|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
1-454 |
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: 761.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1 MGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESG 80
Cdd:cd01380 209 QGGSPVIDGVDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDES 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 81 RVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFS--GKQHTFIGVLDIYGFETFDVN 158
Cdd:cd01380 289 QLAKWLCKRKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPvkEKQHSFIGVLDIYGFETFEVN 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 159 SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL 238
Cdd:cd01380 369 SFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 239 YNNFVNR-NPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHlcanffqenptppspfgsmi 317
Cdd:cd01380 449 YNQHLKKpNKHFKKPRFSNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR-------------------- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 tvksakqviKPnskhfrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:cd01380 509 ---------KK-------TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAA 572
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 398 SYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd01380 573 GFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| Myo5c_CBD |
cd15476 |
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ... |
1082-1449 |
0e+00 |
|
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins.MyoVb and myoVc areprimarily expressed in epithelial cells, and have been implicated as motors involved in recycling endosomes.
Pssm-ID: 271260 [Multi-domain] Cd Length: 332 Bit Score: 674.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1082 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1161
Cdd:cd15476 1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1162 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1241
Cdd:cd15476 81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1242 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1321
Cdd:cd15476 143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1322 NISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1401
Cdd:cd15476 205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462545116 1402 RKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKL 1449
Cdd:cd15476 285 RKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
1-465 |
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: 587.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1 MGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNE-RSSVSEDDSHLKVFCELLGLES 79
Cdd:smart00242 227 QGGCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 80 GRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNS 159
Cdd:smart00242 307 EELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 160 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKL 238
Cdd:smart00242 387 FEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 239 YNNFvNRNPLFEKP-RMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmi 317
Cdd:smart00242 467 NQHH-KKHPHFSKPkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS------------ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 tvksakQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:smart00242 534 ------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRA 607
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 398 SYPSRWTYIEFYSRYGILMTKQELSFS-DKKEVCKVVLHRLIQDSNQYQFGKTKIFFRAGQVAYLEKLR 465
Cdd:smart00242 608 GFPYRLPFDEFLQRYRVLLPDTWPPWGgDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
2-454 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 566.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGR 81
Cdd:pfam00063 223 SGCYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTE 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 82 VAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF-SGKQHTFIGVLDIYGFETFDVNSF 160
Cdd:pfam00063 303 LEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 161 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLY 239
Cdd:pfam00063 383 EQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLY 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 240 NNFvNRNPLFEKPR-MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptpPSPFGSMIT 318
Cdd:pfam00063 463 STF-SKHPHFQKPRlQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPD----YETAESAAA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 319 VKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQS 398
Cdd:pfam00063 538 NESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAG 617
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 399 YPSRWTYIEFYSRYGILMTK-QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:pfam00063 618 FPNRITFQEFVQRYRILAPKtWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| Myo5_CBD |
cd15470 |
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
1082-1448 |
0e+00 |
|
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.
Pssm-ID: 271254 [Multi-domain] Cd Length: 332 Bit Score: 562.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1082 EDEAKLIQNLILDLKPRGVVvNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1161
Cdd:cd15470 1 EDESRLIKNLITDLKPRGAV-GLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1162 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1241
Cdd:cd15470 80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1242 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1321
Cdd:cd15470 142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1322 NISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1401
Cdd:cd15470 204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462545116 1402 RKVQALLNSREDSS--QLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFK 1448
Cdd:cd15470 284 RKVQARLNERADSNqlQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2-1037 |
7.78e-173 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 556.61 E-value: 7.78e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSeDDSHLKVFCELLGLESGR 81
Cdd:COG5022 289 GGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIFS-DNSVLDKACYLLGIDPSL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 82 VAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFE 161
Cdd:COG5022 368 FVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK--MGILELLDEECLLPHGTDENWLQKLY 239
Cdd:COG5022 448 QLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 240 NNF-VNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENptppspfgsmit 318
Cdd:COG5022 528 QRLnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE------------ 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 319 vksakqvIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQS 398
Cdd:COG5022 596 -------ENIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAG 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 399 YPSRWTYIEFYSRYGILM-----TKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFRAGQVAYLEKLRLDKLRQSC 473
Cdd:COG5022 669 FPSRWTFDEFVQRYRILSpskswTGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIA 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 474 VMVQKHMRGWLQRKKFLRERRaaliIQQYFRGQQTVRKAITAVALKEAW-AAIIIQKHCRGYLVRSlYQLIRMATITMQA 552
Cdd:COG5022 749 TRIQRAIRGRYLRRRYLQALK----RIKKIQVIQHGFRLRRLVDYELKWrLFIKLQPLLSLLGSRK-EYRSYLACIIKLQ 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 553 YS--RGFLARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKEnhglVEKLTSLAA 630
Cdd:COG5022 824 KTikREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKID----VKSISSLKL 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 631 LRAGDVEKIQKLEAELEKaaTHRRNYEEKgkryrdavEEKLAKLQKHN--------SELETQKEQIQLKLQEKTEELKE- 701
Cdd:COG5022 900 VNLELESEIIELKKSLSS--DLIENLEFK--------TELIARLKKLLnnidleegPSIEYVKLPELNKLHEVESKLKEt 969
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 702 --KMDNLTKQLfdDVQKEERQRMLLE-KSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDgLKAEVARLS 778
Cdd:COG5022 970 seEYEDLLKKS--TILVREGNKANSElKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISS-ESTELSILK 1046
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 779 KQVKTISEFEKEIELLQAQKIDVekhvqSQKREMREKMSeitkqlLESYDIEDVRSRLSVedlehLNEDGELWFAYEGLK 858
Cdd:COG5022 1047 PLQKLKGLLLLENNQLQARYKAL-----KLRRENSLLDD------KQLYQLESTENLLKT-----INVKDLEVTNRNLVK 1110
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 859 KATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTsenmmIPDFKQQISELEKQK 938
Cdd:COG5022 1111 PANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPS-----PPPFAALSEKRLYQS 1185
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 939 QDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKlidkiQEMQEASDHLKKQFETESEVKCN 1018
Cdd:COG5022 1186 ALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYS-----TSLKGFNNLNKKFDTPASMSNEK 1260
|
1050 1060
....*....|....*....|.
gi 2462545116 1019 FRQEASRL--TLENRDLEEEL 1037
Cdd:COG5022 1261 LLSLLNSIdnLLSSYKLEEEV 1281
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
2-454 |
1.24e-164 |
|
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: 509.44 E-value: 1.24e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNE--RSSVSEDDSHLKVFCELLGLES 79
Cdd:cd00124 219 SGCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 80 GRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQH--TFIGVLDIYGFETFDV 157
Cdd:cd00124 299 EDLEEALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEV 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 158 NSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQ 236
Cdd:cd00124 379 NSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 237 KLYNNFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfhlcanffqenptppspfgsm 316
Cdd:cd00124 459 KLYSAHGSHPRFFSKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS----------------------- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 317 itvksakqvikpnskhfrttvGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISA 396
Cdd:cd00124 516 ---------------------GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRR 574
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 397 QSYPSRWTYIEFYSRYGILMTK-QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd00124 575 AGYPVRLPFDEFLKRYRILAPGaTEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| Myo5b_CBD |
cd15477 |
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ... |
1081-1452 |
9.26e-163 |
|
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.
Pssm-ID: 271261 Cd Length: 372 Bit Score: 494.38 E-value: 9.26e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1081 REDEAKLIQNLILDLKPRgVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSN 1160
Cdd:cd15477 1 KEDEALLIRNLVTDLKPQ-AVSATVPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1161 TCHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISG 1240
Cdd:cd15477 80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1241 LKPTGFRKRSSSIDDTD-GYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQI 1319
Cdd:cd15477 160 VKPMGYRKRSSSMADGDnSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1320 RCNISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPS 1399
Cdd:cd15477 240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 1400 FVRKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKLGFL 1452
Cdd:cd15477 320 FIRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1081-1455 |
6.96e-161 |
|
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.
Pssm-ID: 271262 Cd Length: 375 Bit Score: 489.54 E-value: 6.96e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1081 REDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSN 1160
Cdd:cd15478 1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1161 TCHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISG 1240
Cdd:cd15478 81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1241 LKPTGFRKRSSSIDDTDGYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIR 1320
Cdd:cd15478 161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1321 CNISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSF 1400
Cdd:cd15478 241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 1401 VRKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKLGFLNRL 1455
Cdd:cd15478 321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
3-454 |
2.43e-145 |
|
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: 459.24 E-value: 2.43e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd01377 217 GELTIDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd01377 297 LKALLKPRIKVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQ 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYN 240
Cdd:cd01377 377 LCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYS 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 241 NFVNRNPLFEKPRMS--NTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqENPTPPSPFGSMIT 318
Cdd:cd01377 457 NHLGKSKNFKKPKPKksEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLF-KDYEESGGGGGKKK 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 319 VKSAKqvikpnskhFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQS 398
Cdd:cd01377 536 KKGGS---------FR-TVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKG 605
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 399 YPSRWTYIEFYSRYGILM-TKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd01377 606 FPNRIIFAEFKQRYSILApNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
7-454 |
9.82e-136 |
|
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: 432.87 E-value: 9.82e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 7 IEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDS---HLKVFCELLGLESGRVA 83
Cdd:cd01384 216 LDGVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKsefHLKAAAELLMCDEKALE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 84 QWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQF 163
Cdd:cd01384 296 DALCKRVIVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQF 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 164 CINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNF 242
Cdd:cd01384 376 CINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPRSTHETFAQKLYQTL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 243 VNrNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptPPSPFGSmiTVKSA 322
Cdd:cd01384 456 KD-HKRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF-----PPLPREG--TSSSS 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 323 KqvikpnskhFrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSR 402
Cdd:cd01384 528 K---------F-SSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTR 597
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 403 WTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLiqDSNQYQFGKTKIFFR 454
Cdd:cd01384 598 KPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKA--GLKGYQIGKTKVFLR 647
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
6-454 |
1.25e-129 |
|
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: 416.33 E-value: 1.25e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 6 VIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQW 85
Cdd:cd01383 208 TIDGVDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 86 LCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQH-TFIGVLDIYGFETFDVNSFEQFC 164
Cdd:cd01383 288 LSTRKIQAGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLC 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 165 INYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFV 243
Cdd:cd01383 368 INYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 244 NRNPLFEKPRmsNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLcanffqenptpPSPFGSMITVKSAK 323
Cdd:cd01383 447 KSNSCFKGER--GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQL-----------PQLFASKMLDASRK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 324 Q--VIKPNSKHF-RTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYP 400
Cdd:cd01383 514 AlpLTKASGSDSqKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYP 593
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 401 SRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd01383 594 TRMTHQEFARRYGFLLPEDVSASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
1-454 |
1.46e-123 |
|
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: 400.09 E-value: 1.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1 MGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITA--VGNERSSVSEDDSHLKVFCELLGLE 78
Cdd:cd01381 205 QGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVP 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 79 SGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-QFSGKQH--TFIGVLDIYGFETF 155
Cdd:cd01381 285 KQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIyKPRGTDSsrTSIGVLDIFGFENF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 156 DVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLI-EAKMGILELLDEECLLPHGTDENW 234
Cdd:cd01381 365 EVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEFVDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTM 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 235 LQKLYNNFVNrNPLFEKPRM-SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENptppSPF 313
Cdd:cd01381 445 LEKLHSTHGN-NKNYLKPKSdLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNED----ISM 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 314 GSmitvKSAKQVIkpnskhfrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIR 393
Cdd:cd01381 520 GS----ETRKKSP---------TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIR 586
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 394 ISAQSYPSRWTYIEFYSRYGIL------MTKQELSFSDKKEVCKVVLHrliqDSNqYQFGKTKIFFR 454
Cdd:cd01381 587 IRKAGYPIRHTFEEFVERYRVLvpgippAHKTDCRAATRKICCAVLGG----DAD-YQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
2-454 |
4.30e-123 |
|
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: 398.84 E-value: 4.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSeDDSHLKVFCELLGLESGR 81
Cdd:cd01378 210 SGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAIS-DTSVLDFVAYLLGVDPDQ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 82 VAQWLCNRKIVTSSE---TVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQH-TFIGVLDIYGFETFDV 157
Cdd:cd01378 289 LEKALTHRTIETGGGgrsVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 158 NSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWL 235
Cdd:cd01378 369 NSFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLTAGdATDQTFL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 236 QKLyNNFVNRNPLFEKP----RMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPtpps 311
Cdd:cd01378 449 QKL-NQLFSNHPHFECPsghfELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV---- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 312 pfgsmitvksakqviKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLET 391
Cdd:cd01378 524 ---------------DLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLEN 588
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 392 IRISAQSYPSRWTYIEFYSRYGILMTKQELSFS-DKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd01378 589 VRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDgTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
4-454 |
6.66e-120 |
|
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: 390.29 E-value: 6.66e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 4 NTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGN--ERSSVSEDDSHLKVFCELLGLESGR 81
Cdd:cd14903 208 TIKIEGMSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNddEKSAIAPGDQGAVYATKLLGLSPEA 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 82 VAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFE 161
Cdd:cd14903 288 LEKALCSRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14903 368 QFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSMITVKS 321
Cdd:cd14903 448 HKDEQDVIEFPRTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 322 AKQVIKPNSKhfrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPS 401
Cdd:cd14903 528 RRRRGGALTT---TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPN 604
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 402 RWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRL-IQDSNQYQFGKTKIFFR 454
Cdd:cd14903 605 RLLHEEFLDKFWLFLPEGRNTDVPVAERCEALMKKLkLESPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
7-454 |
5.06e-118 |
|
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: 385.14 E-value: 5.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 7 IEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSH-LKVFCELLGLESGRVAQW 85
Cdd:cd14883 213 IDNINDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEiLKIVAKLLGVDPDKLKKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 86 LCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCI 165
Cdd:cd14883 293 LTIRQINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 166 NYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvN 244
Cdd:cd14883 373 NYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-E 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 245 RNPLFEKP--RMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFF--QENPTPPSPFGSMITVK 320
Cdd:cd14883 452 KHPYYEKPdrRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtyPDLLALTGLSISLGGDT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 321 SAKQvikpnSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYP 400
Cdd:cd14883 532 TSRG-----TSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFP 606
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 401 SRWTYIEFYSRYGILMTK-QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14883 607 IHLTFKEFVDRYLCLDPRaRSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
7-454 |
1.49e-115 |
|
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: 377.96 E-value: 1.49e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 7 IEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCE---LLGLESGRVA 83
Cdd:cd14872 209 VEGVDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLE 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 84 QWLCNRKI-VTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-QFSGKQHTFIGVLDIYGFETFDVNSFE 161
Cdd:cd14872 289 EALTSRLMeIKGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYN 240
Cdd:cd14872 369 QLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 241 NF-VNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptPPSpfgsmitv 319
Cdd:cd14872 449 THaAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-----PPS-------- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 320 ksakqviKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSY 399
Cdd:cd14872 516 -------EGDQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGY 588
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545116 400 PSRWTYIEFYSRYGILMTKQELSF-SDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14872 589 PFRYSHERFLKRYRFLVKTIAKRVgPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
8-454 |
4.24e-112 |
|
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: 370.17 E-value: 4.24e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 8 EGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI---TAVGNERSSVSEDDShLKVFCELLGLESGRVAQ 84
Cdd:cd01385 214 EGEDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYkkkAYHRDESVTVGNPEV-LDIISELLRVKEETLLE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 85 WLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQ----FSGKQHTFIGVLDIYGFETFDVNSF 160
Cdd:cd01385 293 ALTTKKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALLnkkdLEEAKGLSIGVLDIFGFEDFGNNSF 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 161 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKlY 239
Cdd:cd01385 373 EQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-F 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 240 NNFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK-----------------------F 296
Cdd:cd01385 452 KQQHKDNKYYEKPQVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligidpvavfrwavlraF 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 297 HLCANFFQE----NPTPPSPFGSMITVKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPF 372
Cdd:cd01385 532 FRAMAAFREagrrRAQRTAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPL 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 373 EFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSfsdKKEVCKVVLHRLIQDSNQYQFGKTKIF 452
Cdd:cd01385 612 RFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEKLNLDRDNYQIGKTKVF 688
|
..
gi 2462545116 453 FR 454
Cdd:cd01385 689 LK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
8-454 |
9.34e-111 |
|
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: 364.89 E-value: 9.34e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 8 EGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSsvseDDSHLKVFCELLGLESGRVAQWL 86
Cdd:cd14873 222 KTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEfITAGGAQVS----FKTALGRSAELLGLDPTQLTDAL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 87 CNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQfsGKQH-TFIGVLDIYGFETFDVNSFEQFCI 165
Cdd:cd14873 298 TQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIK--GKEDfKSIGILDIFGFENFEVNHFEQFNI 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 166 NYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNr 245
Cdd:cd14873 376 NYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHAN- 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 246 NPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmITVKSAKQV 325
Cdd:cd14873 455 NHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEH-----------VSSRNNQDT 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 326 IKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTY 405
Cdd:cd14873 524 LKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPF 603
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2462545116 406 IEFYSRYGILMtKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14873 604 QDFYKRYKVLM-RNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
5-454 |
4.27e-109 |
|
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: 360.41 E-value: 4.27e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 5 TVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGnERSSVSEDDSHLKVFCELLGLESGRVAQ 84
Cdd:cd14904 212 MQIPGLDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSD-ENGSRISNGSQLSQVAKMLGLPTTRIEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 85 WLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQF 163
Cdd:cd14904 291 ALCNRSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQF 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 164 CINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFV 243
Cdd:cd14904 371 CINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQ 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 244 NR--NPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSmitvKS 321
Cdd:cd14904 451 TKkdNESIDFPKVKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEG----KS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 322 AKQVIKPNSkhfrttVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPS 401
Cdd:cd14904 527 GKGTKAPKS------LGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPS 600
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 402 RWTYIEFYSRYGIlMTKQELSFSDKKEVCKVVLHRLIQDSN-QYQFGKTKIFFR 454
Cdd:cd14904 601 RLTPKELATRYAI-MFPPSMHSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
2-454 |
5.46e-106 |
|
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: 352.13 E-value: 5.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNV-----QITAvGNERSSVSEDdSHLKVFCELLG 76
Cdd:cd01387 206 GGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVyfhkrQLRH-GQEGVSVGSD-AEIQWVAHLLQ 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 77 LESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFD 156
Cdd:cd01387 284 ISPEGLQKALTFKVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLS 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 157 VNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWL 235
Cdd:cd01387 364 ENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 236 QKLYNNFvNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQ------ENPTP 309
Cdd:cd01387 444 EKCHYHH-ALNELYSKPRMPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSshraqtDKAPP 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 310 PSPFGSMITVKsakqvikpnskhFRT-TVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGV 388
Cdd:cd01387 523 RLGKGRFVTMK------------PRTpTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGM 590
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 389 LETIRISAQSYPSRWTYIEFYSRYGILMtKQELSFSDKKEVCKVVLHRL--IQDSNQYQFGKTKIFFR 454
Cdd:cd01387 591 LETIRIRKEGYPVRLPFQVFIDRYRCLV-ALKLPRPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
18-454 |
4.15e-105 |
|
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: 348.88 E-value: 4.15e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 18 ETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNE----RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVT 93
Cdd:cd01379 227 EIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 94 SSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYAN 169
Cdd:cd01379 307 RGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDrsasDEPLS-IGILDIFGFENFQKNSFEQLCINIAN 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 170 EKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvnRNPL 248
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKY 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 249 FEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqENPTppspfgsmitvksakqvikp 328
Cdd:cd01379 464 YWRPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSS----------ENPL-------------------- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 329 nskhFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEF 408
Cdd:cd01379 514 ----VRQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADF 589
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2462545116 409 YSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 454
Cdd:cd01379 590 LKRYYFLAFKWNEEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
10-454 |
2.02e-102 |
|
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: 341.92 E-value: 2.02e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 10 VNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNER---SSVSEDDSH-LKVFCELLGLESGRVAQW 85
Cdd:cd01382 200 LDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVS 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 86 LCNRKIVTSSE----TVVK-PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHtFIGVLDIYGFETFDVNSF 160
Cdd:cd01382 280 LTTRVMQTTRGgakgTVIKvPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSSY-FIGVLDIAGFEYFEVNSF 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 161 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLY 239
Cdd:cd01382 359 EQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVH 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 240 NNFVNrNPLFEKPRMS----------NTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTP 309
Cdd:cd01382 439 QKHKN-HFRLSIPRKSklkihrnlrdDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNN 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 310 PSpfgsmitvKSAKQVIKPNSKhfrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVL 389
Cdd:cd01382 518 NK--------DSKQKAGKLSFI----SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMV 585
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 390 ETIRISAQSYPSRWTYIEFYSRYGILMTKqELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd01382 586 SVLDLMQGGFPSRTSFHDLYNMYKKYLPP-KLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
8-452 |
2.03e-101 |
|
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: 339.07 E-value: 2.03e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 8 EGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWL 86
Cdd:cd14901 232 DGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 87 CNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF--SGKQHTFIGVLDIYGFETFDVNSFEQFC 164
Cdd:cd14901 312 CTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYseSTGASRFIGIVDIFGFEIFATNSLEQLC 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 165 INYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFV 243
Cdd:cd14901 392 INFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 244 NRNPL-FEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCAnffqenptppspfgsmitvksa 322
Cdd:cd14901 472 KHASFsVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS---------------------- 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 323 kqvikpnskhfrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSR 402
Cdd:cd14901 530 ------------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVR 597
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 403 WTYIEFYSRYGILMTKQElsfSDKKEVCKVVLHR---------LIQDSNQYQFGKTKIF 452
Cdd:cd14901 598 FPHDAFVHTYSCLAPDGA---SDTWKVNELAERLmsqlqhselNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
3-454 |
7.05e-101 |
|
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: 337.89 E-value: 7.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTV-IEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKV--FCELLGLES 79
Cdd:cd14892 226 GNCVeVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVakAAGLLGVDA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 80 GRVAQWLCNRKIVTSSETVVK-PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQ----------FSGKQHTFIGVLD 148
Cdd:cd14892 306 AELMFKLVTQTTSTARGSVLEiKLTAREAKNALDALCKYLYGELFDWLISRINACHKqqtsgvtggaASPTFSPFIGILD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 149 IYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLP 227
Cdd:cd14892 386 IFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLK 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 228 H-GTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqen 306
Cdd:cd14892 466 RkTTDKQLLTIYHQTHLDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS------------ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 307 ptppspfgsmitvksakqvikpnskhfrttvgSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRAC 386
Cdd:cd14892 534 --------------------------------SKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYS 581
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 387 GVLETIRISAQSYPSRWTYIEFYSRYGIL---MTKQELSFSDK------KEVCKVVLHRLiqDSNQYQFGKTKIFFR 454
Cdd:cd14892 582 GVLEVVRIRREGFPIRRQFEEFYEKFWPLarnKAGVAASPDACdattarKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
6-454 |
1.27e-100 |
|
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: 337.13 E-value: 1.27e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 6 VIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVgnERSSVSEDDS---HLKVFCELLGLESGRV 82
Cdd:cd14890 233 SIPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATtlqSLKLAAELLGVNEDAL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14890 311 EKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM----GILELLDEECLLpHGTDEN--WLQ 236
Cdd:cd14890 391 LCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRF-KGEEANkkFVS 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 237 KLYNNF------------VNRNPLFEKPRMSNT-SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanff 303
Cdd:cd14890 470 QLHASFgrksgsggtrrgSSQHPHFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS--------- 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 304 qenptppspfGSMITVKSakqvikpnskhfrttVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQL 383
Cdd:cd14890 541 ----------RRSIREVS---------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQL 595
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 384 RACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQElsfsDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14890 596 KYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAE----NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
7-454 |
2.46e-99 |
|
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: 333.58 E-value: 2.46e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 7 IEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSSV--SEDDSHLKVFCELLGLESGRVA 83
Cdd:cd14888 247 LPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVvsASCTDDLEKVASLLGVDAEDLL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 84 QWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHT-FIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14888 327 NALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLlFCGVLDIFGFECFQLNSFEQ 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14888 407 LCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKDQGLCNKLCQK 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNrNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfhlcanffqeNPTPPSPFGSMItvkS 321
Cdd:cd14888 487 HKG-HKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK----------NPFISNLFSAYL---R 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 322 AKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPS 401
Cdd:cd14888 553 RGTDGNTKKKKFV-TVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPV 631
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 402 RWTYIEFYSRYGILMTKQE-LSFSdkkevckvvlhrliqdsnQYQFGKTKIFFR 454
Cdd:cd14888 632 RLSHAEFYNDYRILLNGEGkKQLS------------------IWAVGKTLCFFK 667
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
3-454 |
9.34e-95 |
|
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: 321.13 E-value: 9.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14927 222 GVTTVDNMDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14927 302 LKGLLHPRVKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQ 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14927 382 LCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDN 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPRMSN-----TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqENptppspFGSM 316
Cdd:cd14927 462 HLGKSPNFQKPRPDKkrkyeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY-EN------YVGS 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 317 ITVKSAKQVIKPNSKHFRT--TVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRI 394
Cdd:cd14927 535 DSTEDPKSGVKEKRKKAASfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRI 614
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 395 SAQSYPSRWTYIEFYSRYGILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14927 615 CRKGFPNRILYADFKQRYRILNPSAipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
25-454 |
1.81e-92 |
|
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: 314.15 E-value: 1.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 25 LLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 103
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHT 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 104 RPQAVNARDALAKKIYAHLFDFIVERINQAL----QFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMH 179
Cdd:cd14889 312 KQQAEDARDSIAKVAYGRVFGWIVSKINQLLapkdDSSVELRE-IGILDIFGFENFAVNRFEQACINLANEQLQYFFNHH 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 180 VFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMSNTS 258
Cdd:cd14889 391 IFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHF-KGNSYYGKSRSKSPK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 259 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQenpTPPSPFGSMITVKSAKQVIKPNSKHFRT-TV 337
Cdd:cd14889 470 FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFT---ATRSRTGTLMPRAKLPQAGSDNFNSTRKqSV 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 338 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 417
Cdd:cd14889 547 GAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLC 626
|
410 420 430
....*....|....*....|....*....|....*..
