 123 LRYLE------------EELRRSKATLQSRikDREAEIEKLRNQLTSKSQSSSSQSEL----ENRLHQLTETL 179
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1111-1280 |
9.90e-03 |
|
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: 40.90 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1111 LEKLKRRLDGESSELQEQMVEQQQRAEE-LRSQLGRKEEELQAALARAEDEGGARAQllkslreaqaalaeaQEDLEAER 1189
Cdd:pfam09731 289 IAHAHREIDQLSKKLAELKKREEKHIERaLEKQKEELDKLAEELSARLEEVRAADEA---------------QLRLEFER 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743142585 1190 VARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEvTELKKTLEEETRIHEAAVQELRQRHG---QALGEL 1266
Cdd:pfam09731 354 EREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANLKgleKATSSH 432
|
170
....*....|....
gi 1743142585 1267 AEQLEQARRGKGAW 1280
Cdd:pfam09731 433 SEVEDENRKAQQLW 446
|
|
| |