gi 2462545116 418 KQELSFSdkKEVCKVVLHRliQDSNQYQFGKTKIFFR 454
Cdd:cd14889 627 EPALPGT--KQSCLRILKA--TKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
3-454 |
6.11e-92 |
|
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: 312.93 E-value: 6.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14909 216 GKVTVPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAEL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14909 296 YKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQ 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14909 376 LCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNT 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPRMSNTS-----FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGsm 316
Cdd:cd14909 456 HLGKSAPFQKPKPPKPGqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGE-- 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 317 itvkSAKQVIKPNSKHFrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISA 396
Cdd:cd14909 534 ----QAKGGRGKKGGGF-ATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICR 608
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 397 QSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14909 609 KGFPNRMMYPDFKMRYKILNPAGIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
3-454 |
1.24e-91 |
|
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: 311.99 E-value: 1.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14913 218 GEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14913 298 LKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQ 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14913 378 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPRM----SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptppSPFGSMI 317
Cdd:cd14913 458 HLGKSNNFQKPKVvkgrAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-------ATFATAD 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 TVKSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:cd14913 531 ADSGKKKVAKKKGSSFQ-TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRK 609
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 398 SYPSRWTYIEFYSRYGILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14913 610 GFPNRILYGDFKQRYRVLNASAipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
2-454 |
2.89e-90 |
|
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: 308.09 E-value: 2.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGR 81
Cdd:cd14920 214 NGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 82 VAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSF 160
Cdd:cd14920 294 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSF 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 161 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQ 236
Cdd:cd14920 374 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 237 KLYNNfVNRNPLFEKPRM--SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQE-NPTPPSPF 313
Cdd:cd14920 454 KLVQE-QGSHSKFQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvDRIVGLDQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 314 GSMITVKSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIR 393
Cdd:cd14920 533 VTGMTETAFGSAYKTKKGMFR-TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIR 611
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 394 ISAQSYPSRWTYIEFYSRYGILMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14920 612 ICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
3-454 |
9.53e-88 |
|
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: 300.74 E-value: 9.53e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14929 212 GAVAVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14929 292 VKGLIHPRIKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14929 372 LCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDN 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPRMSNTSFVIQ----HFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPS--PFGS 315
Cdd:cd14929 452 HFGKSVHFQKPKPDKKKFEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSaiQFGE 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 316 mitvksaKQVIKPNSKHfrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRIS 395
Cdd:cd14929 532 -------KKRKKGASFQ---TVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRIC 601
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 396 AQSYPSRWTYIEFYSRYGILMTK--QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14929 602 REGFPNRLLYADFKQRYCILNPRtfPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
3-454 |
2.33e-86 |
|
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: 297.01 E-value: 2.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14917 218 GETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14917 298 LKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQ 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14917 378 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDN 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPR----MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPfgsmi 317
Cdd:cd14917 458 HLGKSNNFQKPRnikgKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP----- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 tVKSAKQVIKPNSKHfrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:cd14917 533 -IEKGKGKAKKGSSF--QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRK 609
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 398 SYPSRWTYIEFYSRYGILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14917 610 GFPNRILYGDFRQRYRILNPAAipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
3-454 |
8.26e-84 |
|
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: 289.71 E-value: 8.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14918 218 GEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14918 298 LKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14918 378 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPRM----SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptppSPFGSMI 317
Cdd:cd14918 458 HLGKSANFQKPKVvkgkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF-------STYASAE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 TVKSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:cd14918 531 ADSGAKKGAKKKGSSFQ-TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 609
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 398 SYPSRWTYIEFYSRYGILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14918 610 GFPSRILYGDFKQRYKVLNASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
3-454 |
9.13e-84 |
|
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: 289.57 E-value: 9.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGF-KEDFQMdVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGR 81
Cdd:cd14911 224 GSLPVPGVDDYAEFQATVKSMNIMGMtSEDFNS-IFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTD 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 82 VAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSF 160
Cdd:cd14911 303 MTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 161 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLY 239
Cdd:cd14911 383 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 240 NNFvNRNPLFEKPRMSNTS-FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSMIT 318
Cdd:cd14911 463 SAH-SMHPKFMKTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 319 VKSAKQVIKpnsKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQS 398
Cdd:cd14911 542 TQFGARTRK---GMFR-TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQG 617
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 399 YPSRWTYIEFYSRYGILMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14911 618 FPNRIPFQEFRQRYELLTPNViPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
3-454 |
2.21e-83 |
|
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: 288.08 E-value: 2.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14934 214 GVTVVDNMDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14934 294 QKGITRPRVKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQ 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14934 374 LCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDN 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKP-----RMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpfgsm 316
Cdd:cd14934 454 HLGKSSNFLKPkggkgKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG----- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 317 itvkSAKQviKPNSKHFrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISA 396
Cdd:cd14934 529 ----SKKQ--KRGSSFM--TVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICR 600
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 397 QSYPSRWTYIEFYSRYGILMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14934 601 KGFPNRLQYPEFKQRYQVLNPNViPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
3-454 |
9.84e-83 |
|
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: 286.57 E-value: 9.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14916 219 GEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14916 299 LKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14916 379 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDN 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPR----MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpfGSMI 317
Cdd:cd14916 459 HLGKSNNFQKPRnvkgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADT--GDSG 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 TVKSAKQvikpNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:cd14916 537 KGKGGKK----KGSSFQ-TVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRK 611
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 398 SYPSRWTYIEFYSRYGIL--MTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14916 612 GFPNRILYGDFRQRYRILnpAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
25-454 |
3.12e-82 |
|
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: 283.89 E-value: 3.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 25 LLGF-KEDFQMdVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 103
Cdd:cd14897 237 LIGFsEEDISV-IFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKS 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 104 RPQAVNARDALAKKIYAHLFDFIVERINQAL----QFSGK-QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 178
Cdd:cd14897 316 LRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMtRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFND 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 179 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNRNPLFEKPRMSNT 257
Cdd:cd14897 396 YVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRV 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 258 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFqenptppspfgsmitvksakqvikpnSKHfrttv 337
Cdd:cd14897 475 AFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF--------------------------TSY----- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 338 gskFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 417
Cdd:cd14897 524 ---FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICD 600
|
410 420 430
....*....|....*....|....*....|....*..
gi 2462545116 418 KQELSFSDKKEVCKVVLHrlIQDSNQYQFGKTKIFFR 454
Cdd:cd14897 601 FSNKVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
3-454 |
5.03e-82 |
|
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: 284.70 E-value: 5.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14910 220 GEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14910 300 LKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14910 380 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPRMSN----TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGsmi 317
Cdd:cd14910 460 HLGKSNNFQKPKPAKgkveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEG--- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 tvkSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:cd14910 537 ---GGKKGGKKKGSSFQ-TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 612
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 398 SYPSRWTYIEFYSRYGILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14910 613 GFPSRILYADFKQRYKVLNASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
3-454 |
5.11e-82 |
|
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: 284.70 E-value: 5.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14912 220 GEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14912 300 LKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14912 380 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPRM----SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSmi 317
Cdd:cd14912 460 HLGKSANFQKPKVvkgkAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAG-- 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 tvKSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:cd14912 538 --GGAKKGGKKKGSSFQ-TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 614
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 398 SYPSRWTYIEFYSRYGILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14912 615 GFPSRILYADFKQRYKVLNASAipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
3-454 |
1.30e-81 |
|
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: 283.46 E-value: 1.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14932 219 GNVTIPGQQDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDF 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFE 161
Cdd:cd14932 299 TRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQK 237
Cdd:cd14932 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 238 LYNNFVNrNPLFEKPR--MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGS 315
Cdd:cd14932 459 VVQEQGN-NPKFQKPKklKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKV 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 316 MITVKSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRIS 395
Cdd:cd14932 538 AGMGESLHGAFKTRKGMFR-TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRIC 616
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 396 AQSYPSRWTYIEFYSRYGILM-TKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14932 617 RQGFPNRIVFQEFRQRYEILTpNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
3-454 |
7.98e-80 |
|
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: 278.11 E-value: 7.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14923 219 GEVTVASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEM 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14923 299 LKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14923 379 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPR----MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGSmi 317
Cdd:cd14923 459 HLGKSNNFQKPKpakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSG-- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 tvkSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:cd14923 537 ---GSKKGGKKKGSSFQ-TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRK 612
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 398 SYPSRWTYIEFYSRYGILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14923 613 GFPSRILYADFKQRYRILNASAipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
2-454 |
1.49e-79 |
|
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: 277.30 E-value: 1.49e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI---TAVGNERSSVSeDDSHLKVFCELLGLE 78
Cdd:cd14907 239 SNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddsTLDDNSPCCVK-NKETLQIIAKLLGID 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 79 SGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL--QFSGKQHTF------IGVLDIY 150
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIF 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 151 GFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTL--IDFYDNQPVIDLIE-AKMGILELLDEECLLP 227
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 228 HGTDENWLQKLYNNFvNRNPLFEKPRMSN-TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEN 306
Cdd:cd14907 478 TGTDEKLLNKIKKQH-KNNSKLIFPNKINkDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 307 ptppspFGSMITVKSAKQVIKPNSKhfrtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRAC 386
Cdd:cd14907 557 ------DGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 387 GVLETIRISAQSYPSRWTYIEFYSRYGILmtkqelsfsdkkevckvvlhrliqdSNQYQFGKTKIFFR 454
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLL-------------------------KKNVLFGKTKIFMK 669
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
8-454 |
1.50e-79 |
|
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: 278.37 E-value: 1.50e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 8 EGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVqitAVGNERSSVSEDDS--------------------- 66
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNV---LFVASSEDEGEEDNgaasapcrlasaspssltvqq 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 67 HLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQA---LQFSGKQHT- 142
Cdd:cd14895 314 HLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAspqRQFALNPNKa 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 143 -------FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-M 214
Cdd:cd14895 394 ankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 215 GILELLDEECLLPHGTDENWLQKLYNNFVNRNPlFEKPR--MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEIL- 291
Cdd:cd14895 474 GIFSLLDEECVVPKGSDAGFARKLYQRLQEHSN-FSASRtdQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLg 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 292 RASKFHL--CANFFQENPTPPSPFGSMITVKSAKQVIKpnskhfrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEK 369
Cdd:cd14895 553 KTSDAHLreLFEFFKASESAELSLGQPKLRRRSSVLSS-------VGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDES 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 370 LPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKvVLHRLiqdsnQYQFGKT 449
Cdd:cd14895 626 ASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIE-TLKVD-----HAELGKT 699
|
....*
gi 2462545116 450 KIFFR 454
Cdd:cd14895 700 RVFLR 704
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
3-454 |
3.59e-79 |
|
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: 276.23 E-value: 3.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14915 220 GEITVPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQ 162
Cdd:cd14915 300 LKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 163 FCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNN 241
Cdd:cd14915 380 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 242 FVNRNPLFEKPR----MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPFGsmi 317
Cdd:cd14915 460 HLGKSNNFQKPKpakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGG--- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 318 tvkSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQ 397
Cdd:cd14915 537 ---GGKKGGKKKGSSFQ-TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 612
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 398 SYPSRWTYIEFYSRYGILMTKQ--ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14915 613 GFPSRILYADFKQRYKVLNASAipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
2-454 |
3.86e-79 |
|
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: 276.40 E-value: 3.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVS---EDDSHLKVFCELLGLE 78
Cdd:cd14908 236 GGAPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARVAKLLGVD 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 79 SGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ--HTFIGVLDIYGFETFD 156
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 157 VNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLP-HGTDENW 234
Cdd:cd14908 396 HNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANY 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 235 LQKLYNNFVNRNP--LFEKPRMSNTS-------FVIQHFADKVEYKCE-GFLEKNRDTVydmlveilraskfhlcanffq 304
Cdd:cd14908 476 ASRLYETYLPEKNqtHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKDEI--------------------- 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 305 enptppspfgsmitvksakqvikPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLR 384
Cdd:cd14908 535 -----------------------PLTADSLFESGQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 385 ACGVLETIRISAQSYPSRWTYIEFYSRYGILMT---KQELSFSDK---------KEVCKV-VLHRLIQD--------SNQ 443
Cdd:cd14908 592 YGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPlipEVVLSWSMErldpqklcvKKMCKDlVKGVLSPAmvsmknipEDT 671
|
490
....*....|.
gi 2462545116 444 YQFGKTKIFFR 454
Cdd:cd14908 672 MQLGKSKVFMR 682
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
19-452 |
7.77e-78 |
|
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: 272.11 E-value: 7.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 19 TQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSS---VSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSS 95
Cdd:cd14880 231 TREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 96 ETVV--KPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 172
Cdd:cd14880 311 QQQVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSIcADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 173 QQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEK 251
Cdd:cd14880 391 QQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSpISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGH 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 252 PRMS-NTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTppspfgsmitvKSAKQVIKPNS 330
Cdd:cd14880 471 NKLSrEPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQS 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 331 KHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYS 410
Cdd:cd14880 540 RAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVE 619
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2462545116 411 RYGILMTKQELSFSDKKEVCKVVLHrliqdSNQYQFGKTKIF 452
Cdd:cd14880 620 RYKLLRRLRPHTSSGPHSPYPAKGL-----SEPVHCGRTKVF 656
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
3-454 |
4.81e-77 |
|
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: 269.96 E-value: 4.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14921 215 GFVPIPAAQDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDF 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFE 161
Cdd:cd14921 295 TRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQK 237
Cdd:cd14921 375 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEK 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 238 LYNNFVNrNPLFEKPRM--SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQE-NPTPPSPFG 314
Cdd:cd14921 455 LCTEQGN-HPKFQKPKQlkDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvDRIVGLDQM 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 315 SMITVKSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRI 394
Cdd:cd14921 534 AKMTESSLPSASKTKKGMFR-TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRI 612
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 395 SAQSYPSRWTYIEFYSRYGILMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14921 613 CRQGFPNRIVFQEFRQRYEILAANAiPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
2-454 |
2.00e-76 |
|
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: 267.30 E-value: 2.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI----TAVGNERSSVSEDDSHLKVFCELLGL 77
Cdd:cd14891 228 SGCVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGV 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 78 ESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFD- 156
Cdd:cd14891 308 DEEALEKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEt 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 157 VNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWL 235
Cdd:cd14891 388 KNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLN 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 236 QKLYNNFvNRNPLF--EKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfhlcanffqenptppspf 313
Cdd:cd14891 468 ETLHKTH-KRHPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA------------------ 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 314 gsmitvksakqvikpnskhfrttvgsKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIR 393
Cdd:cd14891 529 --------------------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCE 582
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 394 ISAQSYPSRWTYIEFYSRYGILMTKQELSF--SDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14891 583 VLKVGLPTRVTYAELVDVYKPVLPPSVTRLfaENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
12-454 |
8.55e-76 |
|
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: 266.19 E-value: 8.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 12 DRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKI 91
Cdd:cd14930 223 ERELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRI 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 92 VTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANE 170
Cdd:cd14930 303 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 171 KLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRN 246
Cdd:cd14930 383 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE-QGGH 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 247 PLFEKPR--MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpFGSMITVKSAKQ 324
Cdd:cd14930 462 PKFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVG-LEQVSSLGDGPP 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 325 VIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWT 404
Cdd:cd14930 541 GGRPRRGMFR-TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRIL 619
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 405 YIEFYSRYGILMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14930 620 FQEFRQRYEILTPNAiPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
3-454 |
8.83e-76 |
|
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: 266.55 E-value: 8.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd15896 219 GNVTIPGQQDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDF 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFE 161
Cdd:cd15896 299 TRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIE---AKMGILELLDEECLLPHGTDENWLQK 237
Cdd:cd15896 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 238 LYNNfVNRNPLFEKPR--MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSpFGS 315
Cdd:cd15896 459 VLQE-QGTHPKFFKPKklKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVG-LDK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 316 MITVKSAKQVIKPNSKHFRtTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRIS 395
Cdd:cd15896 537 VSGMSEMPGAFKTRKGMFR-TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIC 615
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 396 AQSYPSRWTYIEFYSRYGILMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd15896 616 RQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
25-415 |
1.24e-75 |
|
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: 264.86 E-value: 1.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 25 LLGFKEDFQMDVFKILAAILHLGNVQItAVGNERSSVSEDDSHLKVFCE--------LLGLESGRVAQWLCNRKIVTSSE 96
Cdd:cd14900 230 IIGFTPHERAGIFDLLAALLHIGNLTF-EHDENSDRLGQLKSDLAPSSIwsrdaaatLLSVDATKLEKALSVRRIRAGTD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 97 TVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF--SGKQHT---FIGVLDIYGFETFDVNSFEQFCINYANEK 171
Cdd:cd14900 309 FVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddSSKSHGglhFIGILDIFGFEVFPKNSFEQLCINFANET 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 172 LQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFE 250
Cdd:cd14900 389 LQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLASKLYRACGS-HPRFS 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 251 KPRMSNTS--FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfhlcanffqenptppspfgsmitvksakqvikp 328
Cdd:cd14900 468 ASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY----------------------------------- 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 329 nskhfrttvGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEF 408
Cdd:cd14900 513 ---------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEF 583
|
....*..
gi 2462545116 409 YSRYGIL 415
Cdd:cd14900 584 VARYFSL 590
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
3-454 |
4.49e-75 |
|
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: 264.26 E-value: 4.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 3 GNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRV 82
Cdd:cd14919 212 GHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDF 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 83 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFE 161
Cdd:cd14919 292 TRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQK 237
Cdd:cd14919 372 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 238 LYNNfVNRNPLFEKPRM--SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptpPSPFGS 315
Cdd:cd14919 452 VVQE-QGTHPKFQKPKQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD----VDRIIG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 316 MITVKSAKQVIKPNSKHFRT----TVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLET 391
Cdd:cd14919 527 LDQVAGMSETALPGAFKTRKgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 606
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 392 IRISAQSYPSRWTYIEFYSRYGILMTKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14919 607 IRICRQGFPNRVVFQEFRQRYEILTPNSiPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
10-454 |
2.36e-73 |
|
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: 260.21 E-value: 2.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 10 VNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVS---EDDSHLKVFCELLGLESGRVAQWL 86
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvtaASRFHLAKCAELMGVDVDKLETLL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 87 CNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTF---------IGVLDIYGFETFDV 157
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNR 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 158 NSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQ 236
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALST 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 237 KLYNNFVNRNplfekprmsntSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCAnFFQENPTPPSPfgsm 316
Cdd:cd14902 478 KFYRYHGGLG-----------QFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV-AIGADENRDSP---- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 317 iTVKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISA 396
Cdd:cd14902 542 -GADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIAR 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 397 QSYPSRWTYIEFYSRYGILMTKQELSFSDKK-------------EVCKVVLHRLIQDSNQ-------------------- 443
Cdd:cd14902 621 HGYSVRLAHASFIELFSGFKCFLSTRDRAAKmnnhdlaqalvtvLMDRVLLEDGVEREEKnpgaltavtgdgsgtafend 700
|
490
....*....|....*.
gi 2462545116 444 -----YQFGKTKIFFR 454
Cdd:cd14902 701 crrkdVQVGRTLVFCK 716
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
35-447 |
5.53e-73 |
|
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: 259.14 E-value: 5.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 35 DVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVF---CELLGLESGRVAQWLCNRKIVTSSETVV--KPMTRPQAVN 109
Cdd:cd14906 269 AIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIESVFKQALLNRNLKAGGRGSVycRPMEVAQSEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 110 ARDALAKKIYAHLFDFIVERINQ-----------ALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 178
Cdd:cd14906 349 TRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 179 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPrMSNT 257
Cdd:cd14906 429 NVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKGSEQSLLEKYNKQYHNTNQYYQRT-LAKG 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 258 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPTPPSPfgsmiTVKSAKQVIkpnskhfrtTV 337
Cdd:cd14906 508 TLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITSTTN-----TTKKQTQSN---------TV 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 338 GSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT 417
Cdd:cd14906 574 SGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVD 653
|
410 420 430
....*....|....*....|....*....|
gi 2462545116 418 KQELSfSDKKEVCKVVLHRLIQDSNQYQFG 447
Cdd:cd14906 654 MYNRK-NNNNPKLASQLILQNIQSKLKTMG 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
7-504 |
6.13e-72 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 258.42 E-value: 6.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 7 IEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITavGNERSSVSE----DDSHLKVF---CELLGLES 79
Cdd:PTZ00014 322 VPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDaaaiSDESLEVFneaCELLFLDY 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 80 GRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNS 159
Cdd:PTZ00014 400 ESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNS 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 160 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKL 238
Cdd:PTZ00014 480 LEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSC 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 239 YNNFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQenptppspfGSMIT 318
Cdd:PTZ00014 560 NTNLKNNPKYKPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE---------GVEVE 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 319 V-KSAK-QVIkpnskhfrttvGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISA 396
Cdd:PTZ00014 631 KgKLAKgQLI-----------GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQ 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 397 QSYPSRWTYIEFYSRYGIL-MTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR---AGQVAYLEKLRLDKLRQS 472
Cdd:PTZ00014 700 LGFSYRRTFAEFLSQFKYLdLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPL 779
|
490 500 510
....*....|....*....|....*....|..
gi 2462545116 473 CVMVQKHMRGWLQRKKFLRERRAALIIQQYFR 504
Cdd:PTZ00014 780 VSVLEALILKIKKKRKVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
2-454 |
1.68e-70 |
|
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: 250.08 E-value: 1.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSE--DDSHLKVFCELLGLES 79
Cdd:cd14896 206 GGACRLQGKEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAvsSWAEIHTAARLLQVPP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 80 GRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTF--IGVLDIYGFETFDV 157
Cdd:cd14896 286 ERLEGAVTHRVTETPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRV 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 158 NSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQ 236
Cdd:cd14896 366 NGLEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIPQPPRESCLDLLVDQpHSLLSILDDQTWLSQATDHTFLQ 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 237 KLYNNFVNrNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsm 316
Cdd:cd14896 446 KCHYHHGD-HPSYAKPQLPLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE----------- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 317 itvKSAKQVIKPNskhfRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISA 396
Cdd:cd14896 514 ---AEPQYGLGQG----KPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRS 586
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 397 QSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14896 587 EGFPVRVPFQAFLARFGALGSERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
7-452 |
3.25e-70 |
|
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: 249.52 E-value: 3.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 7 IEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITA-----VGNERSSVSEDDSHLKVFCELLGLESGR 81
Cdd:cd14876 213 VPGIDDVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGkteqgVDDAAAISNESLEVFKEACSLLFLDPEA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 82 VAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFE 161
Cdd:cd14876 293 LKRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTDENWLQKLYN 240
Cdd:cd14876 373 QLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVS 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 241 NFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENPtppspfgsMITVK 320
Cdd:cd14876 453 KLKSNGKFKPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVV--------VEKGK 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 321 SAK-QVIkpnskhfrttvGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSY 399
Cdd:cd14876 525 IAKgSLI-----------GSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGY 593
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 400 PSRWTYIEFYSRYGIL-MTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIF 452
Cdd:cd14876 594 SYRRPFEEFLYQFKFLdLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1082-1408 |
5.05e-69 |
|
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo.
Pssm-ID: 271253 [Multi-domain] Cd Length: 288 Bit Score: 233.83 E-value: 5.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1082 EDEAKLIQNLILDLKPRGVVVnmiPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1161
Cdd:cd14945 1 SEEDSLLRGIVTDFEPSSGDH---KLTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1162 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1241
Cdd:cd14945 78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1242 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1321
Cdd:cd14945 140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1322 NISYLEEWLKDKNLqNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1401
Cdd:cd14945 202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280
|
....*..
gi 2462545116 1402 RKVQALL 1408
Cdd:cd14945 281 RTLAAEV 287
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
7-454 |
3.25e-68 |
|
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: 243.64 E-value: 3.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 7 IEGVNDRAEMVETQKTFTLLGFKEDFQmDVFKILAAILHLGNVQ---ITAVGNERSSVSEDDSHLKVFCELLGLESGRVA 83
Cdd:cd14886 218 APGIDDQKEFAPVRSQLEKLFSKNEID-SFYKCISGILLAGNIEfseEGDMGVINAAKISNDEDFGKMCELLGIESSKAA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 84 QWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQF 163
Cdd:cd14886 297 QAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 164 CINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLPHGTDENWLQKLYNNF 242
Cdd:cd14886 377 LINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSCKSKI 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 243 vnRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHlcanffqenptppspfgsmITVKSA 322
Cdd:cd14886 457 --KNNSFIPGKGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNP-------------------IVNKAF 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 323 KQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSR 402
Cdd:cd14886 516 SDIPNEDGNMKGKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYN 595
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 403 WTYIEFYSRYGILMTKQELSF---SDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14886 596 DTFEEFFHRNKILISHNSSSQnagEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
8-412 |
1.03e-62 |
|
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: 228.83 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 8 EGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNER------------SSVSEDDSHLKVFCELL 75
Cdd:cd14899 248 DGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfadearvmSSTTGAFDHFTKAAELL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 76 GLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGK---------------Q 140
Cdd:cd14899 328 GVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesdvddeedA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 141 HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILEL 219
Cdd:cd14899 408 TDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRpIGIFSL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 220 LDEECLLPHGTDENWLQKLYNNFVNR--NPLFEKPRM--SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK 295
Cdd:cd14899 488 TDQECVFPQGTDRALVAKYYLEFEKKnsHPHFRSAPLiqRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQLLAGSS 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 296 FHLCANFFQENPTPPSPFGSMITVKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFD 375
Cdd:cd14899 568 NPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQ 647
|
410 420 430
....*....|....*....|....*....|....*..
gi 2462545116 376 SKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 412
Cdd:cd14899 648 STRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
2-454 |
2.27e-59 |
|
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: 217.76 E-value: 2.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVI------EGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVsEDDSHLKVFCELL 75
Cdd:cd14875 220 GGNTFVrrgvdgKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQI-ADETPFLTACRLL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 76 GLESGRVAQWLcnrkIVTSSETVVKPMTRPQ-AVNARDALAKKIYAHLFDFIVERINQAL--QFSGKQHTFIGVLDIYGF 152
Cdd:cd14875 299 QLDPAKLRECF----LVKSKTSLVTILANKTeAEGFRNAFCKAIYVGLFDRLVEFVNASItpQGDCSGCKYIGLLDIFGF 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 153 ETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTD 231
Cdd:cd14875 375 ENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTT 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 232 ENWLQKLYNNFVNRNPLFEKPRMS-NTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfhlcANFFQenptpp 310
Cdd:cd14875 455 ERFTTNLWDQWANKSPYFVLPKSTiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNST----DEFIR------ 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 311 spfgsmiTVKSAKQVikpnSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLE 390
Cdd:cd14875 525 -------TLLSTEKG----LARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQ 593
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 391 TIRISAQSYPSRWTYIEFYSRYGILMTKQELSF---SDKKEVCKVVLHRLIQ----DSNQYQFGKTKIFFR 454
Cdd:cd14875 594 TIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLfkqEKYSEAAKDFLAYYQRlygwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
34-453 |
6.88e-56 |
|
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: 206.50 E-value: 6.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 34 MDVFKILAAILHLGNVQITAvGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDA 113
Cdd:cd14881 232 LDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNMTRDA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 114 LAKKIYAHLFDFIVERINQALQFSGKQHT-----FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 188
Cdd:cd14881 311 LAKALYCRTVATIVRRANSLKRLGSTLGThatdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESC 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 189 MKEDIPWTL-IDFYDNQPVIDLIEA-KMGILELLDEECLlPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFAD 266
Cdd:cd14881 391 RDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIRHFAG 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 267 KVEYKCEGFLEKNRDTVYDMLVEILRAskfHLCAnffqenptppspFGsmitvksakqvikpnskhFRTTVgSKFRSSLY 346
Cdd:cd14881 470 RVVYDASDFLDTNRDVVPDDLVAVFYK---QNCN------------FG------------------FATHT-QDFHTRLD 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 347 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDK 426
Cdd:cd14881 516 NLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEE 595
|
410 420 430
....*....|....*....|....*....|....*..
gi 2462545116 427 KEV--CKVVL-----HRLIQDSN---QYQFGKTKIFF 453
Cdd:cd14881 596 KALedCALILqfleaQPPSKLSSvstSWALGKRHIFL 632
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
40-415 |
5.56e-55 |
|
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: 202.44 E-value: 5.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 40 LAAILHLGNVQITavgNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIY 119
Cdd:cd14898 228 LLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSMARLLY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 120 AHLFDFIVERINQALQFSGKQHtfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLID 199
Cdd:cd14898 305 SNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 200 FYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL--YNN-FVNRNplfekprmSNTSFVIQHFADKVEYKCEGFL 276
Cdd:cd14898 383 FFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNgFINTK--------ARDKIKVSHYAGDVEYDLRDFL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 277 EKNRDtvydmlveilrasKFHLcanffqenptppSPFGSMITVKSAKqvikpnskhfRTTVGSKFRSSLYLLMETLNATT 356
Cdd:cd14898 455 DKNRE-------------KGQL------------LIFKNLLINDEGS----------KEDLVKYFKDSMNKLLNSINETQ 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 357 PHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL 415
Cdd:cd14898 500 AKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
9-453 |
5.20e-53 |
|
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: 198.16 E-value: 5.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 9 GVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQIT--AVGNERSSVSEDDSHLKVFCELLGLESGRVAQWL 86
Cdd:cd14879 230 GSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 87 CNR-KIVtSSE--TVvkpMTRP-QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFD---VN 158
Cdd:cd14879 310 TYKtKLV-RKElcTV---FLDPeGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDfATFISLLDFPGFQNRSstgGN 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 159 SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMG--ILELLDEECLLPHGTDENWLQ 236
Cdd:cd14879 386 SLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGglLGILDDQTRRMPKKTDEQMLE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 237 KLYNNFVNRNPLFEKPRMSNTS----FVIQHFADKVEYKCEGFLEKNRDtvydmlveilraskfHLCANFfqenptppsp 312
Cdd:cd14879 466 ALRKRFGNHSSFIAVGNFATRSgsasFTVNHYAGEVTYSVEGFLERNGD---------------VLSPDF---------- 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 313 fgsMITVKSAKQvikpnskhfrttvgskFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETI 392
Cdd:cd14879 521 ---VNLLRGATQ----------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELA 581
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 393 RISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKevckvVLHRLIQDSNQYQFGKTKIFF 453
Cdd:cd14879 582 ARLRVEYVVSLEHAEFCERYKSTLRGSAAERIRQC-----ARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
8-454 |
1.31e-46 |
|
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: 180.23 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 8 EGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQIT----------------AVGNE-----RSSVSE--- 63
Cdd:cd14887 209 EGDPESTDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTtdqepetskkrkltsvSVGCEetaadRSHSSEvkc 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 64 ----------DDSHLKVFCELLGLESGRVAQWLCNRKIVTSS--ETVvKPMTRPQAVNARDALAKKIYAHLFDFIVERIN 131
Cdd:cd14887 289 lssglkvteaSRKHLKTVARLLGLPPGVEGEEMLRLALVSRSvrETR-SFFDLDGAAAARDAACKNLYSRAFDAVVARIN 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 132 QALQFSGK--------------QHTFIGVLDIYGFETF---DVNSFEQFCINYANEKLqqqfnmHVFKLEQ----EE--Y 188
Cdd:cd14887 368 AGLQRSAKpsesdsdedtpsttGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERL------HCFLLEQlilnEHmlY 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 189 MKEDIPWTLIDFYDNQP-------------VIDLI-EAKMGILELLDEECLLPHG----------TDENW---------- 234
Cdd:cd14887 442 TQEGVFQNQDCSAFPFSfplastltsspssTSPFSpTPSFRSSSAFATSPSLPSSlsslssslssSPPVWegrdnsdlfy 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 235 --LQKLYNNFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAskfhlCANFFQENPTPPSP 312
Cdd:cd14887 522 ekLNKNIINSAKYKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA-----CSTYTRLVGSKKNS 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 313 FGSMITVKsakqvikpnskhfRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETI 392
Cdd:cd14887 597 GVRAISSR-------------RSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLL 663
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 393 RISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 454
Cdd:cd14887 664 RVMADGFPCRLPYVELWRRYETKLPMALREALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
12-454 |
4.60e-45 |
|
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: 174.62 E-value: 4.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 12 DRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKI 91
Cdd:cd14878 224 NREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 92 VTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQ----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINY 167
Cdd:cd14878 304 YFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNM 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 168 ANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQP-VIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYN----- 240
Cdd:cd14878 384 TNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTgVLDFFFQKpSGFLSLLDEESQMIWSVEPNLPKKLQSlless 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 241 --NFV-------NRNPlfeKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQenptpps 311
Cdd:cd14878 464 ntNAVyspmkdgNGNV---ALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ------- 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 312 pfgsmitvksakqvikpnSKhfRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLET 391
Cdd:cd14878 534 ------------------SK--LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEM 593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 392 IRISAQSYPSRWTYIEFYSRYG-----ILMTKQELSfsdKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 454
Cdd:cd14878 594 VKIFRYGYPVRLSFSDFLSRYKpladtLLGEKKKQS---AEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
18-454 |
7.43e-45 |
|
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: 173.77 E-value: 7.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 18 ETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQItaVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSET 97
Cdd:cd14882 231 EFEEILKDLDFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 98 VVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQ 173
Cdd:cd14882 309 ERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPravfGDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 174 QQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKmgilelldeecllPHG----TDENWLQKLYNNFV------ 243
Cdd:cd14882 388 YHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTK-------------PDGlfyiIDDASRSCQDQNYImdrike 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 244 NRNPlFEKPrMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASkfhlcanffqenptppspfgsmiTVKSAK 323
Cdd:cd14882 455 KHSQ-FVKK-HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSS-----------------------LDESVK 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 324 QVIKPNSKHFRTTVGSKFRSSLYLLMETL----NATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSY 399
Cdd:cd14882 510 LMFTNSQVRNMRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGF 589
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 400 PSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 454
Cdd:cd14882 590 SYRIPFQEFLRRYQFLAFDFDETVEMTKDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
4-454 |
1.74e-44 |
|
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: 172.51 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 4 NTVIEGVNDRAEMVETQKTFTLLGFkEDFQMDVFKILAAILHLGNVQITAV-GNERSSVSE-DDSHLKVFCE---LLGLE 78
Cdd:cd14937 203 NVVIPEIDDAKDFGNLMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQEIeKGGKTNCSElDKNNLELVNEisnLLGIN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 79 SGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVN 158
Cdd:cd14937 282 YENLKDCLVFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 159 SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL 238
Cdd:cd14937 362 SLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVY 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 239 YNNFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQEnptppspfgsmit 318
Cdd:cd14937 442 TNKFSKHEKYASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED------------- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 319 VKSAKQVIKPNSKHFrttvgsKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAqS 398
Cdd:cd14937 509 VEVSESLGRKNLITF------KYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISF-F 581
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 399 YPSRWTYIEFYSRYGIL--MTKQELSFSDKKEVCKVVLHRLiqDSNQYQFGKTKIFFR 454
Cdd:cd14937 582 FQYKYTFDVFLSYFEYLdySTSKDSSLTDKEKVSMILQNTV--DPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
26-454 |
3.79e-42 |
|
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: 165.04 E-value: 3.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 26 LGFKEDFQMDVFKILAAILHLGNVQITAVGNerSSVSED------DSHLKVFCELLGLEsgrVAQWLcnrKIVTSSETVV 99
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTKRN--PNVEQDvveignMSEVKWVAFLLEVD---FDQLV---NFLLPKSEDG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 100 KPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSgKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMH 179
Cdd:cd14874 291 TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCP-LHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKH 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 180 VFKLEQEEYMKEDIPwtlIDF-----YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR 253
Cdd:cd14874 370 SFHDQLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 254 MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHLCANFFQENptppSPFGSMITVKSAKQVIKpnskhf 333
Cdd:cd14874 447 KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY----SSNTSDMIVSQAQFILR------ 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 334 rttvGSKfrsslyLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYG 413
Cdd:cd14874 517 ----GAQ------EIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYR 586
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2462545116 414 ILMTKQELSFSDKKEVCKVVLH-RLIQDSNQYQFGKTKIFFR 454
Cdd:cd14874 587 CLLPGDIAMCQNEKEIIQDILQgQGVKYENDFKIGTEYVFLR 628
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
2-454 |
9.26e-39 |
|
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: 155.64 E-value: 9.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 2 GGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAvGNERSSVsEDDSHLKVFCELLGLESGR 81
Cdd:cd14905 206 GGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQ-KNGKTEV-KDRTLIESLSHNITFDSTK 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 82 VAQWLCNRKIVTSSEtvvkpmtrpqAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTfIGVLDIYGFETFDVNSFE 161
Cdd:cd14905 284 LENILISDRSMPVNE----------AVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPW-TLIDFYDNQPVIDLIEAKMGILELLDEECllpHGTDENWLQKLyN 240
Cdd:cd14905 353 QFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDNEESVEMMEKIINLLDQESKNI---NSSDQIFLEKL-Q 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 241 NFVNRNPLF-EKPrmsnTSFVIQHFADKVEYKCEGFLEKNRDTVY--------DMLVEIL--RASKFHLCAN-------F 302
Cdd:cd14905 429 NFLSRHHLFgKKP----NKFGIEHYFGQFYYDVRGFIIKNRDEILqrtnvlhkNSITKYLfsRDGVFNINATvaelnqmF 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 303 FQENPTPPSPFgSMITV------KSAKQVIKPNSKH------FRTTVGSKFRSSLYLLMETLNATTP------HYVRCIK 364
Cdd:cd14905 505 DAKNTAKKSPL-SIVKVllscgsNNPNNVNNPNNNSggggggGNSGGGSGSGGSTYTTYSSTNKAINnsncdfHFIRCIK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 365 PNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQElSFSDKKEvcKVVLHRLIQDS--- 441
Cdd:cd14905 584 PNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQR-NFQNLFE--KLKENDINIDSilp 660
|
490
....*....|...
gi 2462545116 442 NQYQFGKTKIFFR 454
Cdd:cd14905 661 PPIQVGNTKIFLR 673
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
12-445 |
2.52e-37 |
|
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: 151.21 E-value: 2.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 12 DRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNvqitavgnerssvseddSHLKVFCELLGLESGRVAQWLCNRKI 91
Cdd:cd14884 255 DEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN-----------------RAYKAAAECLQIEEEDLENVIKYKNI 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 92 VTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL------------QFSGKQHTFIGVLDIYGFETFDVNS 159
Cdd:cd14884 318 RVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAIISILDIYGFEELSGND 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 160 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHG-TDENWLQKL 238
Cdd:cd14884 398 FDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITKLKNQGQKkTDDHFFRYL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 239 YNN-------------FVN---RNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFHlcanF 302
Cdd:cd14884 478 LNNerqqqlegkvsygFVLnhdADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNR----F 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 303 FQENptppspfgsmitvksakqVIKPNSKHFrTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQ 382
Cdd:cd14884 554 LREA------------------NNGGNKGNF-LSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQ 614
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 383 LRACGVLETIRISAQSYPSRwtyiefysrygilMTKQELSFSDKKEVCKVVLHRLIQDSNQYQ 445
Cdd:cd14884 615 LKQCGSNEMIKILNRGLSHK-------------IPKKETAAALKEQIAKELEKCNSNTDIEYQ 664
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1287-1388 |
1.26e-33 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 125.40 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1287 QAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWLKDKNLQnSLAKETLEPLSQAAWLLQVKKTTDSDAKE 1366
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGLE-SEARDHLAPLIQAAQLLQLRKSTLEDLDS 79
|
90 100
....*....|....*....|..
gi 2462545116 1367 IYERCTSLSAVQIIKILNSYTP 1388
Cdd:pfam01843 80 ILQVCPALNPLQLHRLLTLYQP 101
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
14-454 |
3.39e-26 |
|
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: 116.26 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 14 AEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLE-------------SG 80
Cdd:cd01386 221 AAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTleelssaifkhhlSG 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 81 RVAQWLCNRkivTSSETVVKPMTRPQ--AVNARDALAKKIYAHLFDFIVERINQALqfSGKQHTF--IGVLDIYGFEtfd 156
Cdd:cd01386 301 GPQQSTTSS---GQESPARSSSGGPKltGVEALEGFAAGLYSELFAAVVSLINRSL--SSSHHSTssITIVDTPGFQ--- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 157 vN----------SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDN-QPVIDLI--------------- 210
Cdd:cd01386 373 -NpahsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIdqapqqalvrsdlrd 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 211 EAKMGILELLDEECLLPHGTDENWLQKLYNNF----VNRNPLFEKPRMSNTSFVIQHF--ADKVEYKCEGFLeknrdtvy 284
Cdd:cd01386 452 EDRRGLLWLLDEEALYPGSSDDTFLERLFSHYgdkeGGKGHSLLRRSEGPLQFVLGHLlgTNPVEYDVSGWL-------- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 285 dmlveilRASKfhlcanffqENPTPpspfgsmitvKSAKQVIKPNSKHF----RTTVGSKFRSSLYLLMETLNATTPHYV 360
Cdd:cd01386 524 -------KAAK---------ENPSA----------QNATQLLQESQKETaavkRKSPCLQIKFQVDALIDTLRRTGLHFV 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 361 RCIKPN------DEKLPFEFDSKRIVQ------QLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKE 428
Cdd:cd01386 578 HCLLPQhnagkdERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSE 657
|
490 500 510
....*....|....*....|....*....|..
gi 2462545116 429 VC--KVVLHRLIQ----DSNQYQFGKTKIFFR 454
Cdd:cd01386 658 VAdeRKAVEELLEeldlEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
22-412 |
5.10e-25 |
|
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: 112.76 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 22 TFTLLGFKEDFQMDVFKILAAILHLGNVQI---------------TAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWL 86
Cdd:cd14893 252 SFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDPAQILLAAKLLEVEPVVLDNYF 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 87 CNRKIVT--SSETV--VKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-----QFSGK----QHTFIGVLDIYGFE 153
Cdd:cd14893 332 RTRQFFSkdGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSniviNSQGVHVLDMVGFE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 154 TFD--VNSFEQFCINYANEK-----LQQQFNMHVFKLEQEEYMKED--IPWTLIDF-YDNQPVIDLIEAK-MGILELLDE 222
Cdd:cd14893 412 NLTpsQNSFDQLCFNYWSEKvhhfyVQNTLAINFSFLEDESQQVENrlTVNSNVDItSEQEKCLQLFEDKpFGIFDLLTE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 223 ECLLPHGTDENWLQKLYN-------------NFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVE 289
Cdd:cd14893 492 NCKVRLPNDEDFVNKLFSgneavgglsrpnmGADTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKNMLSISSTCAA 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 290 ILRASKFHLCanffqeNPTPPSPFGSMITVKSAKQVIKPNSKH--FRTTVGSKFRSS---------LY----LLMETLNA 354
Cdd:cd14893 572 IMQSSKNAVL------HAVGAAQMAAASSEKAAKQTEERGSTSskFRKSASSARESKnitdsaatdVYnqadALLHALNH 645
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 355 TTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 412
Cdd:cd14893 646 TGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1082-1442 |
4.85e-24 |
|
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown.
Pssm-ID: 271257 [Multi-domain] Cd Length: 316 Bit Score: 104.56 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1082 EDEAKLIQNLILDLKPRGVVVNMIPgLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1161
Cdd:cd15473 7 EDELPRILDLLITNMTPQRSPSQRP-VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1162 C---HFLNCLKQYsgeeefmkhnspqqnknclnNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLqgi 1238
Cdd:cd15473 86 TlllHYLKKDAGL--------------------VEATPEFQQELAELINEIFVLIIRDAERRIDKLLDASPRNITSL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1239 sglkptgfrkrsssiddtdgytMTSVLQQLSYFYttmcqngLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQ 1318
Cdd:cd15473 143 ----------------------LSSTLYVLELYD-------VHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1319 IRCNISYLEEWLKDKNLQ-------NSLAKETLEPLSQAAWLLQVKKT-TDSDA-KEIYERCTSLSAVQIIKILNSYTPi 1389
Cdd:cd15473 194 IRMNLSALEDWARSNNLQpekgespPRIARSHLAPVIQLLQWLQCLSSlDDFESlIATIQQLDALNPLQLLRAVKDYRY- 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 1390 DDFEKRVTPSFVRKVQALLNSRedssqlmLDTKYLFQVTFPFTPsphalEMIQ 1442
Cdd:cd15473 273 EVNEGRMPEECVKYLAQLQKDW-------LDSRYMLPFSLPTDT-----EMLV 313
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1109-1419 |
3.62e-23 |
|
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271264 Cd Length: 363 Bit Score: 103.04 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1109 PAHILFMCvryadsLNDanMLK--------SLMNSTINGIKQVVKEhLEDFEMLS---FWLSNTcHFLNCLKQYSgEEEF 1177
Cdd:cd15480 48 PAHLIILI------LSE--MWRlgltkeseRFLANVMQTIQQHVMS-LKGEDAIVpgaFWLSNV-HELLSFVCLA-ESDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1178 MKHNSPqqnKNCLNNFDLSEYRQILSDV-------AIRIYHQFIIIMEKNIQPiivpgmleyeslqgisglkptgfrkrs 1250
Cdd:cd15480 117 LQGIGP---GKDMREEEWEEYERLVTVVkhdleslEYNIYHTWMKELKKRLEK--------------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1251 ssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWL 1330
Cdd:cd15480 167 ---------TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1331 K-----DKNLQnslaketLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTpIDDFEKRVTPSFVRKVQ 1405
Cdd:cd15480 238 KshdipEGTLQ-------LEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVA 309
|
330
....*....|....
gi 2462545116 1406 ALLNSREDSSQLML 1419
Cdd:cd15480 310 ARVKPEDKSDHLLL 323
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1109-1407 |
6.67e-22 |
|
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271258 Cd Length: 352 Bit Score: 99.03 E-value: 6.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1109 PAHILFMCV---RYADSLNDANMLKSLmNSTINGIKQVVKEHLEDFEMLS--FWLSNTcH----FLNCLKQ---YSGEEE 1176
Cdd:cd15474 34 LGHVNFLIYsqmWKSLLELLTQSERFL-SHVLSYIASIVDSLPKKETIPDgaFWLANL-HelrsFVVYLLSlieHSSSDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1177 FMKHNSPQQNKNclnnfdLSEYRQILSdvaiRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISGlkptgFRKRSSSIDDT 1256
Cdd:cd15474 112 FSKESEEYWNTL------FDKTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDLSE-----LIDLNKEFFNK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1257 DGYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWLKDKNLq 1336
Cdd:cd15474 177 PKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQISYNVSRLKEWCHQHGL- 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 1337 nSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPiDDFEKRVTPSFVRKVQAL 1407
Cdd:cd15474 256 -SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQP-ANYEAPVPKEFLNALEKL 324
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
26-416 |
8.18e-21 |
|
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: 99.43 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 26 LGFKEDFQMDVFKILAAILHLGNVQIT--AVGNE--RSSVSEDDSHLKVfCELLGLESGRVAQWLCNRKIVT---SSETV 98
Cdd:cd14894 393 LNVSPDEQKTIFKVLSAVLWLGNIELDyrEVSGKlvMSSTGALNAPQKV-VELLELGSVEKLERMLMTKSVSlqsTSETF 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 99 VKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFS-----GKQH------------TFIGVLDIYGFETFDVNSFE 161
Cdd:cd14894 472 EVTLEKGQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSalstdGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 162 QFCINYANEKLQQqfnmhvfKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQ----- 236
Cdd:cd14894 552 QLCINYLSEKLYA-------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQeekrn 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 237 KLY-NNFVNRNP--LFEKPR-MSNTS-----------FVIQHFADKVEYKCEGFLEKNRDTVY-DMLVEILRASKFHLCA 300
Cdd:cd14894 625 KLFvRNIYDRNSsrLPEPPRvLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYaNLLVGLKTSNSSHFCR 704
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 301 NFFQENPTPPSPFGSMITVKSAKQVIKpNSKHFrttVGsKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIV 380
Cdd:cd14894 705 MLNESSQLGWSPNTNRSMLGSAESRLS-GTKSF---VG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVE 779
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2462545116 381 QQLRACGV---LETIRISAQSYPS-RWTYIEFYSRYGILM 416
Cdd:cd14894 780 QQCRSQRLirqMEICRNSSSSYSAiDISKSTLLTRYGSLL 819
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
599-1069 |
1.76e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 92.04 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAV---EEKLAKLQ 675
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 676 KHNSELETQKEQIQ----------------------LKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSfELKTQ 733
Cdd:TIGR02168 400 NEIERLEARLERLEdrrerlqqeieellkkleeaelKELQAELEELEEELEELQEELERLEEALEELREELEEA-EQALD 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 734 DYEKQIQSLKEEIKALKDekMQLQHLVEGEHVT-----SDGLKAEVARLSKQVKTISEFEKEIEL-------------LQ 795
Cdd:TIGR02168 479 AAERELAQLQARLDSLER--LQENLEGFSEGVKallknQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavvvenLN 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 796 AQKIDVE--------------------KHVQSQKREMREKMSEITKQL--LESYDIE---DVRSRLS----VEDLEHLNE 846
Cdd:TIGR02168 557 AAKKAIAflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAkdLVKFDPKlrkALSYLLGgvlvVDDLDNALE 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 847 --------------DGEL----WFAYEGLKKATRVLESHFQSQKDCyEKEIEALNFKVVHLSQEINHLQKLFREendINE 908
Cdd:TIGR02168 637 lakklrpgyrivtlDGDLvrpgGVITGGSAKTNSSILERRREIEEL-EEKIEELEEKIAELEKALAELRKELEE---LEE 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 909 SIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLnEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAqneihtkEK 988
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI-AQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EI 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 989 EKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSS 1068
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
.
gi 2462545116 1069 G 1069
Cdd:TIGR02168 865 E 865
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
526-1096 |
5.00e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 87.48 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 526 IIQKHCRGYLVRSLYQLIRMATITMQAYSRGFLARRRYRKMLEE-HKAVILqkyARAWLARRRFQSIRRFVLNIQLTYRV 604
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVL---ANSELTEARTERDQFSQESGNLDDQL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 605 QRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKaathrRNYEekgkryrdaVEEKLAKLQKHNSELETQ 684
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD-----RNME---------VQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 685 KEQIQLKLQEKTEELkEKMDNLTKQLFDD-------VQKEERQRMLLEKS------FELKTQDYEKQIQSLKEEIKALK- 750
Cdd:pfam15921 446 MERQMAAIQGKNESL-EKVSSLTAQLESTkemlrkvVEELTAKKMTLESSertvsdLTASLQEKERAIEATNAEITKLRs 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 751 --DEKMQ-LQHL-VEGEHVTSDGLKAEVARLSkqvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEitKQLLES 826
Cdd:pfam15921 525 rvDLKLQeLQHLkNEGDHLRNVQTECEALKLQ-----MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE--KAQLEK 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 827 yDIEDvrSRLSVEDLEHLNEdgelwfayeglKKATRVLESHFQSQkdcyekEIEALNFKVVHLSQEINHLQKLFREEND- 905
Cdd:pfam15921 598 -EIND--RRLELQEFKILKD-----------KKDAKIRELEARVS------DLELEKVKLVNAGSERLRAVKDIKQERDq 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 906 -INE--SIRHEVTRLTSE-NMMIPDFKQQISELEKQKQDLEIRLneqaEKMKGKLEELSNQLHRSQEEEGTQRK-ALEAQ 980
Cdd:pfam15921 658 lLNEvkTSRNELNSLSEDyEVLKRNFRNKSEEMETTTNKLKMQL----KSAQSELEQTRNTLKSMEGSDGHAMKvAMGMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 981 NEIHTK--EKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1058
Cdd:pfam15921 734 KQITAKrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
570 580 590
....*....|....*....|....*....|....*...
gi 2462545116 1059 GKAndvhsSSGPKEYLGMLQYKREDEAKLIQNLILDLK 1096
Cdd:pfam15921 814 DKA-----SLQFAECQDIIQRQEQESVRLKLQHTLDVK 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
603-1057 |
1.09e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.89 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLE---AELEKAATHRRNYEEKGKRYRDaVEEKLAKLQKHNS 679
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYIKLSEFYEE-YLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 680 ELETQKEQIQLKLQE------KTEELKEKMDNLTKQ---LFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALK 750
Cdd:PRK03918 318 RLEEEINGIEERIKEleekeeRLEELKKKLKELEKRleeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 751 DEKMQLQHLVEGEHVTSDGLKAEVARLSKQV-----------------------KTISEFEKEIELLQAQKIDVEKHVQS 807
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 808 QKREMREKMSEITKQ-----LLESYD-IEDVRSRLSVEDLEHLNEDGELwfaYEGLKKATRVLESHFQSQKDCYEKeIEA 881
Cdd:PRK03918 478 LRKELRELEKVLKKEselikLKELAEqLKELEEKLKKYNLEELEKKAEE---YEKLKEKLIKLKGEIKSLKKELEK-LEE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 882 LNFKVVHLSQEINHLQKLFREENDINESIRHE-VTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQaEKMKGKLEELS 960
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-KKLEEELDKAF 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 961 NQLHRSQEEEGTQRKALEAQNEIHTKEK-EKLIDKIQEMQEASDHLKKQFETESEVkcnfRQEASRlTLEnrDLEEELDM 1039
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKR----REEIKK-TLE--KLKEELEE 705
|
490
....*....|....*...
gi 2462545116 1040 KDRVIKKLQDQVKTLSKT 1057
Cdd:PRK03918 706 REKAKKELEKLEKALERV 723
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
28-452 |
1.64e-16 |
|
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: 85.27 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 28 FKEDFQMD-VFKILAAILHLGNVQITAV---------------------------GNERSSVSEDDSHLKVFCELLGLES 79
Cdd:cd14938 254 FDDDKEIDfIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilseleNSEDIGLDENVKNLLLACKLLSFDI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 80 GRVAQWLCNRKIVTSSeTVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQ---ALQFSGKQHTFIGVLDIYGFETFD 156
Cdd:cd14938 334 ETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNININTNYINVLDMAYFENSK 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 157 VNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTL-IDFYDNQPVID-LIEAKMGILELLDEECLLPHGTDENW 234
Cdd:cd14938 413 DNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSLFSLLENVSTKTIFDKSN 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 235 LQKLYNNFVNRNPLFEKPR---MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK----FHLCANFFQENP 307
Cdd:cd14938 493 LHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEneymRQFCMFYNYDNS 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 308 TPPSPFGSMITVKSAKQVIKPNSKHFRTTVGSKFRSSLYLLMETLNATTPHYVRCIKPNDEK-LPFEFDSKRIVQQLRAC 386
Cdd:cd14938 573 GNIVEEKRRYSIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKrELCSFDANIVLRQVRNF 652
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545116 387 GVLETIRISAQSYPSRWTYIEFYSrygILMTKQElsfsDKKEVCKVVLHRLIQDSNQYQFGKTKIF 452
Cdd:cd14938 653 SIVEASQLKVGYYPHKFTLNEFLS---IFDIKNE----DLKEKVEALIKSYQISNYEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
599-1063 |
4.96e-16 |
|
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: 84.34 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 678
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 679 SELETQKEQIQLkLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEkSFELKTQDYEKQIQSLKEEIKALKDEKMQLQH 758
Cdd:TIGR02168 337 EELAELEEKLEE-LKEELESLEAELEELEAELEELESRLEELEEQLE-TLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 759 LVEGEH--VTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKqllESYDIEDVRSRL 836
Cdd:TIGR02168 415 RRERLQqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA---AERELAQLQARL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 837 -SVEDLEHLNED-----GELWFAYEGLKKATRVLESHFQSQKDcYEKEIEA-----LNFKVVHLSQE----INHLQK--- 898
Cdd:TIGR02168 492 dSLERLQENLEGfsegvKALLKNQSGLSGILGVLSELISVDEG-YEAAIEAalggrLQAVVVENLNAakkaIAFLKQnel 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 899 ---LFREENDINESIRHEVTRLTSENmmIPDFKQQISELEKQKQDLEIRLN------------EQAEKMKGKLEEL---- 959
Cdd:TIGR02168 571 grvTFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGyriv 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 960 ---------------------SNQLHRSQE--EEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVK 1016
Cdd:TIGR02168 649 tldgdlvrpggvitggsaktnSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2462545116 1017 CNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1063
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
603-1062 |
5.18e-16 |
|
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: 83.53 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 682
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 683 TQKEQIqLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFElKTQDYEKQIQSLKEEIKALKDEKMQLQHLVeg 762
Cdd:TIGR04523 114 NDKEQK-NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN-KYNDLKKQKEELENELNLLEKEKLNIQKNI-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 763 ehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLE 842
Cdd:TIGR04523 190 -----DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 843 HLNEDGELWFAYEGLKKATRVLESHFQSqkdcYEKEIEALNfkvvhlSQEINHLQKLFREE-NDINESIRHEVTRLTSEN 921
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSEISDLN------NQKEQDWNKELKSElKNQEKKLEEIQNQISQNN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 922 MMIPDFKQQISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLHRSQEEE---GTQRKALEAQNEIHTKEKEKLIDKI 995
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIknlESQINDLESKIQNQEKLNQQKDEQI 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 996 QEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAN 1062
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
603-1062 |
1.74e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEKGKRyrdaVEEKLAKLQKHNSELE 682
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 683 TQKEQIQlKLQEKTEE---LKEKMDNLTKQLFDdVQKE----ERQRMLLEKSFElKTQDYEKQIQSLKEEIKALKDEKMQ 755
Cdd:PRK03918 280 EKVKELK-ELKEKAEEyikLSEFYEEYLDELRE-IEKRlsrlEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 756 LQHLVEgEHVTSDGLKAEVARLSKQVK--TISEFEKEIELLQAQKIDVEKHVqsqkREMREKMSEITkqllesydiedvr 833
Cdd:PRK03918 357 LEERHE-LYEEAKAKKEELERLKKRLTglTPEKLEKELEELEKAKEEIEEEI----SKITARIGELK------------- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 834 srlsvedlehlNEDGELWFAYEGLKKATRVL--------ESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEnd 905
Cdd:PRK03918 419 -----------KEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 906 inESIRHEVTRLTSENMMIPDFKQQISELEK-QKQDLEiRLNEQAEKMKGKLEELSNQLhRSQEEEGTQRKALEaqneih 984
Cdd:PRK03918 486 --EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELE-KKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELK------ 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 985 tKEKEKLIDKIQEMQEASDHLKKQ-----FETESEVKCNFR--QEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKT 1057
Cdd:PRK03918 556 -KKLAELEKKLDELEEELAELLKEleelgFESVEELEERLKelEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
....*
gi 2462545116 1058 IGKAN 1062
Cdd:PRK03918 635 LAETE 639
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-1056 |
2.59e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.11 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKenhglVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 682
Cdd:PTZ00121 1303 KADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 683 TQKEQIQLKLQE--KTEELKEKMDNLTKQLfDDVQKEERQRmllEKSFELKTQDYEK----QIQSLKEEIKALKDEKMQL 756
Cdd:PTZ00121 1378 KKADAAKKKAEEkkKADEAKKKAEEDKKKA-DELKKAAAAK---KKADEAKKKAEEKkkadEAKKKAEEAKKADEAKKKA 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 757 QHLVEGEHVTSdglKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV-QSQKREMREKMSEITKQLLESYDIEDVRSR 835
Cdd:PTZ00121 1454 EEAKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 836 LSVEDLEHLNEDGELWFAYEgLKKATRVLESHFQSQKDCYEKEIEALNF---KVVHLSQ----EINHLQKLFREENDIN- 907
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMalrKAEEAKKaeeaRIEEVMKLYEEEKKMKa 1609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 908 -ESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEgtQRKALEAQNEIHTK 986
Cdd:PTZ00121 1610 eEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDE 1687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 987 EK--EKLIDKIQEMQEASDHLKK---------QFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLS 1055
Cdd:PTZ00121 1688 KKaaEALKKEAEEAKKAEELKKKeaeekkkaeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
.
gi 2462545116 1056 K 1056
Cdd:PTZ00121 1768 K 1768
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
608-1038 |
3.32e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 608 QKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR------DAVEEKLAKLQKHNSEL 681
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreelETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 682 ETQKEQIQLKLQEKTEELKEKMDNLTKQL----FDDV--------------QKEERQRMLLEKSfeLKTQDYEKQIQSLK 743
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLaeagLDDAdaeavearreeledRDEELRDRLEECR--VAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 744 EEIKALKDEKMQLQHlvEGEHVTSDGLKAEVArLSKQVKTISEFEKEIELLQAQKIDVE---KHVQSQKREMREKMSEIT 820
Cdd:PRK02224 349 EDADDLEERAEELRE--EAAELESELEEAREA-VEDRREEIEELEEEIEELRERFGDAPvdlGNAEDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 821 KQLLE-SYDIEDVRSRlsVEDLEHLNEDG---ELWFAYEGLKKATRVLEShfQSQKDCYEKEIEALNFKVVHLSQEINHL 896
Cdd:PRK02224 426 EREAElEATLRTARER--VEEAEALLEAGkcpECGQPVEGSPHVETIEED--RERVEELEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 897 QKLFREENDIN--ESIRHEVTRLTSENMMIPDFKQ-QISELEKQKQDLEirlNEQAEKmkgklEELSNQLHRSQEEEGTQ 973
Cdd:PRK02224 502 EDLVEAEDRIErlEERREDLEELIAERRETIEEKReRAEELRERAAELE---AEAEEK-----REAAAEAEEEAEEAREE 573
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 974 RKALEAQNEIHTKEKEKLiDKIQEMQEASDHLKKQFETESEVKCNF--RQEASRLTLEN-----RDLEEELD 1038
Cdd:PRK02224 574 VAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALaeLNDERRERLAEkrerkRELEAEFD 644
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
637-1000 |
3.83e-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: 77.80 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 637 EKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfdDVQK 716
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-KLKERLEELEEDLSSL------EQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 717 EERQRMLleKSFELKTQDYEKQIQSLKEEIKALKDekMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQA 796
Cdd:TIGR02169 754 ENVKSEL--KELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 797 QKIDVEKHVQSQKREMREKMSEITKQLLESY-DIEDVRSRLSvedlEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCY 875
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNgKKEELEEELE----ELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 876 EKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTrLTSENMMIPDFKQQISELEKqkqdlEIRlneqaekmkgK 955
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVEE-----EIR----------A 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2462545116 956 LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1000
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
567-959 |
7.32e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 567 LEEHKAVILQKYARAWLARRRFQSIRrfvlniQLTYRVQRLQKKLEDQNKENhgLVEKLTSLAalragdvEKIQKLEAEL 646
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAK------AKKEELERLKKRLTGLTPEK--LEKELEELE-------KAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 647 EKAATHRRNYEEKGKRYRDAVEE-KLAKLQ--KHNSEL-ETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRM 722
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEElKKAKGKcpVCGRELtEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 723 LLEKSFEL-KTQDYEKQIQSLKEEIKALKDEKM-QLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLqaqkid 800
Cdd:PRK03918 488 VLKKESELiKLKELAEQLKELEEKLKKYNLEELeKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL------ 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 801 vekhvQSQKREMREKMSEITKQLLES--YDIEDVRSRLsvEDLEhlnedgELWFAYEGLKKATRVLESHFQSQKDCYE-- 876
Cdd:PRK03918 562 -----EKKLDELEEELAELLKELEELgfESVEELEERL--KELE------PFYNEYLELKDAEKELEREEKELKKLEEel 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 877 ----KEIEALNFKVVHLSQEINHLQKLFREENdiNESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEI---RLNEQA 949
Cdd:PRK03918 629 dkafEELAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRE---LAGLRAELEELEKRREEIKKtleKLKEEL 703
|
410
....*....|
gi 2462545116 950 EKMKGKLEEL 959
Cdd:PRK03918 704 EEREKAKKEL 713
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-1050 |
9.18e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.10 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKenhglVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKR---YRDAVEEKLAKLQKHNS 679
Cdd:PTZ00121 1379 KADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeaKKKAEEAKKADEAKKKA 1453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 680 ELETQKEQIQLKLQE--KTEELKEKMDNLTKQlfDDVQKEERQRMllEKSFELKTQDYEKQiqslKEEIKALKDEKMQLQ 757
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEakKADEAKKKAEEAKKA--DEAKKKAEEAK--KKADEAKKAAEAKK----KADEAKKAEEAKKAD 1525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 758 HLVEGEhvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDV--EKHVQSQKREMREKMSEITKQLlESYDIEDVRSR 835
Cdd:PTZ00121 1526 EAKKAE----EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKKA-EEARIEEVMKL 1600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 836 LSVEDL---EHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDinesirh 912
Cdd:PTZ00121 1601 YEEEKKmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------- 1673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 913 evtrltsenmmipdfKQQISELEKQKQDLeiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLI 992
Cdd:PTZ00121 1674 ---------------KKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 993 DKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRD----LEEELDMKDRVIKKLQDQ 1050
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEkeavIEEELDEEDEKRRMEVDK 1798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
599-997 |
1.30e-12 |
|
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: 72.78 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQKKLEDQNKEnhgLVEKLTSLAALRAgDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 678
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKA---LAELRKELEELEE-ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 679 SELETQKEQIQLKLQEKTEELKEKMDNLTKQlfddvqkeerqrmlleksfELKTQDYEKQIQSLKEEIKALKDEKMQLQh 758
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEEL-------------------EAQIEQLKEELKALREALDELRAELTLLN- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 759 lvEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEkHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 838
Cdd:TIGR02168 817 --EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 839 EDLEHLNEDgelwfayeglkkaTRVLESHFQSQKDCYE---KEIEALNFKVVHLSQEINHLQKLFREENDIN--ESIRHE 913
Cdd:TIGR02168 894 SELEELSEE-------------LRELESKRSELRRELEelrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTleEAEALE 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 914 VTRLTSENmmipDFKQQISELEKQKQDL-EIRLN--EQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEK 990
Cdd:TIGR02168 961 NKIEDDEE----EARRRLKRLENKIKELgPVNLAaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
....*..
gi 2462545116 991 LIDKIQE 997
Cdd:TIGR02168 1037 TFDQVNE 1043
|
|
| Myo5p-like_CBD_afadin |
cd15471 |
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ... |
1109-1415 |
3.16e-12 |
|
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain.
Pssm-ID: 271255 Cd Length: 322 Bit Score: 69.26 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1109 PAHILFMCVRYADSLND---------ANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNTCHFLNCLKQysgeeefmk 1179
Cdd:cd15471 25 PAYTLYLAARYRLSTHYrpeltpterAHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1180 hnspqqnknclnNFDLSEYR----QILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISGlkptgfrkrsssIDD 1255
Cdd:cd15471 96 ------------DRDLSAFSvqaqDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPA------------IGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1256 tdgytmtsVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKD--MCSCRKGMQIRCNISYLEEWLKDK 1333
Cdd:cd15471 152 --------VLHTLSSAMRLLRRCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWAERQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1334 NLQnsLAKET-LEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPiDDFEKRVTPSFVRKVQALLNSRE 1412
Cdd:cd15471 224 GLE--LAADChLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP-PPGEPPIPPDLIERVVRLAESQA 300
|
...
gi 2462545116 1413 DSS 1415
Cdd:cd15471 301 DEL 303
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
635-1065 |
3.83e-12 |
|
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: 71.29 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 635 DVEKIQKLEAELEKAAThrrNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTE-------ELKEKMDNLT 707
Cdd:pfam05483 220 DHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN-QLEEKTKlqdenlkELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 708 KQLfDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDE--KMQLQH-LVEGEHVTS-----DGLKAEVARLSK 779
Cdd:pfam05483 296 KEL-EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEElnKAKAAHsFVVTEFEATtcsleELLRTEQQRLEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 780 ---QVKTIS-EFEKEI-ELLQAQKIDVEKHVQSQkrEMREKMSEITKQLLESYDIEDVRSRLSvedlehlNEDGELWFAY 854
Cdd:pfam05483 375 nedQLKIITmELQKKSsELEEMTKFKNNKEVELE--ELKKILAEDEKLLDEKKQFEKIAEELK-------GKEQELIFLL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 855 EGLKK----------ATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHL----QKLFREENDINESIRHEVTRLTSE 920
Cdd:pfam05483 446 QAREKeihdleiqltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLllenKELTQEASDMTLELKKHQEDIINC 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 921 NMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEeegtqrKALEAQNEIHTKEKEKLIdkiqeMQE 1000
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEE------NARSIEYEVLKKEKQMKI-----LEN 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 1001 ASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVH 1065
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
592-1091 |
4.55e-12 |
|
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: 71.30 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 592 RRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALR-AGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEK 670
Cdd:pfam15921 239 RIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEiTGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 671 LAKLQKHNSELETQKEQIQLKLQEKTEELKEK------------------------MDNLTKQLFDDVQKEERQrMLLEK 726
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanseltearterdqfsqesgnLDDQLQKLLADLHKREKE-LSLEK 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 727 S------------------FELKTQDYEKQIQSLKEEIKALKDE-KMQLQHLVEGEHVTSDGLKaEVARLSKQVKTISE- 786
Cdd:pfam15921 398 EqnkrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEm 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 787 FEKEIELLQAQKI----------DVEKHVQSQKREMREKMSEITKqllesydiedVRSR--LSVEDLEHLNEDGElwfay 854
Cdd:pfam15921 477 LRKVVEELTAKKMtlessertvsDLTASLQEKERAIEATNAEITK----------LRSRvdLKLQELQHLKNEGD----- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 855 eglkkatrvlesHFQS-QKDCYEKEIE-ALNFKVVH-LSQEINHLQKLFREENDINESIRHEVTRLTSE----NMMIPDF 927
Cdd:pfam15921 542 ------------HLRNvQTECEALKLQmAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEindrRLELQEF 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 928 K-------QQISELEKQKQDLEIR----LNEQAEKMKGkLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQ 996
Cdd:pfam15921 610 KilkdkkdAKIRELEARVSDLELEkvklVNAGSERLRA-VKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 997 EMQEASDHLKKQFET-ESEVkcnfrqEASRLTLENRD------------LEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1063
Cdd:pfam15921 689 EMETTTNKLKMQLKSaQSEL------EQTRNTLKSMEgsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANK 762
|
570 580
....*....|....*....|....*...
gi 2462545116 1064 vhsssgPKEYLgmlqykREDEAKLIQNL 1091
Cdd:pfam15921 763 ------EKHFL------KEEKNKLSQEL 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
607-1010 |
5.40e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.43 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 607 LQKKLEDQNKENHGLVEKLTSLAalragdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKE 686
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 687 QIQlKLQEKTEELK-EKMDNLTKQLFDDVQKEERQRMLLEKsfelKTQDYEKQIQSLKEEIKALKDEKMQLqhlvEGEHV 765
Cdd:TIGR04523 289 QLN-QLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN----QISQNNKIISQLNEQISQLKKELTNS----ESENS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 766 TSDG-LKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVE----- 839
Cdd:TIGR04523 360 EKQReLEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiiknn 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 840 ----DLEhlNEDGELWFAYEGLKKATRVLESHFQSQKDCY-----------------EKEIEALNFKVVHLSQEINHL-- 896
Cdd:TIGR04523 440 seikDLT--NQDSVKELIIKNLDNTRESLETQLKVLSRSInkikqnleqkqkelkskEKELKKLNEEKKELEEKVKDLtk 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 897 ---------QKLFREEN-------DINESIRHEVTRLTSENM--MIPDFKQQISELeKQKQDLEIRLNEQAEKMKGKLEE 958
Cdd:TIGR04523 518 kisslkekiEKLESEKKekeskisDLEDELNKDDFELKKENLekEIDEKNKEIEEL-KQTQKSLKKKQEEKQELIDQKEK 596
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 959 LSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFE 1010
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
627-1000 |
7.63e-12 |
|
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: 70.47 E-value: 7.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 627 SLAALRAGDVEKI-----QKLEAELEKAA---THRRNYEEKGKRYRDAvEEKLAKLQKHNSELETQKEQIQL------KL 692
Cdd:TIGR02168 137 SYSIIEQGKISEIieakpEERRAIFEEAAgisKYKERRKETERKLERT-RENLDRLEDILNELERQLKSLERqaekaeRY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 693 QEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKA 772
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 773 EVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE-SYDIEDVRSRLSVedlehlnedgelw 851
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELEE------------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 852 fayegLKKATRVLESHFQSQkdcyEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSEnmmIPDFKQQI 931
Cdd:TIGR02168 363 -----LEAELEELESRLEEL----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE---IEELLKKL 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 932 SELEKQKQDLEI-RLNEQAEKMKGKLEELSNQLHRSQEE-EGTQRKALEAQNEIHTKEKEklIDKIQEMQE 1000
Cdd:TIGR02168 431 EEAELKELQAELeELEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQAR--LDSLERLQE 499
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
588-1001 |
1.16e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 588 FQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAV 667
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 668 EEKLAKLQKHNSELETQKEQIQLK-LQEKTEELKEKMDNLTKQLFDDVQKEERQRML---LEKSFELKTQDYEKQIQSLK 743
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAELAeLPERLEELEERLEELRELEEELEELEAELAELqeeLEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 744 EEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEK---------------------------------- 789
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 790 ---EIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLES 866
Cdd:COG4717 279 lflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 867 HF-QSQKDCYEKEIEAL-NFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENmmiPDFKQQISELEKQkqdleiR 944
Cdd:COG4717 359 LEeELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELL---GELEELLEALDEE------E 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 945 LNEQAEKMKGKLEELSNQLHRSQEEEGT---QRKALEAQNEIHTK--EKEKLIDKIQEMQEA 1001
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAEleaELEQLEEDGELAELlqELEELKAELRELAEE 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
604-1054 |
3.38e-11 |
|
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: 68.28 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 604 VQRLQKKLEdQNKENHGLVEKltSLAALRAGDVEkiqkLEAELEKAATHRRNYEEKGKRyrdaVEEKLAKLQKHNSELET 683
Cdd:pfam01576 358 LEELTEQLE-QAKRNKANLEK--AKQALESENAE----LQAELRTLQQAKQDSEHKRKK----LEGQLQELQARLSESER 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 684 QKEQiqlkLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEK---SFELKTQDYEKQIQ-------SLKEEIKALKDEK 753
Cdd:pfam01576 427 QRAE----LAEKLSKLQSELESVSSLL----NEAEGKNIKLSKdvsSLESQLQDTQELLQeetrqklNLSTRLRQLEDER 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 754 MQLQHLVEGEHVTSDGLKAEVARLSKQV----KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITK-------- 821
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrl 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 822 -QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEglkkatRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLF 900
Cdd:pfam01576 579 qQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEE------KAISARYAEERDRAEAEAREKETRALSLARALEEALEAK 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 901 REENDINESIRHEVTRLTSENmmiPDFKQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSQE-----EEGTQrk 975
Cdd:pfam01576 653 EELERTNKQLRAEMEDLVSSK---DDVGKNVHELERSKRALE----QQVEEMKTQLEELEDELQATEDaklrlEVNMQ-- 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 976 ALEAQNE--IHTKE------KEKLIDKIQEMQEASDHLKKQFETESEVKcnfrqeaSRLTLENRDLEEELDM----KDRV 1043
Cdd:pfam01576 724 ALKAQFErdLQARDeqgeekRRQLVKQVRELEAELEDERKQRAQAVAAK-------KKLELDLKELEAQIDAankgREEA 796
|
490
....*....|....
gi 2462545116 1044 IK---KLQDQVKTL 1054
Cdd:pfam01576 797 VKqlkKLQAQMKDL 810
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
586-850 |
7.07e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 586 RRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENhglvEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRD 665
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 666 AVEEKLAKLQKHNSELETQKEQIQ------LKLQEKTEELKEKMDNLTKQL---FDDVQKEERQRMLLEKSFELKTQDYE 736
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRReleerlEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 737 KQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKM 816
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270
....*....|....*....|....*....|....
gi 2462545116 817 SEITKQLLESYDIEDVRSRLSVEDLEHLNEDGEL 850
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
675-1063 |
7.43e-11 |
|
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: 67.39 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 675 QKHNSELETQKEQiqLKLQEKTEELKEKMDNLTKQLfDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKM 754
Cdd:TIGR02168 667 KTNSSILERRREI--EELEEKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 755 QLQHLVEGEHVTSDGLKAEV----ARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITkqlLESYDIE 830
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT---LLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 831 DVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLEShfqsqkdcYEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 910
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIES--------LAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 911 RHEVTRLTSEnmmipdfkqqISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLhRSQEEEGTQRKALEAqnEIHTKE 987
Cdd:TIGR02168 893 RSELEELSEE----------LRELESKRSELRrelEELREKLAQLELRLEGLEVRI-DNLQERLSEEYSLTL--EEAEAL 959
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545116 988 KEKLIDKIQEMQEASDHLKKQFETESEVkcNFRQEAsrltlENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1063
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIE-----EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
485-1063 |
1.42e-10 |
|
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: 66.23 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 485 QRKKFLRERRAALIIQQYFRG---QQTVRKAITAVALKEAWAAIIIQkhcrgylVRSLYQLIRMATITMQAYSRGFLARR 561
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEaqlEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 562 R-YRKMLEEHKAVILQKYARAWLARRRFQSIRRfvlniqltyRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGdvEKIQ 640
Cdd:TIGR02168 375 EeLEEQLETLRSKVAQLELQIASLNNEIERLEA---------RLERLEDRRERLQQEIEELLKKLEEAELKELQ--AELE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 641 KLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQK------EQIQLKLQEKTEELKEKMDN------LTK 708
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNqsglsgILG 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 709 QLFDDVQKEERQRMLLEKSFELKTQDYE-KQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAE-----------VAR 776
Cdd:TIGR02168 524 VLSELISVDEGYEAAIEAALGGRLQAVVvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNdreilkniegfLGV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 777 LSKQVKTISEFEKEIELLQAQKIDVE--KHVQSQKREMREKMSEITKqllesyDIEDVRSRLSV------EDLEHLNEDG 848
Cdd:TIGR02168 604 AKDLVKFDPKLRKALSYLLGGVLVVDdlDNALELAKKLRPGYRIVTL------DGDLVRPGGVItggsakTNSSILERRR 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 849 ELwfayEGLKKATRVLESHFQSQK---DCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSenmMIP 925
Cdd:TIGR02168 678 EI----EELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE---RIA 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 926 DFKQQISELEKQKQDLEIRLNEQAEKMK---GKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLID---KIQEMQ 999
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLESLE 830
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 1000 EASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1063
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
605-1091 |
1.52e-10 |
|
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: 66.15 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 605 QRLQKKLEDQNKENHGLVEKLTSLaalragdvEKIQKLEAELEKAaTHRRNYEEKGKRY---RDAVEEKLAKLQKHNSEL 681
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARI--------EELRAQEAVLEET-QERINRARKAAPLaahIKAVTQIEQQAQRIHTEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 682 ETQKEQIQLKLQEKTEELKEKMD-----NLTKQLF---------DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIK 747
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSieeqrRLLQTLHsqeihirdaHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 748 ALKDEKMQL---QHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLL 824
Cdd:TIGR00618 397 SLCKELDILqreQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 825 ESYDIEDVRSRLSVEDLEHLNEDGELWFAYEG----------LKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEIN 894
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGscihpnparqDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 895 HLQKLFREEndinESIRHEVTRLTSenmMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQR 974
Cdd:TIGR00618 557 QRASLKEQM----QEIQQSFSILTQ---CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 975 KALEAQNEIHTKEKEKL------IDKIQEMQEASDHLKKQFETES-EVKCNFRQEASRLTLENRDLEEELDMKDRVIKKL 1047
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTalhalqLTLTQERVREHALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2462545116 1048 QDQVKTLSKTIGKANDVHSSSGPKeylgmLQYKREDEAKLIQNL 1091
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSD-----LAAREDALNQSLKEL 748
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
560-1058 |
1.80e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 560 RRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLtyRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKI 639
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELEL--ELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 640 QKLEAELEKAATHRRNYEEKgkryRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLtkqlfDDVQKEER 719
Cdd:COG1196 319 EELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 720 QRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKI 799
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 800 DVEKHVQSQKREMREKMSE------ITKQLLESYD--IEDVRSRLSVEDLEHLNEDGELW----FAYEGL---------- 857
Cdd:COG1196 470 EEAALLEAALAELLEELAEaaarllLLLEAEADYEgfLEGVKAALLLAGLRGLAGAVAVLigveAAYEAAleaalaaalq 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 858 -------------------KKATRV----LESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEV 914
Cdd:COG1196 550 nivveddevaaaaieylkaAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 915 TRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEiHTKEKEKLIDK 994
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE-ALLAEEEEERE 708
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 995 IQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDR----VIKKLQDQVKTLSKTI 1058
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELpeppDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
562-898 |
4.19e-10 |
|
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: 64.70 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 562 RYRKMLEEhkaviLQKYaRAWLARRRFQSIRRfvlniqltyRVQRLQKKLEDQNKEnhglVEKLTslaalragdvEKIQK 641
Cdd:TIGR02169 212 RYQALLKE-----KREY-EGYELLKEKEALER---------QKEAIERQLASLEEE----LEKLT----------EEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 642 LEAELEKAathRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELkEKMDNLTKQLFddvqkEERQR 721
Cdd:TIGR02169 263 LEKRLEEI---EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLE-----AEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 722 MLLEK-SFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKID 800
Cdd:TIGR02169 334 LLAEIeELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 801 VEKHVQSQKREMREKMSEITKQLLEsydiedVRSRLSVEDLEhlnedgelwfayegLKKATRVLEShFQSQKDCYEKEIE 880
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINE------LEEEKEDKALE--------------IKKQEWKLEQ-LAADLSKYEQELY 472
|
330
....*....|....*...
gi 2462545116 881 ALNFKVVHLSQEINHLQK 898
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQR 490
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
601-966 |
8.43e-10 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 63.33 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 601 TYRVQRLQKKLEDqnkenhglVEKLTSLAAlraGDVEKIQK-LEAELEKAATHRRNYEEKGKRYR--------------- 664
Cdd:pfam06160 78 KYRFKKAKKALDE--------IEELLDDIE---EDIKQILEeLDELLESEEKNREEVEELKDKYRelrktllanrfsygp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 665 --DAVEEKLAKLQKHNSELETQKEQ--------IQLKLQEKTEELKEKMDNLtKQLFDDVQKE---------ERQRMLLE 725
Cdd:pfam06160 147 aiDELEKQLAEIEEEFSQFEELTESgdyleareVLEKLEEETDALEELMEDI-PPLYEELKTElpdqleelkEGYREMEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 726 KSFELKTQDYEKQIQSLKEEIKALkdekmqLQHLVEGEhvtSDGLKAEVARLSKQVKTISE-FEKEIEllqaQKIDVEKH 804
Cdd:pfam06160 226 EGYALEHLNVDKEIQQLEEQLEEN------LALLENLE---LDEAEEALEEIEERIDQLYDlLEKEVD----AKKYVEKN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 805 vQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHlnedgelwfayeglkkaTRVLESHFQSQKDCYEKEIEALNF 884
Cdd:pfam06160 293 -LPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELER-----------------VRGLEKQLEELEKRYDEIVERLEE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 885 KVVHLSQEINHLQKLFREENDINEsiRHEvtrltsenmmipDFKQQISELEKQkqdlEIRLNEQAEKMKGKLEELSNQLH 964
Cdd:pfam06160 355 KEVAYSELQEELEEILEQLEEIEE--EQE------------EFKESLQSLRKD----ELEAREKLDEFKLELREIKRLVE 416
|
..
gi 2462545116 965 RS 966
Cdd:pfam06160 417 KS 418
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
679-1058 |
1.41e-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: 63.07 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 679 SELETQKEQIQLKLQEKTEELKEKMDNLTkqlfddvqKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEkmQLQH 758
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLE--------ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD--YLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 759 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsYDIEDVRSRLSV 838
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-LLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 839 EDLEHLNEDGELwfaYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHL---QKLFREENDINESIRHEVT 915
Cdd:pfam02463 314 EKLKESEKEKKK---AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLeqlEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 916 RLTSENMMIPDFKQQISELEKQ--KQDLEIRLNEQAEKMKGKLEELSnqlhrsqEEEGTQRKALEAQNEIHTKEKEKLID 993
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEE-------SIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 994 KIQEMQEASDHLKKQfETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1058
Cdd:pfam02463 464 ELELKKSEDLLKETQ-LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
701-1060 |
2.20e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 701 EKMDNLTKQL--FDDVQKEERQRMLLEKSFELKTQDYEKQIQS---LKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVA 775
Cdd:PRK03918 145 ESREKVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 776 RLSKQVKTISEFEKEIELLQAQKIDVEKHvqsqKREMREKMSEITKQLLES-YDIEDVRSRlsVEDLEHLNEDGELWFAY 854
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGS----KRKLEEKIRELEERIEELkKEIEELEEK--VKELKELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 855 EGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEndinESIRHEVTRLTSENMMIPDFKQQISEL 934
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL----KELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 935 EKQKQDLEirlNEQAEKMKGKLEELSNqlhrsqeeegtqrkaleAQNEIhTKEKEKLIDKIQEMQEASDHLKKQFE--TE 1012
Cdd:PRK03918 375 ERLKKRLT---GLTPEKLEKELEELEK-----------------AKEEI-EEEISKITARIGELKKEIKELKKAIEelKK 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 1013 SEVKC---------NFRQE-ASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1060
Cdd:PRK03918 434 AKGKCpvcgrelteEHRKElLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
668-1007 |
2.53e-09 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 62.27 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 668 EEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRmlleKSFELKTQDYEKQIQSLKEEIK 747
Cdd:pfam15818 27 EEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEK----GKYQLATEIKEKEIEGLKETLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 748 ALKDEKMQLQhlvegehvtsdglkaevarlskqvKTISEFEKEIELLQAQKIDVEKhvqsQKREMREKMSEITKQL---- 823
Cdd:pfam15818 103 ALQVSKYSLQ------------------------KKVSEMEQKLQLHLLAKEDHHK----QLNEIEKYYATITGQFglvk 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 824 -----LESYDIEDVR--SRLSVedlehLNE--DGELWFAYEGLKKATRVL-ESHFQSQkdcYEKEIEALNFKVVHlsQEI 893
Cdd:pfam15818 155 enhgkLEQNVQEAIQlnKRLSA-----LNKkqESEICSLKKELKKVTSDLiKSKVTCQ---YKMGEENINLTIKE--QKF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 894 NHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELS--NQLHRSQEEEg 971
Cdd:pfam15818 225 QELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLErdNELQREKVKE- 303
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2462545116 972 TQRKALEAQNEiHTK-------EKEKLIDKIQEMQEASDHLKK 1007
Cdd:pfam15818 304 NEEKFLNLQNE-HEKalgtwkkHVEELNGEINEIKNELSSLKE 345
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
725-1070 |
2.84e-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: 62.01 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 725 EKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQvktISEFEKEIELLQAQkidvekh 804
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQLEQE------- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 805 vqsqkremREKMSEItkqllesydIEDVRSRLSVEDLEHLNEDGELwfayeglkkatrvleshfqsqkDCYEKEIEALNF 884
Cdd:TIGR02169 732 --------EEKLKER---------LEELEEDLSSLEQEIENVKSEL----------------------KELEARIEELEE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 885 KVVHLSQEINHLqklfreENDINESIRHEVTRLTSEnmmipdFKQQISELEKQKQDLEIRLNEQAEKmKGKLEELSNQLH 964
Cdd:TIGR02169 773 DLHKLEEALNDL------EARLSHSRIPEIQAELSK------LEEEVSRIEARLREIEQKLNRLTLE-KEYLEKEIQELQ 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 965 RSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFEtesevkcNFRQEASRLTLENRDLEEELDMKDRVI 1044
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG-------DLKKERDELEAQLRELERKIEELEAQI 912
|
330 340
....*....|....*....|....*.
gi 2462545116 1045 KKLQDQVKTLSKTIGKANDVHSSSGP 1070
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIED 938
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
604-953 |
3.12e-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: 61.91 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 604 VQRLQKKLEDQNKEnhgLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELET 683
Cdd:pfam02463 164 GSRLKRKKKEALKK---LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 684 QKEQIQLKLQEKTEELKEKMDNlTKQLFDDVQKEERQrmlleksfelktqdyEKQIQSLKEEIKALKD-----EKMQLQH 758
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEK-EEEKLAQVLKENKE---------------EEKEKKLQEEELKLLAkeeeeLKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 759 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 838
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 839 EDLEHLNEDGELW-FAYEGLKKATRVLEsHFQSQKDCY--EKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVT 915
Cdd:pfam02463 385 RLSSAAKLKEEELeLKSEEEKEAQLLLE-LARQLEDLLkeEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462545116 916 RLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMK 953
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
679-1061 |
3.96e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 679 SELETQKEQIQLKLqEKTEElkekmdNLTKqlFDDVQKE--------ERQRMLLEKSFELKTQDYEKQIQSLKEEIKALK 750
Cdd:COG1196 168 SKYKERKEEAERKL-EATEE------NLER--LEDILGElerqleplERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 751 DEKMQLQHLVEGEHVTSDGLKAEVARLskqvktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQllesydie 830
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAEL----------EAELEELRLELEELELELEEAQAEEYELLAELARL-------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 831 dvrsrlsVEDLEHLNEDgelwfayeglkkatrvlESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 910
Cdd:COG1196 301 -------EQDIARLEER-----------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 911 RhevtrltsenmmipdfkQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEgTQRKALEAQNEIHTKEKEK 990
Cdd:COG1196 357 E-----------------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLER 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 991 LIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKA 1061
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
586-1042 |
4.41e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 586 RRFQSIRRFVLNIQL-----TYRVQRLQKKLEDQNKENHGLVEKLTS--------LAAL--RAGDVEKIQKLEaELE--- 647
Cdd:COG4913 496 EHYAAALRWVNRLHLrgrlvYERVRTGLPDPERPRLDPDSLAGKLDFkphpfrawLEAElgRRFDYVCVDSPE-ELRrhp 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 648 KAAT------HRRNYEEKGKRYRDA--------VEEKLAKLQKhnsELETQKEQIQlKLQEKTEELKEKMDNLTKQLfdd 713
Cdd:COG4913 575 RAITragqvkGNGTRHEKDDRRRIRsryvlgfdNRAKLAALEA---ELAELEEELA-EAEERLEALEAELDALQERR--- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 714 vqkeERQRMLLEKSF-ELKTQDYEKQIQSLKEEIKALKDEKMQLQHLvegehvtsdglkaevarlskqvktisefEKEIE 792
Cdd:COG4913 648 ----EALQRLAEYSWdEIDVASAEREIAELEAELERLDASSDDLAAL----------------------------EEQLE 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 793 LLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQK 872
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 873 DCYEKEIEALNFKVVHLSQEINHLQKLFREENDI----NESIRHEVTRLTSENmmIPDFKQQISELEKQ-----KQDLEI 943
Cdd:COG4913 776 DALRARLNRAEEELERAMRAFNREWPAETADLDAdlesLPEYLALLDRLEEDG--LPEYEERFKELLNEnsiefVADLLS 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 944 RLNEQAEKMKGKLEELSNQLHRSQEEEGTqRKALEAQNEIHTKEKEKLidkiQEMQEASDHLKKQFETESEVKCNFRQEA 1023
Cdd:COG4913 854 KLRRAIREIKERIDPLNDSLKRIPFGPGR-YLRLEARPRPDPEVREFR----QELRAVTSGASLFDEELSEARFAALKRL 928
|
490 500
....*....|....*....|
gi 2462545116 1024 -SRLtlenRDLEEELDMKDR 1042
Cdd:COG4913 929 iERL----RSEEEESDRRWR 944
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
637-1058 |
6.16e-09 |
|
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: 60.96 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 637 EKIQKLEAEL--EKAATHRRNYEE-----KGKRyrdaVEEKLAKLQKHNSELETQKEQIQLKLQEKTEEL---KEKMDNL 706
Cdd:pfam01576 103 QHIQDLEEQLdeEEAARQKLQLEKvtteaKIKK----LEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeeEEKAKSL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 707 TK----------QLFDDVQKEERQRMLLEKS---FELKTQDYEKQIQSLKEEIKALKdekMQLQHlvegehvTSDGLKAE 773
Cdd:pfam01576 179 SKlknkheamisDLEERLKKEEKGRQELEKAkrkLEGESTDLQEQIAELQAQIAELR---AQLAK-------KEEELQAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 774 VARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQkREMREKMSEITKQLLEsyDIEDVRSRLsvED-LEHLNEDGELWF 852
Cdd:pfam01576 249 LARLEEETAQKNNALKKIRELEAQISELQEDLESE-RAARNKAEKQRRDLGE--ELEALKTEL--EDtLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 853 AYEG----LKKA----TRVLESHFQSQKDCYEKEIEALN--------FKVV------HLSQEINHLQKLFREENDINESI 910
Cdd:pfam01576 324 KREQevteLKKAleeeTRSHEAQLQEMRQKHTQALEELTeqleqakrNKANlekakqALESENAELQAELRTLQQAKQDS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 911 RHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEI---H 984
Cdd:pfam01576 404 EHKRKKLEGQ---LQELQARLSESERQRAELAEKLSKlqsELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELlqeE 480
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 985 TKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1058
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
641-1060 |
6.27e-09 |
|
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: 60.90 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 641 KLEAELEkaaTHRRNYEEKGKRYRDAVEEKLA--------KLQKHNSELETQK---EQIQLKLQEKTEELKEKMDNLTkq 709
Cdd:pfam15921 56 KYEVELD---SPRKIIAYPGKEHIERVLEEYShqvkdlqrRLNESNELHEKQKfylRQSVIDLQTKLQEMQMERDAMA-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 710 lfdDVQKEERQrmlleksfelKTQDYEKQIQSLKEEIKA---LKDE-------------KMQLQH---LVEGEHVTSDGL 770
Cdd:pfam15921 131 ---DIRRRESQ----------SQEDLRNQLQNTVHELEAakcLKEDmledsntqieqlrKMMLSHegvLQEIRSILVDFE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 771 KAEVARLSKQ---------------VKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQ-------LLESYD 828
Cdd:pfam15921 198 EASGKKIYEHdsmstmhfrslgsaiSKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhqdrieqLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 829 IE----------------DVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVV----- 887
Cdd:pfam15921 278 VEitgltekassarsqanSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVlanse 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 888 ---------HLSQEI----NHLQKLF-------------REEN------DINESIR--HEVTRLTSENMMIP-------- 925
Cdd:pfam15921 358 ltearterdQFSQESgnldDQLQKLLadlhkrekelsleKEQNkrlwdrDTGNSITidHLRRELDDRNMEVQrleallka 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 926 -------DFKQQISELEKQKQDLE------IRLNEQAEKMKGKLEELSNQLHRSQEEEGT----------QRKALEAQNE 982
Cdd:pfam15921 438 mksecqgQMERQMAAIQGKNESLEkvssltAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltaslqeKERAIEATNA 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 983 IHTKEKEKLIDKIQEMQeasdHLKkqfeTESEVKCNFRQEASRLTLenrdleeELDMKDRVIKKLQDQVKTLSKTIGK 1060
Cdd:pfam15921 518 EITKLRSRVDLKLQELQ----HLK----NEGDHLRNVQTECEALKL-------QMAEKDKVIEILRQQIENMTQLVGQ 580
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
666-1035 |
9.90e-09 |
|
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: 60.37 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 666 AVEEKLAKLQKHNSE------LETQKEQIQLkLQEKTEELKEKMDNLTK---------QLFDDVQKEERQRMLLEKSFEL 730
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKtftrvvLLPQGEFAQF-LKAKSKEKKELLMNLFPldqytqlalMEFAKKKSLHGKAELLTLRSQL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 731 KTQDYEKQIQSLKEEIKALKDEKMQL----QHLVEGEHVTSDGLKAEVARLSKQvKTISEFEKEIELLQAQKIDVEKhvQ 806
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLrealQQTQQSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEELRAQEAVLEE--T 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 807 SQKREMREKMSEITkqllesydiedvrsrLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKV 886
Cdd:TIGR00618 283 QERINRARKAAPLA---------------AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 887 VHLSQEINHlqklFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQ----KQDLEIRLNEQAEKMKGKLEE--LS 960
Cdd:TIGR00618 348 QTLHSQEIH----IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKlqslCKELDILQREQATIDTRTSAFrdLQ 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 961 NQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEE 1035
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
624-1056 |
1.04e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 624 KLTSLAALRAGDVEKIQKLEAELEKAA--THRRNYEEkgkryRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKE 701
Cdd:COG4717 36 KSTLLAFIRAMLLERLEKEADELFKPQgrKPELNLKE-----LKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 702 KMDNLTKQLfDDVQKEERQRMLLEKSFELKTQ--DYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSK 779
Cdd:COG4717 110 ELEELREEL-EKLEKLLQLLPLYQELEALEAElaELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 780 QV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEI--TKQLLESYDIEDVRSRLSV----------------ED 840
Cdd:COG4717 189 ATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELeqLENELEAAALEERLKEARLllliaaallallglggSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 841 LEHLNEDGELWFAYEGLkkaTRVLESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIrhEVTRLTSE 920
Cdd:COG4717 269 LSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQ-ALPALEELEEEELEELLAALGLPPDL--SPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 921 NMMIPDFKQQISELEKQKQDLEIRLNEQaekmkgKLEELSNQLHRSQEEEgtQRKALEAQNEIHtKEKEKLIDKIQEMQE 1000
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQ------EIAALLAEAGVEDEEE--LRAALEQAEEYQ-ELKEELEELEEQLEE 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545116 1001 ASDHLKKQFETESEVKCnfRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSK 1056
Cdd:COG4717 414 LLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
696-1101 |
1.46e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.85 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 696 TEELKEKMDNLTKQLFDDVQKEERQrmllEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHL-VEGEHVTSDGLKAEV 774
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAA----EEQLVQANGELEKASREETFARTALKNARLDLRRLfDEKQSEKDKKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 775 ARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSrlsvedlehlneDGELWFAY 854
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL------------KAAIAARR 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 855 EGLKKATRVLESHfqsqkdcYEKEIEALNF---KVVHLSQEINHL-QKLFREENDinesiRHEVTRLTsenmmipDFKQQ 930
Cdd:pfam12128 743 SGAKAELKALETW-------YKRDLASLGVdpdVIAKLKREIRTLeRKIERIAVR-----RQEVLRYF-------DWYQE 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 931 ISELEKQkqdleiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQneihTKEKEKLIDKIQEMQEASDHLKKQFE 1010
Cdd:pfam12128 804 TWLQRRP------RLATQLSNIERAISELQQQLARLIADTKLRRAKLEME----RKASEKQQVRLSENLRGLRCEMSKLA 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1011 TESEvKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKandvHSSSGPKEYlgmLQYKREDEAKLIQN 1090
Cdd:pfam12128 874 TLKE-DANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD----HSGSGLAET---WESLREEDHYQNDK 945
|
410
....*....|.
gi 2462545116 1091 LILDLKPRGVV 1101
Cdd:pfam12128 946 GIRLLDYRKLV 956
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
605-1027 |
1.47e-08 |
|
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: 59.35 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 605 QRLQKKlEDQNK-------ENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKH 677
Cdd:pfam05483 370 QRLEKN-EDQLKiitmelqKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 678 NSE---LETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELkTQDYEKQIQSLKEEIKALKDEKM 754
Cdd:pfam05483 449 EKEihdLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL-TQEASDMTLELKKHQEDIINCKK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 755 QLQHLVegehvtsdglkaevarlskqvktisefeKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESydiEDVRS 834
Cdd:pfam05483 528 QEERML----------------------------KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS---EENAR 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 835 RLSVEDLEHLNEDGELWFAYEGLKK----ATRVLESHFQSQK------DCYEKEIEALNFKVVHLSQEINHLQKLFREEN 904
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKqienKNKNIEELHQENKalkkkgSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 905 DiNESIRHEVTRLTSENMM--IPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNE 982
Cdd:pfam05483 657 D-NYQKEIEDKKISEEKLLeeVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2462545116 983 IHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLT 1027
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
592-961 |
2.08e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 592 RRFVLNIQLTYRvQRLQKKLEDQNKENHGLVEKLTSLAALragdVEKIQKLEAELEKAATHR------RNYEEKGKRYRD 665
Cdd:PRK04863 281 RRVHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAEL----NEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 666 AVEEKLAKLQKHNSELETQKEQiQLKLQEKTEELKEKMDNLTKQLFDDVQK-EERQRMLLEksfelktqdYEKQIQSLkE 744
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQ-QEENEARAEAAEEEVDELKSQLADYQQAlDVQQTRAIQ---------YQQAVQAL-E 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 745 EIKALKD---------EKMQLQHLVEGEHVTSDGLKAEvARLSKQVKTISEFEKEIELLQAQKIDVE------------- 802
Cdd:PRK04863 425 RAKQLCGlpdltadnaEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSQFEQAYQLVRKIAGEVSrseawdvarellr 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 803 -----KHVQSQKREMREKMSEITKQLLESYDIEDVRSRL---------SVEDLEHLNEDGElwfayeglkkatRVLESHF 868
Cdd:PRK04863 504 rlreqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFckrlgknldDEDELEQLQEELE------------ARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 869 QSQKDCYEKEIEaLNFKVVHLSQEINHLQKL---FREENDINESIRHEV--TRLTSENMMipDFKQQISELEKQKQDLEI 943
Cdd:PRK04863 572 ESVSEARERRMA-LRQQLEQLQARIQRLAARapaWLAAQDALARLREQSgeEFEDSQDVT--EYMQQLLERERELTVERD 648
|
410
....*....|....*...
gi 2462545116 944 RLNEQAEKMKGKLEELSN 961
Cdd:PRK04863 649 ELAARKQALDEEIERLSQ 666
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
686-1050 |
2.35e-08 |
|
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: 58.37 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 686 EQIQLKLQEKTEELKEKMdNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHV 765
Cdd:pfam07888 30 ELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 766 TSDGLKAEVARLSKQ----VKTISEFEKEIELLQAQKIDVEkhvqSQKREMREKMSEITKQLLESY-DIEDVRSRL--SV 838
Cdd:pfam07888 109 SSEELSEEKDALLAQraahEARIRELEEDIKTLTQRVLERE----TELERMKERAKKAGAQRKEEEaERKQLQAKLqqTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 839 EDLEHLNEDgelwfaYEGLKKATRVLESHFQSQKDcyekeiealnfKVVHLSQEINHLQKLFREENDINESIRHEVTRLT 918
Cdd:pfam07888 185 EELRSLSKE------FQELRNSLAQRDTQVLQLQD-----------TITTLTQKLTTAHRKEAENEALLEELRSLQERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 919 SENMMIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKI 995
Cdd:pfam07888 248 ASERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 996 QEMQEA-----SDHLKKQFETESEVKCNFRQEAsrltlENRDLEEELDMKDRVIKKLQDQ 1050
Cdd:pfam07888 328 QRLEERlqeerMEREKLEVELGREKDCNRVQLS-----ESRRELQELKASLRVAQKEKEQ 382
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
634-1060 |
5.10e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 634 GDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLqekteelkekmdnltkqlfdd 713
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKL--------------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 714 vqkeerqrmlleksfelktQDYEKQIQSLKEEIKALKDEKMQLQHLVE-----------GEHVTSDGLKAEVARLSKQVK 782
Cdd:PRK01156 419 -------------------QDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKS 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 783 TISEFEKEIElLQAQKIDvEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATR 862
Cdd:PRK01156 480 RLEEKIREIE-IEVKDID-EKIVDLKKRKEYLESEEINKSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 863 VLEshfqsQKDCYEKEIEALNFKVVHLSQEINHLQKLFreeNDINESIRHEVTRLTSENMMIPDFK----QQISELEKQK 938
Cdd:PRK01156 557 SLK-----LEDLDSKRTSWLNALAVISLIDIETNRSRS---NEIKKQLNDLESRLQEIEIGFPDDKsyidKSIREIENEA 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 939 QDLEIRLNE------QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT--KEKEKLIDKIqemqeasdhLKKQFE 1010
Cdd:PRK01156 629 NNLNNKYNEiqenkiLIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDnlKKSRKALDDA---------KANRAR 699
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1011 TESEVKCNfRQEASRLTLENRDLEEELDMKDRVIKKLQDqVKTLSKTIGK 1060
Cdd:PRK01156 700 LESTIEIL-RTRINELSDRINDINETLESMKKIKKAIGD-LKRLREAFDK 747
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
564-999 |
5.62e-08 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 57.45 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 564 RKMLEEHKavilqkyarawlaRRRFQSIRRFVLNiQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVE------ 637
Cdd:pfam07111 131 RKNLEEGS-------------QRELEEIQRLHQE-QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKqlaeaq 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 638 --------KIQKLEAELEKAAT-----------------HRRNYEEKGKRYRDAVEEklakLQKHNSELETQKEQIQLKL 692
Cdd:pfam07111 197 keaellrkQLSKTQEELEAQVTlveslrkyvgeqvppevHSQTWELERQELLDTMQH----LQEDRADLQATVELLQVRV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 693 QEKTEELKEKMDNLTK--QLFDDVQKE--ERQRMLL----EKSF----ELKTQDYEK---------QIQSLKEEIKALKD 751
Cdd:pfam07111 273 QSLTHMLALQEEELTRkiQPSDSLEPEfpKKCRSLLnrwrEKVFalmvQLKAQDLEHrdsvkqlrgQVAELQEQVTSQSQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 752 EKMQLQHL-------VEGEHVTSDGLKAEVARLS----KQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEI- 819
Cdd:pfam07111 353 EQAILQRAlqdkaaeVEVERMSAKGLQMELSRAQearrRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIp 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 820 --TKQLleSYDIEDVRS------------RLSVE-----------------DLEHLNEDGELWFAYegLKKATRVLESHF 868
Cdd:pfam07111 433 slSNRL--SYAVRKVHTikglmarkvalaQLRQEscpppppappvdadlslELEQLREERNRLDAE--LQLSAHLIQQEV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 869 QSQKDCYEKEIEALNFKVVHLSQEINHLQKLF--------------REENDINESIRHEVTRltSENMMIPDFKQQISEL 934
Cdd:pfam07111 509 GRAREQGEAERQQLSEVAQQLEQELQRAQESLasvgqqlevarqgqQESTEEAASLRQELTQ--QQEIYGQALQEKVAEV 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545116 935 E----KQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQ 999
Cdd:pfam07111 587 EtrlrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELE 655
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
603-1072 |
1.18e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.45 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSLAALragdVEKIQKLEAELEKAATHRRNYEEKGKRYRDaVEEKLAKLQkhNSELE 682
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSALNELSSL----EDMKNRYESEIKTAESDLSMELEKNNYYKE-LEERHMKII--NDPVY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 683 TQKEQIQ--LKLQEKTEELKEKMDNLTKQL--FDDVQKEERQrmlLEKSFElktqDYEKQiQSLKEEIKALKDEkmqlqh 758
Cdd:PRK01156 292 KNRNYINdyFKYKNDIENKKQILSNIDAEInkYHAIIKKLSV---LQKDYN----DYIKK-KSRYDDLNNQILE------ 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 759 lVEGEHVTSDGLKAEVARLSKQvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE-SYDIE--DVRSR 835
Cdd:PRK01156 358 -LEGYEMDYNSYLKSIESLKKK---IEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDiSSKVSslNQRIR 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 836 LSVEDLEHLNEDGELWFAYE---------GLKKATRVLEsHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKL--FREEN 904
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQSvcpvcgttlGEEKSNHIIN-HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRkeYLESE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 905 DINESIrhevtrlTSENmmipdfkqQISELEKQKQDLEIRLNEQAEKmKGKLEELSNQlHRSQEEEGTQRKALEAQNEIH 984
Cdd:PRK01156 513 EINKSI-------NEYN--------KIESARADLEDIKIKINELKDK-HDKYEEIKNR-YKSLKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 985 TKEkekLIDkIQEMQEASDHLKKQF-ETES---EVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1060
Cdd:PRK01156 576 VIS---LID-IETNRSRSNEIKKQLnDLESrlqEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGK 651
|
490
....*....|..
gi 2462545116 1061 ANDVHSSSGPKE 1072
Cdd:PRK01156 652 IDNYKKQIAEID 663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
559-1086 |
1.49e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 559 ARR--RYRKMLEEHKAVILQKY--ARAWLARRRFQSIRRF--VLNIQLTYRVQRLQKKLEDQNKenhglvekltslaALR 632
Cdd:PTZ00121 1181 ARKaeEVRKAEELRKAEDARKAeaARKAEEERKAEEARKAedAKKAEAVKKAEEAKKDAEEAKK-------------AEE 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 633 AGDVEKIQKLEaELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFD 712
Cdd:PTZ00121 1248 ERNNEEIRKFE-EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 713 DVQKEERQRmllEKSFELKTQDYEKQIQSLKEEIKALKDEKmqlqhlvegehvtsdglKAEVARLSKqvktiSEFEKEIE 792
Cdd:PTZ00121 1327 AKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEE-----------------KAEAAEKKK-----EEAKKKAD 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 793 LLQAQKIDVEKHVQSQKR--EMREKMSEITKQLLESYDIEDVRSRLSvedlehlnedgELWFAYEGLKKATRVLESHFQS 870
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKKADEAKKKAE-----------EKKKADEAKKKAEEAKKADEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 871 QKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIR--HEVTRLTSENMMIPDFKQQISEL----EKQKQDlEIR 944
Cdd:PTZ00121 1451 KKAEEAKKAEEAK-KKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEAKKAAEAKKKADEAkkaeEAKKAD-EAK 1528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 945 LNEQAEKM--------KGKLEELSNQLHRSQEEEgtQRKALEAQNEihTKEKEKLIDKIQEMQEASDHLKKQFETESEVK 1016
Cdd:PTZ00121 1529 KAEEAKKAdeakkaeeKKKADELKKAEELKKAEE--KKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1017 CNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPKEYLGMLQYKREDEAK 1086
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
599-943 |
1.73e-07 |
|
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: 55.90 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQKKLEDQNKENHGLVEKltslaalragdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 678
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQ------------ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 679 S-ELETQKEQIQLKLQEKTEELK-----------EKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQ--IQSLKE 744
Cdd:pfam17380 341 RmAMERERELERIRQEERKRELErirqeeiameiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQrkIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 745 EIKALKDEKmqlqhlvegehvtSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVekhVQSQKREMREKMSEITKQLL 824
Cdd:pfam17380 421 EMEQIRAEQ-------------EEARQREVRRLEEERAREMERVRLEEQERQQQVER---LRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 825 ESYDIEDVRSRLSVEDLEHLNEdgelwfAYEGLKKATRVLESHFQS-QKDCYEKEIEalnfkvvHLSQEINHLQKLFREE 903
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQ------AMIEEERKRKLLEKEMEErQKAIYEEERR-------REAEEERRKQQEMEER 551
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2462545116 904 NDINESIR---HEVTRLTS---ENMMIpdfkQQISELEKQKQDLEI 943
Cdd:pfam17380 552 RRIQEQMRkatEERSRLEAmerEREMM----RQIVESEKARAEYEA 593
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
784-1066 |
1.86e-07 |
|
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: 56.23 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 784 ISEFEKEIELLQA------QKIDVEKHVQSQKREMREKMsEITKQLLESYDieDVRSRL-SVEDLEHLNEdgelwfayeg 856
Cdd:TIGR02169 165 VAEFDRKKEKALEeleeveENIERLDLIIDEKRQQLERL-RREREKAERYQ--ALLKEKrEYEGYELLKE---------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 857 lKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEN-DINE-------SIRHEVTRLTSE----NMMI 924
Cdd:TIGR02169 232 -KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkKIKDlgeeeqlRVKEKIGELEAEiaslERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 925 PDFKQQISELEKQKQDLEIRLNEQAEKM----------KGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT--------- 985
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIeelereieeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelkdy 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 986 -KEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDV 1064
Cdd:TIGR02169 391 rEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
..
gi 2462545116 1065 HS 1066
Cdd:TIGR02169 471 LY 472
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
621-1067 |
2.45e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 621 LVEKLTSLAALRAgDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEK-LAKLQKHNSELETQKEQIQlKLQEKTEEL 699
Cdd:COG4913 230 LVEHFDDLERAHE-ALEDAREQIELLEPIRELAERYAAARERLAELEYLRaALRLWFAQRRLELLEAELE-ELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 700 KEKMDNLTKQLfDDVQKEERQrmlLEKsfELKTQDYEkQIQSLKEEIKALKDEK-------MQLQHLVEGEHVTSDGLKA 772
Cdd:COG4913 308 EAELERLEARL-DALREELDE---LEA--QIRGNGGD-RLEQLEREIERLERELeererrrARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 773 EVARLSKQVKTISEFEKEI-ELLQAQKIDVEKHVQSQKREMREKMSEItkQLLES------YDIEDVRSRLSvedlEHLN 845
Cdd:COG4913 381 EFAALRAEAAALLEALEEElEALEEALAEAEAALRDLRRELRELEAEI--ASLERrksnipARLLALRDALA----EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 846 ED-GELWF----------------AYEGL---------------KKATRVLESHFQSQKDCYEKeIEALNFKVVHLSQEI 893
Cdd:COG4913 455 LDeAELPFvgelievrpeeerwrgAIERVlggfaltllvppehyAAALRWVNRLHLRGRLVYER-VRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 894 NHL-QKLFREENDINESIRHEVTR-------------------LTSENMM--------------IP-------DFKQQIS 932
Cdd:COG4913 534 DSLaGKLDFKPHPFRAWLEAELGRrfdyvcvdspeelrrhpraITRAGQVkgngtrhekddrrrIRsryvlgfDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 933 ELEKQKQDLEIRLNE---QAEKMKGKLEELSNQ---LHRSQEEEGTQRKALEAQNEIHTKEKEklidkIQEMQEASDHLK 1006
Cdd:COG4913 614 ALEAELAELEEELAEaeeRLEALEAELDALQERreaLQRLAEYSWDEIDVASAEREIAELEAE-----LERLDASSDDLA 688
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 1007 KQfetesevkcnfRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSS 1067
Cdd:COG4913 689 AL-----------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
536-951 |
2.63e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 536 VRSLYQLIRMATITMQAYSRGFLARRRYRKMLEEHKAVILQkyarawlARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQN 615
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-------LREELEKLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 616 KENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEK-GKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQE 694
Cdd:COG4717 146 ERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELE-EAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 695 KTEELKEKMDNLTKQLFDDVQKEERQRMLLEK-------SFELKTQDYEKQIQSLKEEIKA---------LKDEKMQLQH 758
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLliaaallALLGLGGSLLSLILTIAGVLFLvlgllallfLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 759 LVEGEHVTSDGLKAEVARLS-KQVKTISEFEKEIELLQAQK-IDVEKHVQSQKREMREKMSEITKQLLESyDIEDVRSRL 836
Cdd:COG4717 301 GKEAEELQALPALEELEEEElEELLAALGLPPDLSPEELLElLDRIEELQELLREAEELEEELQLEELEQ-EIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 837 SVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKvvHLSQEINHLQ-KLFREENDINEsIRHEVT 915
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEeELEELEEELEE-LREELA 456
|
410 420 430
....*....|....*....|....*....|....*.
gi 2462545116 916 RLTSENMMIPDfKQQISELEKQKQDLEIRLNEQAEK 951
Cdd:COG4717 457 ELEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
603-983 |
3.13e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAElEKAATHRRNYEEKGKRYRDAVEEKLaKLQKHNSELE 682
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKI-KAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 683 TQKEQIQLKLQE-----KTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEkmQLQ 757
Cdd:PTZ00121 1631 EKKKVEQLKKKEaeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE--ELK 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 758 HLVEGEHVTSDGL-KAEVARLSKQVKTISEFEKEIELLQAQKIDVE--KHVQSQKREMREKMSEITKQ----LLESYDIE 830
Cdd:PTZ00121 1709 KKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekKKIAHLKKEEEKKAEEIRKEkeavIEEELDEE 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 831 DVRSRLSVE-DLEHLNEDGELwfAYEGLKKATRVLeshfQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINES 909
Cdd:PTZ00121 1789 DEKRRMEVDkKIKDIFDNFAN--IIEGGKEGNLVI----NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 910 IRHEVTRLTSENMMIPDFKQQISELEKQKQ----DLEIRLNEQaeKMKGKLEELSNQlhRSQEEEGTQRKALEAQNEI 983
Cdd:PTZ00121 1863 DGNKEADFNKEKDLKEDDEEEIEEADEIEKidkdDIEREIPNN--NMAGKNNDIIDD--KLDKDEYIKRDAEETREEI 1936
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
603-756 |
3.69e-07 |
|
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: 53.00 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKEnhgLVEKLTSLAALRAgdveKIQKLEAELEKAATHRRNYEEKGKRYRDAVEekLAKLQKhnsELE 682
Cdd:COG1579 32 ELAELEDELAALEAR---LEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRNNKE--YEALQK---EIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 683 TQKEQIQlKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQL 756
Cdd:COG1579 100 SLKRRIS-DLEDEILELMERIEELEEEL----AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
625-822 |
5.26e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 625 LTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMD 704
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-KLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 705 NLTKQL---FDDVQKEERQRMLLE-----KSFE--LKTQDYEKQI----QSLKEEIKALKDEKMQLQHLVEGEHVTSDGL 770
Cdd:COG3883 83 ERREELgerARALYRSGGSVSYLDvllgsESFSdfLDRLSALSKIadadADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 771 KAEVARLSKQV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQ 822
Cdd:COG3883 163 KAELEAAKAELeAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
607-1037 |
9.53e-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: 53.80 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 607 LQKKLEDQNKENHGLVEKLTSLAALRAGDVEkiqkLEAELEKAATHRR------NYEEKGKRYRDAVEEKLAKLQKHNSE 680
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARELEELSARESD----LEQDYQAASDHLNlvqtalRQQEKIERYQEDLEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 681 LETQKEQiQLKLQEKTEELKEKMDNLTKQLfDDVQK--EERQRMLLEksfelktqdYEKQIQSLKEEikalkdekmqlQH 758
Cdd:COG3096 370 VEEAAEQ-LAEAEARLEAAEEEVDSLKSQL-ADYQQalDVQQTRAIQ---------YQQAVQALEKA-----------RA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 759 LVEGEHVTSDGLKAEVARLSKQVKTISEfekeiELLQA-QKIDVEkhvQSQKREMREKMseitkQLLESYDIEDVRSRls 837
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATE-----EVLELeQKLSVA---DAARRQFEKAY-----ELVCKIAGEVERSQ-- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 838 vedlehlnedgelwfAYEglkKATRVLESHfQSQKDCYEKEiEALNFKVVHLSQEINHLQKLFREENDINESIRHEVtrl 917
Cdd:COG3096 493 ---------------AWQ---TARELLRRY-RSQQALAQRL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL--- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 918 tSENMMIPDFKqqiSELEKQKQDLEIRLNEQAEKmkgkleelSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLiDKIQE 997
Cdd:COG3096 550 -DAAEELEELL---AELEAQLEELEEQAAEAVEQ--------RSELRQQLEQLRARIKELAARAPAWLAAQDAL-ERLRE 616
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462545116 998 M--------QEASDHLKKQFETESEVKcnfrQEASRLTLENRDLEEEL 1037
Cdd:COG3096 617 QsgealadsQEVTAAMQQLLEREREAT----VERDELAARKQALESQI 660
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
686-1033 |
1.36e-06 |
|
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: 52.84 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 686 EQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERqrmlleKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHV 765
Cdd:pfam09731 44 EEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTG------ESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 766 TSDglKAEVARLSKQVKTISEFEKEIELLQAQ--------KIDVEKHVQSQKREM------REKMSEITKQLLESYDIED 831
Cdd:pfam09731 118 QLP--KSEQEKEKALEEVLKEAISKAESATAVakeakddaIQAVKAHTDSLKEASdtaeisREKATDSALQKAEALAEKL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 832 VRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIR 911
Cdd:pfam09731 196 KEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 912 HEVTRLTSE-NMMIPDFKQQISELEKQKQDL----EIRLNEQAEKMKGKLEELSNQL------HRSQEEEGTQRKALEAQ 980
Cdd:pfam09731 276 EDNLLSNDDlNSLIAHAHREIDQLSKKLAELkkreEKHIERALEKQKEELDKLAEELsarleeVRAADEAQLRLEFERER 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 981 NEIHTKEKEKLIDKIQEMQEA-SDHLKKQFET-ESEVKCNFRQEASRLTLENRDL 1033
Cdd:pfam09731 356 EEIRESYEEKLRTELERQAEAhEEHLKDVLVEqEIELQREFLQDIKEKVEEERAG 410
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
605-970 |
1.42e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.52 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 605 QRLQKKLEDQNKENHGLVEKLTSLAALRagDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVE--EKLAKLQKHNSELE 682
Cdd:TIGR01612 1325 KELQKNLLDAQKHNSDINLYLNEIANIY--NILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDksEKLIKKIKDDINLE 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 683 TQKEQIQLKLQE-------------KTEELKEKMDNLTkqLFDDVQKEERQRMLLEKSFEL---KTQ------------D 734
Cdd:TIGR01612 1403 ECKSKIESTLDDkdidecikkikelKNHILSEESNIDT--YFKNADENNENVLLLFKNIEMadnKSQhilkikkdnatnD 1480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 735 YEKQIQSLKEEI---KALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQV------KTISEFEKEIELLQAQKIDVEKHV 805
Cdd:TIGR01612 1481 HDFNINELKEHIdksKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYsalaikNKFAKTKKDSEIIIKEIKDAHKKF 1560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 806 QSQKREMREKMSEITKqllESYDIEDvrsrlsveDLEHLNEDGElwfAYEGLKKATRVLESHF-------QSQKDCYeKE 878
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKK---EKFRIED--------DAAKNDKSNK---AAIDIQLSLENFENKFlkisdikKKINDCL-KE 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 879 IEALNFKVVHLSqeINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEE 958
Cdd:TIGR01612 1626 TESIEKKISSFS--IDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIE 1703
|
410
....*....|..
gi 2462545116 959 LSNQLHRSQEEE 970
Cdd:TIGR01612 1704 KIKEIAIANKEE 1715
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
608-898 |
2.10e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 51.35 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 608 QKKLEDqNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAathrrnyEEK---GKRYRDAVEEKLAKLQKHNSELETQ 684
Cdd:pfam15905 66 QKNLKE-SKDQKELEKEIRALVQERGEQDKRLQALEEELEKV-------EAKlnaAVREKTSLSASVASLEKQLLELTRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 685 KEQIQLKLQEKTEelKEKMDNLTKQLF---DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVE 761
Cdd:pfam15905 138 NELLKAKFSEDGT--QKKMSSLSMELMklrNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 762 GEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQllesydIEDVRSRLSVedL 841
Cdd:pfam15905 216 EEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ------IKDLNEKCKL--L 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 842 EHLNEDgelwfayeglkkatrvLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQK 898
Cdd:pfam15905 288 ESEKEE----------------LLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
636-978 |
2.13e-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: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 636 VEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQ 715
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 716 KEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKdekmqlqhlvegehvtsDGLKAEVARLSKQVKTISEfEKEIELLQ 795
Cdd:COG5185 315 EEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQ-----------------ESLTENLEAIKEEIENIVG-EVELSKSS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 796 AQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDgelwfayegLKKATRVLEShFQSQKDCY 875
Cdd:COG5185 377 EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQ---------IEQATSSNEE-VSKLLNEL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 876 EKEIEalnfKVVHLSQEiNHLQKLFREENDINESIRHEVTRLTSENMMIpdfKQQISELEKQKQDLEIRLNEQAEKMKGK 955
Cdd:COG5185 447 ISELN----KVMREADE-ESQSRLEEAYDEINRSVRSKKEDLNEELTQI---ESRVSTLKATLEKLRAKLERQLEGVRSK 518
|
330 340
....*....|....*....|...
gi 2462545116 956 LEELSNQLHRSQEEEGTQRKALE 978
Cdd:COG5185 519 LDQVAESLKDFMRARGYAHILAL 541
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
604-1055 |
2.24e-06 |
|
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: 52.48 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 604 VQRLQKKLEDQNKEnhgLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR---DAVEEKLAKLQKHNSE 680
Cdd:pfam01576 403 SEHKRKKLEGQLQE---LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSkdvSSLESQLQDTQELLQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 681 LETQK----------EQIQLKLQEKTEELKEKMDNLTK-------QLFDDVQKEERQRMLLEKSFELK---TQDYEKQIQ 740
Cdd:pfam01576 480 ETRQKlnlstrlrqlEDERNSLQEQLEEEEEAKRNVERqlstlqaQLSDMKKKLEEDAGTLEALEEGKkrlQRELEALTQ 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 741 SLKEEIKA---LKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMS 817
Cdd:pfam01576 560 QLEEKAAAydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAL 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 818 EITKQLLESYD----IEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQS---QKDCYEKEIEA-----LNFK 885
Cdd:pfam01576 640 SLARALEEALEakeeLERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEmktQLEELEDELQAtedakLRLE 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 886 VVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNE-----------------Q 948
Cdd:pfam01576 720 VNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqidaankgreeavkQ 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 949 AEKMKGKLEELSNQL---HRSQEEEGTQRKaleaQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETE-----SEVKCN-- 1018
Cdd:pfam01576 800 LKKLQAQMKDLQRELeeaRASRDEILAQSK----ESEKKLKNLEAELLQLQEDLAASERARRQAQQErdelaDEIASGas 875
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462545116 1019 ----FRQEASRLTLENRDLEEELD--------MKDRViKKLQDQVKTLS 1055
Cdd:pfam01576 876 gksaLQDEKRRLEARIAQLEEELEeeqsntelLNDRL-RKSTLQVEQLT 923
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
609-1086 |
2.36e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 609 KKLEDQNKENHGLVEKLTSL--AALRAGDVEKIQKLE--AELEKAATHRRNYEEK----GKRYRDAVEEKLAKLQKHNSE 680
Cdd:PTZ00121 1098 GKAEEAKKTETGKAEEARKAeeAKKKAEDARKAEEARkaEDARKAEEARKAEDAKrveiARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 681 LETQKEQIQLKlqeKTEELKEKmdnltkqlfDDVQKEERQRMLLE--KSFELKTQDYEKQIQSLKEEIKALKDE----KM 754
Cdd:PTZ00121 1178 AEAARKAEEVR---KAEELRKA---------EDARKAEAARKAEEerKAEEARKAEDAKKAEAVKKAEEAKKDAeeakKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 755 QLQHLVEGEHVTSDGLKAEVARLSKQVKTiSEFEKEIELLQAQkiDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRS 834
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKADELKKAE--EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 835 RLSvedlEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKeiealnfkvvhlSQEINHLQKLFREEndinESIRHEV 914
Cdd:PTZ00121 1323 KAE----EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA------------AEEKAEAAEKKKEE----AKKKADA 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 915 TRLTSEnmmipdfkqqiselEKQKQDleiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDK 994
Cdd:PTZ00121 1383 AKKKAE--------------EKKKAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 995 IQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPK--- 1071
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkad 1525
|
490
....*....|....*
gi 2462545116 1072 EYLGMLQYKREDEAK 1086
Cdd:PTZ00121 1526 EAKKAEEAKKADEAK 1540
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
672-882 |
2.69e-06 |
|
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: 52.07 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 672 AKLQKHNSELETQKEQIQLKLQEKTEELKEKmdnltkqlFDDVQKEERQRMLLEKSFELKtqDYEKQIQSLKEEIKALKD 751
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEE--------LDKLAEELSARLEEVRAADEA--QLRLEFEREREEIRESYE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 752 EKMQLQhLVEGEHVTSDGLKAEVArlskqvktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsydIED 831
Cdd:pfam09731 364 EKLRTE-LERQAEAHEEHLKDVLV------------EQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKG---LEK 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 832 VRSRLSVEDLEHLNEDgELWFAYEGLKKATRvlESHFQSQKDCYEKEIEAL 882
Cdd:pfam09731 428 ATSSHSEVEDENRKAQ-QLWLAVEALRSTLE--DGSADSRPRPLVRELKAL 475
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
668-1086 |
3.03e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.97 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 668 EEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNL------------TKQLFDDVQKEERQRMLLEKsfelKTQDY 735
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqdeesdLERLKEEIEKSSKQRAMLAG----ATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 736 EKQIQSLKEEI--------------KALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEF----EKEIELLQAQ 797
Cdd:TIGR00606 666 SQFITQLTDENqsccpvcqrvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrQSIIDLKEKE 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 798 KIDVEKHVQSQKREMREKMSEITKQ--LLESYDIEDVRSRLSVED------LEHLNEDGELWFAYEGLKKATRVLESHFQ 869
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQetLLGTIMPEEESAKVCLTDvtimerFQMELKDVERKIAQQAAKLQGSDLDRTVQ 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 870 SQKdcyeKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQA 949
Cdd:TIGR00606 826 QVN----QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 950 EKMKGKLEE---LSNQLHRSQEEEGTQRKALEAQNEIHTKE----KEKLIDKIQEM-------QEASDHLKKQFETE--- 1012
Cdd:TIGR00606 902 REIKDAKEQdspLETFLEKDQQEKEELISSKETSNKKAQDKvndiKEKVKNIHGYMkdienkiQDGKDDYLKQKETElnt 981
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 1013 ---SEVKCNFRQEasRLTLENRDLEEELDMKDRVIKKLQDQVkTLSKTIGKANDVHSSsgPKEYLGMLQYKREDEAK 1086
Cdd:TIGR00606 982 vnaQLEECEKHQE--KINEDMRLMRQDIDTQKIQERWLQDNL-TLRKRENELKEVEEE--LKQHLKEMGQMQVLQMK 1053
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
637-1037 |
4.23e-06 |
|
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: 51.71 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 637 EKIQKLEAELEKAathrrnyeekgKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKT------EELKEKMDNlTKQL 710
Cdd:pfam01576 5 EEMQAKEEELQKV-----------KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcaeaEEMRARLAA-RKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 711 FDDV---------QKEER-QRMLLEKsfelktQDYEKQIQSLKEEIKALKDEKMQLQHlvegEHVTSDGlkaevarlskq 780
Cdd:pfam01576 73 LEEIlhelesrleEEEERsQQLQNEK------KKMQQHIQDLEEQLDEEEAARQKLQL----EKVTTEA----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 781 vkTISEFEKEIELLQAQKIDVEKhvqsQKREMREKMSEITKQLLESYDIEDVRSRLS------VEDLE-HLNEDGELWFA 853
Cdd:pfam01576 132 --KIKKLEEDILLLEDQNSKLSK----ERKLLEERISEFTSNLAEEEEKAKSLSKLKnkheamISDLEeRLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 854 YEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREE----NDINESIRHEVTRLTSENMMIPDFKQ 929
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEEtaqkNNALKKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 930 QISELEKQKQDLEirlnEQAEKMKGKLEE------LSNQLHRSQEEEGTQ-RKALEAQNEIHtkeKEKLIDKIQEMQEAS 1002
Cdd:pfam01576 286 ARNKAEKQRRDLG----EELEALKTELEDtldttaAQQELRSKREQEVTElKKALEEETRSH---EAQLQEMRQKHTQAL 358
|
410 420 430
....*....|....*....|....*....|....*
gi 2462545116 1003 DHLKKQFETESEVKCNFRQEASRLTLENRDLEEEL 1037
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
599-986 |
5.70e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQKKLEDQNKEnhglvekLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEklakLQKHN 678
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQ-------LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR----LQDLT 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 679 SELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLK--EEIKALKDEKMQ- 755
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsiRVLPKELLASRQl 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 756 ----LQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQ----AQKIDVEKHVQSQKREMREKMSEITKQLLESY 827
Cdd:TIGR00618 681 alqkMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEnassSLGSDLAAREDALNQSLKELMHQARTVLKART 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 828 DIEDVRSRLSVEDLEHLNE----DGELWF---AYEGLKKATRVLESHFQSQKDCYEkeiEALNFKVVHLSQEINHLQKLF 900
Cdd:TIGR00618 761 EAHFNNNEEVTAALQTGAElshlAAEIQFfnrLREEDTHLLKTLEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRL 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 901 REENDINESIRHEVTRLTsenmmipDFKQQISELEKQKQDLeIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQ 980
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYE-------ECSKQLAQLTQEQAKI-IQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLA 909
|
....*.
gi 2462545116 981 NEIHTK 986
Cdd:TIGR00618 910 NQSEGR 915
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
584-749 |
5.83e-06 |
|
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: 51.21 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 584 ARRRFQSIRRFVLNiqLTYRVQRLQKKLEDQNKENHGLV-------EKLTSLAALRAGDVEKIQKLEAELEKA------- 649
Cdd:TIGR02168 808 LRAELTLLNEEAAN--LRERLESLERRIAATERRLEDLEeqieelsEDIESLAAEIEELEELIEELESELEALlnerasl 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 650 ----ATHRRNYEEKGKRYRDaVEEKLAKLQKHNSELETQKEQIQLKLQekteELKEKMDNLTKQLFDDVQKEERQRMLLE 725
Cdd:TIGR02168 886 eealALLRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLE----GLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
170 180
....*....|....*....|....
gi 2462545116 726 KSFELKTQDYEKQIQSLKEEIKAL 749
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
603-846 |
6.72e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSL----AALRAGDVEKIQKLEAELEKAatHRRNYEEKGKRYRdaVEEKLAKLQKHN 678
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELlkelEELGFESVEELEERLKELEPF--YNEYLELKDAEKE--LEREEKELKKLE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 679 SELETQKEQIQLKLQEkTEELKEKMDNLtKQLFDDVQKEERQRMLLEKSFELKtqdyekqiqSLKEEIKALKDEKmqlqh 758
Cdd:PRK03918 626 EELDKAFEELAETEKR-LEELRKELEEL-EKKYSEEEYEELREEYLELSRELA---------GLRAELEELEKRR----- 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 759 lvegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEkhvqsqkrEMREKMSEItKQLLESYDIEDVrSRLSV 838
Cdd:PRK03918 690 ---------EEIKKTLEKLKEELEEREKAKKELEKLEKALERVE--------ELREKVKKY-KALLKERALSKV-GEIAS 750
|
....*...
gi 2462545116 839 EDLEHLNE 846
Cdd:PRK03918 751 EIFEELTE 758
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
628-823 |
6.97e-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: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 628 LAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQL------KLQEKTEELKE 701
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelaALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 702 KMDNLTKQLfdDVQKEERQRMLLeKSFELKTQDYEKQIQSLKEEIKALKDEKMqLQHLVEGEHVTSDGLKAEVARLSKQV 781
Cdd:COG4942 91 EIAELRAEL--EAQKEELAELLR-ALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462545116 782 KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQL 823
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
603-764 |
6.97e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 50.46 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLtSLAALRAGDVEkiQKLEaELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 682
Cdd:pfam05622 305 RLTELQQLLEDANRRKNELETQN-RLANQRILELQ--QQVE-ELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 683 TQKEQI-------QLKLQEKTEELKEkmdNLTKQLFDDVQKEERQRMLLEKSFE-LKTQDyEKQIQSLKEEIKALKD--- 751
Cdd:pfam05622 381 KKKEQIeelepkqDSNLAQKIDELQE---ALRKKDEDMKAMEERYKKYVEKAKSvIKTLD-PKQNPASPPEIQALKNqll 456
|
170
....*....|...
gi 2462545116 752 EKMQLQHLVEGEH 764
Cdd:pfam05622 457 EKDKKIEHLERDF 469
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
256-365 |
9.30e-06 |
|
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: 47.34 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 256 NTSFVIQHFAD-------KVEYKCEGFLEKNRDTVYDMLVEILraskfhlcanffqenptppsPFGSMITVksAKQVIKP 328
Cdd:cd01363 68 TMKGVIPYLASvafnginKGETEGWVYLTEITVTLEDQILQAN--------------------PILEAFGN--AKTTRNE 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462545116 329 NS----KHFRTTV---GS-KFRSSLYLLMETLNATTPHYVRCIKP 365
Cdd:cd01363 126 NSsrfgKFIEILLdiaGFeIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
601-815 |
1.13e-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: 49.38 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 601 TYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSE 680
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 681 LETQKEQI--QLKLQEKTEELKEKMDNLTKQLFDDVQKeeRQRMLLEKSFELKTQDYE-----KQIQSLKEEIKALKDEK 753
Cdd:COG4942 99 LEAQKEELaeLLRALYRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEElradlAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 754 MQLQHLVEGEHVTSDGLKAEVARLSKQV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREK 815
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
668-1015 |
1.30e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.69 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 668 EEKLAKLQKHNSELETQKEqiqlKLQEKTEELKE----------KMDNLTKQLfdDVQKEERQRmlLEKS---FELKTQD 734
Cdd:pfam05622 20 DQQVSLLQEEKNSLQQENK----KLQERLDQLESgddsgtpggkKYLLLQKQL--EQLQEENFR--LETArddYRIKCEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 735 YEKQI----------QSLKEEIKALKDEKMQLQHlvegehvTSDGLK---AEVARLSKQVKTISEFEKEIELLQ------ 795
Cdd:pfam05622 92 LEKEVlelqhrneelTSLAEEAQALKDEMDILRE-------SSDKVKkleATVETYKKKLEDLGDLRRQVKLLEernaey 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 796 -AQKIDVEK----------HVQSQKREMRE---KMSEIT----------KQLLESYD-IEDVRSRLSVE--DLEHLNEDG 848
Cdd:pfam05622 165 mQRTLQLEEelkkanalrgQLETYKRQVQElhgKLSEESkkadklefeyKKLEEKLEaLQKEKERLIIErdTLRETNEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 849 ELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNF-----------KVVHLSQEINHLQKLFREENDINESIRhEVTRL 917
Cdd:pfam05622 245 RCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIreklirlqhenKMLRLGQEGSYRERLTELQQLLEDANR-RKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 918 TSENMMIpdfKQQISELEKQKQDLEIRLNEQAEK------MKGKLEELSNQLHRSQEEEGTQRKALE-----AQNEIHTK 986
Cdd:pfam05622 324 ETQNRLA---NQRILELQQQVEELQKALQEQGSKaedsslLKQKLEEHLEKLHEAQSELQKKKEQIEelepkQDSNLAQK 400
|
410 420 430
....*....|....*....|....*....|..
gi 2462545116 987 E---KEKLIDKIQEMQEASDHLKKQFETESEV 1015
Cdd:pfam05622 401 IdelQEALRKKDEDMKAMEERYKKYVEKAKSV 432
|
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1109-1388 |
1.54e-05 |
|
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain.
Pssm-ID: 271256 Cd Length: 366 Bit Score: 48.81 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1109 PAHILFMCVRYADS-----------LNDANMLKSLMNSTINGIKQVVKEHLE--------------DFEMLSFWLSNT-- 1161
Cdd:cd15472 25 PAFLLCLCIQHSAThfepghfgkllLKIAKRIQEIVWEKTKELAEKQPEHQDpaslsllsiaelapDLQPLLFWMSNSie 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1162 --CHFLNCLKQYSGE-EEFMKHNSPQQNKNCLNNfDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIvPGMLE------- 1231
Cdd:cd15472 105 llYFIQQKVPLYEQSmEEELDVGSKESLLSSTLT-ASEEAMTVLEEVIMYTFQQCVYYLTKTLYVAL-PALLDsnpftae 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1232 -YESLQGISGLkPTGFRKrsssiddtdgytMTSVLQ---QLsyfyTTMCQngLDPELVRQAVKQLFFLIGAVTLNSLFLR 1307
Cdd:cd15472 183 eRESWSGGSRL-PEGVRR------------VLEIYQatlDL----LRQYQ--VHPEIASQMFAYLFFFSNASLFNQLMEK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 1308 KDMCSC---RKGMQIRCNISYLEEWLKDKNLqNSLAKETLEPLSQAAWLLQVKKTT--DSDAKEIYERCTSLSAVQIIKI 1382
Cdd:cd15472 244 GSGGGFfqwSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQllQMSWSSLRAEFPALNPAQLHHL 322
|
....*.
gi 2462545116 1383 LNSYTP 1388
Cdd:cd15472 323 LRQYQL 328
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
876-1010 |
1.61e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 876 EKEIEALNFKVVHLSQEINHLQKLFRE-ENDInESIRHEVTRLTSENMMIPDFKQ------QISELEKQKQDLE---IRL 945
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRlELEI-EEVEARIKKYEEQLGNVRNNKEyealqkEIESLKRRISDLEdeiLEL 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545116 946 NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEA-SDHLKKQFE 1010
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLALYE 181
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
629-790 |
1.72e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 629 AALRAGDVEKIQKLEAELEKAATH-RRNYEEKGKRYRDaVEEKLAKLQKHNSELEtqkeqiqlklqEKTEELKEKMDNLT 707
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHeERELTEEEEEIRR-LEEQVERLEAEVEELE-----------AELEEKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 708 KQLfDDVQKEERQRMLLEKsfELKTQDYE-----KQIQSLKEEIKALKDEKMQLQHLVEGEHvtSDGLKAevarlskqVK 782
Cdd:COG2433 448 REL-SEARSEERREIRKDR--EISRLDREierleRELEEERERIEELKRKLERLKELWKLEH--SGELVP--------VK 514
|
....*...
gi 2462545116 783 TISEFEKE 790
Cdd:COG2433 515 VVEKFTKE 522
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
891-1058 |
1.73e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 891 QEINHLQKLFREENDINEsIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQ 967
Cdd:COG1579 4 EDLRALLDLQELDSELDR-LEHRLKELPAE---LAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 968 EEEGTQR-----KALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQF-ETESEVKcnfrQEASRLTLENRDLEEELDMKD 1041
Cdd:COG1579 80 EQLGNVRnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELaELEAELA----ELEAELEEKKAELDEELAELE 155
|
170
....*....|....*..
gi 2462545116 1042 RVIKKLQDQVKTLSKTI 1058
Cdd:COG1579 156 AELEELEAEREELAAKI 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
603-822 |
1.85e-05 |
|
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: 49.68 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSLAAlragDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 682
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 683 TQKEQIQLK---LQEKTEELKEKMDNLTKQLfddVQKEERQRMLLEKSFELKTQDYE--KQIQSLKEEIKALKDEKMQLQ 757
Cdd:TIGR02169 868 EELEELEAAlrdLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKRKRLSElkAKLEALEEELSEIEDPKGEDE 944
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 758 HLVEGEHVTSDgLKAEVARLSKQV--------KTISEFEkeiELLQAQKIDVEKH--VQSQKREMREKMSEITKQ 822
Cdd:TIGR02169 945 EIPEEELSLED-VQAELQRVEEEIralepvnmLAIQEYE---EVLKRLDELKEKRakLEEERKAILERIEEYEKK 1015
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
731-1002 |
2.00e-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: 48.61 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 731 KTQDYEKQIQSLKEEIKALKDEKMQLQhlvEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKR 810
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALK---KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 811 EMREKMSEITKQLLESYDIEDvRSRLsvedlehlnedgELWFAYEGLKKATRVLEshfqsqkdcYEKEIEAlnfkvvHLS 890
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGR-QPPL------------ALLLSPEDFLDAVRRLQ---------YLKYLAP------ARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 891 QEINHLQKLFREENDINESIRHEVTRLtsenmmipdfKQQISELEKQKQDLEIRLNEQaekmkgklEELSNQLHRSQEEE 970
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAEL----------EALLAELEEERAALEALKAER--------QKLLARLEKELAEL 211
|
250 260 270
....*....|....*....|....*....|..
gi 2462545116 971 GTQRKALEAQNEIHTKEKEKLIDKIQEMQEAS 1002
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
656-991 |
2.60e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 656 YEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfddvqKEERQRMLleksfelktqdy 735
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRD-ELNAQVKELREEAQEL---------REKRDELN------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 736 eKQIQSLKEEIKALKDEKMQLQHLVegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQaQKIDVEKHVQSQKREMREK 815
Cdd:COG1340 71 -EKVKELKEERDELNEKLNELREEL-------DELRKELAELNKAGGSIDKLRKEIERLE-WRQQTEVLSPEEEKELVEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 816 MSEITKQLlesydiedvrsrlsvEDLEHLNEdgelwfayegLKKATRVLESHFQSQKdcyeKEIEALNFKVVHLSQEINH 895
Cdd:COG1340 142 IKELEKEL---------------EKAKKALE----------KNEKLKELRAELKELR----KEAEEIHKKIKELAEEAQE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 896 L----QKLFREEndinESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNqLHRSQEEEG 971
Cdd:COG1340 193 LheemIELYKEA----DELRKEADELHKE---IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRA-LKREKEKEE 264
|
330 340
....*....|....*....|
gi 2462545116 972 TQRKALEAQNEIhtKEKEKL 991
Cdd:COG1340 265 LEEKAEEIFEKL--KKGEKL 282
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
594-757 |
2.65e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.88 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 594 FVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYeEKGKRYRDAVEEKLAK 673
Cdd:pfam15905 176 MAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 674 LQKHNSELetqkeqiQLKLQEKTEELKEKMDNLTKQLfdDVQKEERQRMLLEksFELKTQDYEKQIQSLKEEIKALKDEK 753
Cdd:pfam15905 255 KNDEIESL-------KQSLEEKEQELSKQIKDLNEKC--KLLESEKEELLRE--YEEKEQTLNAELEELKEKLTLEEQEH 323
|
....
gi 2462545116 754 MQLQ 757
Cdd:pfam15905 324 QKLQ 327
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
603-1087 |
2.66e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSL------AALRAGDV-EKIQKLEAELEKAATH----------------------- 652
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELlveqgrLQLQADRHqEHIRARDSLIQSLATRleldgfergpfserqiknfhtlv 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 653 RRNYEEKGK---RYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFE 729
Cdd:TIGR00606 400 IERQEDEAKtaaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 730 LKTQDYEKQIQSLKEEIKALKDEKMQLQHlvegEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQK 809
Cdd:TIGR00606 480 LRKAERELSKAEKNSLTETLKKEVKSLQN----EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIK 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 810 REMREKMSEI------TKQLLESYDIEDVRSRLSVEDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEI---- 879
Cdd:TIGR00606 556 SRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA---SLEQNKNHINNELESKEEQLSSYEDKLfdvc 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 880 --EALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLE 957
Cdd:TIGR00606 633 gsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 958 ELSNQLHRSQEE-EGTQRKALEAQNEIHTKEKEklidkIQEMQEASDHLKKQFEtesEVKCNFRQEASRLTLENRDLE-- 1034
Cdd:TIGR00606 713 STESELKKKEKRrDEMLGLAPGRQSIIDLKEKE-----IPELRNKLQKVNRDIQ---RLKNDIEEQETLLGTIMPEEEsa 784
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 1035 EELDMKDRVIKKLQDQVKTLSKTIGK-ANDVHSSSGPKEYLGMLQYKREDEAKL 1087
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIAQqAAKLQGSDLDRTVQQVNQEKQEKQHEL 838
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
734-1002 |
2.77e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 734 DYEKQIQSLKEEIKALKDEKMQLQHLVEgehvtsdGLKAEVARLSKQVKTISEfekeiellQAQKIdvekhvQSQKREMR 813
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELK-------ELAEKRDELNAQVKELRE--------EAQEL------REKRDELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 814 EKMSEITKQLLESYD-IEDVRSRLSV--EDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEALNfKVVHLS 890
Cdd:COG1340 71 EKVKELKEERDELNEkLNELREELDElrKELAELNKAGG---SIDKLRKEIERLEWRQQTEVLSPEEEKELVE-KIKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 891 QEINHLQKlfreENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQ---DLEIRLNEQAEKMKGKLEELSNQLHRSQ 967
Cdd:COG1340 147 KELEKAKK----ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQelhEEMIELYKEADELRKEADELHKEIVEAQ 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462545116 968 EEEGTQRKAL-EAQNEIHtkEKEKLIDKIQEMQEAS 1002
Cdd:COG1340 223 EKADELHEEIiELQKELR--ELRKELKKLRKKQRAL 256
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
591-748 |
3.23e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 591 IRRFVLNIQLTYRVQRLQKKLEDQNKEnhglVEKLTSLAALRAGdvEKIQKLEAELEKAATHRRNY----EEKGKRYRDA 666
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKE----AEAIKKEALLEAK--EEIHKLRNEFEKELRERRNElqklEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 667 VEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfddvQKEERQRmlLEKSFELkTQDYEKQI--QSLKE 744
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELE-QKQQELEKKEEELEEL--------IEEQLQE--LERISGL-TAEEAKEIllEKVEE 165
|
....
gi 2462545116 745 EIKA 748
Cdd:PRK12704 166 EARH 169
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
670-860 |
3.83e-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: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 670 KLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKqLFDDVQKEERQRmlleKSFELKTQDYEKQIQSLKEEIKAL 749
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEA-AKTELEDLEKEI----KRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 750 KDEK--MQLQHLVEgehvtsdGLKAEVARLSKQvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsy 827
Cdd:COG1579 86 RNNKeyEALQKEIE-------SLKRRISDLEDE---ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE-- 153
|
170 180 190
....*....|....*....|....*....|....
gi 2462545116 828 dIEDVRSRLSVEDLEHLNE-DGELWFAYEGLKKA 860
Cdd:COG1579 154 -LEAELEELEAEREELAAKiPPELLALYERIRKR 186
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
767-1008 |
4.57e-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: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 767 SDGLKAEVARLSKQVKTISEFEKEIELLQAQKidveKHVQSQKREMREKMSEITKQL--LESyDIEDVRSRLSVedlehl 844
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE----KALLKQLAALERRIAALARRIraLEQ-ELAALEAELAE------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 845 nedgelwfayegLKKATRVLESHFQSQKDCYEKEIEALnfkvvHLSQEINHLQKLFREEnDINESIRhevtRLTSENMMI 924
Cdd:COG4942 88 ------------LEKEIAELRAELEAQKEELAELLRAL-----YRLGRQPPLALLLSPE-DFLDAVR----RLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 925 PDFKQQISELEKQKQDLEiRLNEQAEKMKGKLEELsnqlhrsQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDH 1004
Cdd:COG4942 146 PARREQAEELRADLAELA-ALRAELEAERAELEAL-------LAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
....
gi 2462545116 1005 LKKQ 1008
Cdd:COG4942 218 LQQE 221
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
568-1037 |
4.81e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 568 EEHKAVILQKYARAWLARRRFQSIRRFvlniqltYRVQRlQKKLEDQNKENHGLVEKLTSLAAlragDVEKIQKLEAELE 647
Cdd:PRK04863 753 EELEKAVVVKIADRQWRYSRFPEVPLF-------GRAAR-EKRIEQLRAEREELAERYATLSF----DVQKLQRLHQAFS 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 648 K-AATHRrnyeekgkryrdAV------EEKLAKLQKHNSELETQKEQiqlkLQEKTEELKEKMDNLtKQLFDDVQKEERQ 720
Cdd:PRK04863 821 RfIGSHL------------AVafeadpEAELRQLNRRRVELERALAD----HESQEQQQRSQLEQA-KEGLSALNRLLPR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 721 RMLLEKsfelktQDYEKQIQSLKEEIKALKDEKMQL-QHlvegehvtsdglKAEVARLSKQVKTISEFEKEIELLQAQki 799
Cdd:PRK04863 884 LNLLAD------ETLADRVEEIREQLDEAEEAKRFVqQH------------GNALAQLEPIVSVLQSDPEQFEQLKQD-- 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 800 dvekHVQSQKREMREKMseitkqllESYDIEDVRSRlsvedLEHlnedgelwFAYEglkkatrvleshfQSQKDCYEKei 879
Cdd:PRK04863 944 ----YQQAQQTQRDAKQ--------QAFALTEVVQR-----RAH--------FSYE-------------DAAEMLAKN-- 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 880 EALNFKvvhLSQEINHLQklfREENDINESIRHEVTRLTSENMMIPDFK-------QQISELEKQKQDLEIRLNEQAE-K 951
Cdd:PRK04863 984 SDLNEK---LRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKssydakrQMLQELKQELQDLGVPADSGAEeR 1057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 952 MKGKLEELSNQLHRSQeeegTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENR 1031
Cdd:PRK04863 1058 ARARRDELHARLSANR----SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERR 1133
|
....*.
gi 2462545116 1032 DLEEEL 1037
Cdd:PRK04863 1134 LHRREL 1139
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
638-1048 |
5.16e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 638 KIQKLEAELEKAATHR----------RNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLT 707
Cdd:pfam10174 290 KIDQLKQELSKKESELlalqtkletlTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 708 -------------KQLFDDVQKEERQRMLLEKSFE-LKTQ--DYEKQIQSLKEEIKALkdekmqlqhlvEGEHVTSDglk 771
Cdd:pfam10174 370 dlteekstlageiRDLKDMLDVKERKINVLQKKIEnLQEQlrDKDKQLAGLKERVKSL-----------QTDSSNTD--- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 772 aevARLSKQVKTISEFEKEIELLQAQKidvekhvqsqKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELW 851
Cdd:pfam10174 436 ---TALTTLEEALSEKERIIERLKEQR----------EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 852 -----FAYEGLKKatrvlESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIRH---EVTRLTSENMm 923
Cdd:pfam10174 503 ehassLASSGLKK-----DSKLKSLEIAVEQKKEECS-KLENQLKKAHNAEEAVRTNPEINDRIRLleqEVARYKEESG- 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 924 ipdfKQQiSELEKQKQDLEIRLNEQAEKMK--GKLEELSNQLHRSQEEEGTQRKALeaQNEIHTKEKEKLID-KIQEMQE 1000
Cdd:pfam10174 576 ----KAQ-AEVERLLGILREVENEKNDKDKkiAELESLTLRQMKEQNKKVANIKHG--QQEMKKKGAQLLEEaRRREDNL 648
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462545116 1001 ASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQ 1048
Cdd:pfam10174 649 ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR 696
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
738-1054 |
5.22e-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: 47.91 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 738 QIQSLKEEIKALKDEKMQLQHLvegeHVtsdGLKAEVARLSKQVKTISEFEKEIELLQAQKIDvekhvqsqkrEMREKMS 817
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHL----HF---GYKSDETLIASRQEERQETSAELNQLLRTLDD----------QWKEKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 818 EITKQL-LESYDIEDVRSRLSVEDLEHLNedgelwFAYEGLKKATRVLES--HFQSQKDCYEKEIEALNFKVVHLSQEIN 894
Cdd:pfam12128 305 ELNGELsAADAAVAKDRSELEALEDQHGA------FLDADIETAAADQEQlpSWQSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 895 HLQKLFREEN-----DINE---SIRHEVTRLTSENMmiPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRS 966
Cdd:pfam12128 379 RRRSKIKEQNnrdiaGIKDklaKIREARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 967 Q--EEEGTQRKAleaqneihtkeKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEAS-RLTLENRDLEEELDMKDRV 1043
Cdd:pfam12128 457 TatPELLLQLEN-----------FDERIERAREEQEAANAEVERLQSELRQARKRRDQASeALRQASRRLEERQSALDEL 525
|
330
....*....|.
gi 2462545116 1044 IKKLQDQVKTL 1054
Cdd:pfam12128 526 ELQLFPQAGTL 536
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
599-798 |
5.58e-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: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKH- 677
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 678 ---------NSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKsfelKTQDYEKQIQSLKEEIKA 748
Cdd:COG4942 118 rqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEA----ERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462545116 749 LKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQK 798
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
606-910 |
5.94e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 606 RLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQK 685
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 686 EQIQLKLQEKTEELKEKMDNLT------KQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHL 759
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELEslqeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 760 VEG-EHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 838
Cdd:COG4372 163 QEElAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 839 EDLEHLNEDGElwfayEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 910
Cdd:COG4372 243 ELEEDKEELLE-----EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
700-969 |
6.19e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.84 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 700 KEKMDNLTKQL---FDDVQKEERQRMLLEKSFELKTQD-----------YEKQIQSLKEEIKALKDEKMQLQhlvegehV 765
Cdd:pfam00038 3 KEQLQELNDRLasyIDKVRFLEQQNKLLETKISELRQKkgaepsrlyslYEKEIEDLRRQLDTLTVERARLQ-------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 766 TSDGLKAEVARLSKQVKT-----------ISEFEKEIELLQAQKIDVEKHVQS-------QKREMREKMSEITKQLLESY 827
Cdd:pfam00038 76 ELDNLRLAAEDFRQKYEDelnlrtsaendLVGLRKDLDEATLARVDLEAKIESlkeelafLKKNHEEEVRELQAQVSDTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 828 DIEDVRSRLSVEdlehlnedgelwfayegLKKATRVLESHFQSQKDCYEKEIEAL-NFKVVHLSQEIN-HLQKLFREEND 905
Cdd:pfam00038 156 VNVEMDAARKLD-----------------LTSALAEIRAQYEEIAAKNREEAEEWyQSKLEELQQAAArNGDALRSAKEE 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 906 INESiRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEE 969
Cdd:pfam00038 219 ITEL-RRTIQSLEIE---LQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQE 278
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
908-1083 |
7.04e-05 |
|
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: 47.76 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 908 ESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKE 987
Cdd:TIGR02169 240 EAIERQLASLEEE---LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 988 KEKLIDKIQEMQEASDHLKKQFEtesevkcNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSS 1067
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIE-------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170
....*....|....*.
gi 2462545116 1068 SgpKEYLGMLQYKRED 1083
Cdd:TIGR02169 390 Y--REKLEKLKREINE 403
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
636-813 |
7.87e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 636 VEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKhnsELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvq 715
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQAIKEAKKEADEIIKEL----- 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 716 keerQRMLLEKSFELKTQDYEKQIQSLKEEIKAL---KDEKMQLQH-LVEGEHV--TSDGLKAEVARLSKQVKTISEF-- 787
Cdd:PRK00409 594 ----RQLQKGGYASVKAHELIEARKRLNKANEKKekkKKKQKEKQEeLKVGDEVkyLSLGQKGEVLSIPDDKEAIVQAgi 669
|
170 180 190
....*....|....*....|....*....|..
gi 2462545116 788 ------EKEIELLQAQKIDVEKHVQSQKREMR 813
Cdd:PRK00409 670 mkmkvpLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
805-1049 |
9.13e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 805 VQSQKREMREKMSEITKQL--LESYDIEDV----RSRLS--VEDLEHLNEDGElwFAYEGLKKATRVLESHFQSQK--DC 874
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIeeKEEKDLHERlnglESELAelDEEIERYEEQRE--QARETRDEADEVLEEHEERREelET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 875 YEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSE----NMMIPDFKQQISELEKQKQDLEIRL----- 945
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagldDADAEAVEARREELEDRDEELRDRLeecrv 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 946 -----NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKL--IDK-IQEMQEASDHLKKQFETESEVKC 1017
Cdd:PRK02224 336 aaqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIeeLEEeIEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270
....*....|....*....|....*....|..
gi 2462545116 1018 NFRQEASRLTLENRDLEEELDMKDRVIKKLQD 1049
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
933-1052 |
9.22e-05 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 43.37 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 933 ELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEaqneihtkEKEKLIDKIQEMQEASDHLKKQFETE 1012
Cdd:pfam20492 3 EAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEE--------EAERLEQKRQEAEEEKERLEESAEME 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462545116 1013 SEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVK 1052
Cdd:pfam20492 75 AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELE 114
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
673-989 |
9.50e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 673 KLQKHNSELETQKEQIQLKLQE-KTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKD 751
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 752 EKMQLqHLVEGEHVTSDGLKAEVARLSKQVKTIseFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLlESYDIEd 831
Cdd:TIGR00606 260 NLSKI-MKLDNEIKALKSRKKQMEKDNSELELK--MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQREL-EKLNKE- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 832 vRSRLSVEDLEHLNEDGELWFAYE-----GLKKATRVLESHFQSQKDCYEKEIEAlnfkvvhlSQEINHLQKLFRE-END 905
Cdd:TIGR00606 335 -RRLLNQEKTELLVEQGRLQLQADrhqehIRARDSLIQSLATRLELDGFERGPFS--------ERQIKNFHTLVIErQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 906 INESIRHEVTRLTSENMMIpdfKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT 985
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482
|
....
gi 2462545116 986 KEKE 989
Cdd:TIGR00606 483 AERE 486
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
597-823 |
1.18e-04 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 45.12 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 597 NIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLaalragdvekiqKLEAELEKAATHRrnyeeKGKRYRDaVEEKLAKLQK 676
Cdd:pfam17078 19 NLQLTVQSQNLLSKLEIAQQKESKFLENLASL------------KHENDNLSSMLNR-----KERRLKD-LEDQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 677 HNSELETQKEQIQLKLQEKTE---ELKEKMDNLTKQLFDDVQKEERQRmlleksfelktQDYEKQIQSLKEEIKALK-DE 752
Cdd:pfam17078 81 SYEELTESNKQLKKRLENSSAsetTLEAELERLQIQYDALVDSQNEYK-----------DHYQQEINTLQESLEDLKlEN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545116 753 KMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKE--IELLQ-----AQKIDVEKHVQSQKrEMREKMSEITKQL 823
Cdd:pfam17078 150 EKQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNknNKLLTkldslAQLLDLPSWLNLYP-ESRNKILEYAEKM 226
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
714-1055 |
1.26e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 714 VQKEERQRMLLEKSFELKTQDYEKQ----IQSLKEEIKALKDekmqLQHLVEGEHVTSDGLKAE---VARLSKQ--VKTI 784
Cdd:pfam10174 47 LRKEEAARISVLKEQYRVTQEENQHlqltIQALQDELRAQRD----LNQLLQQDFTTSPVDGEDkfsTPELTEEnfRRLQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 785 SEFE---KEIELLQAQKIDVEKHVQSQKREMrEKMSEITKQLLE----------SYDIEDVRSRLSVEDLEHLNE-DGEL 850
Cdd:pfam10174 123 SEHErqaKELFLLRKTLEEMELRIETQKQTL-GARDESIKKLLEmlqskglpkkSGEEDWERTRRIAEAEMQLGHlEVLL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 851 WFAYEGLKKATRVLESHFQSQKD-----CYEKEIEALNFKVVHLSQEINHLQ---KLFREENDINESIRH------EVTR 916
Cdd:pfam10174 202 DQKEKENIHLREELHRRNQLQPDpaktkALQTVIEMKDTKISSLERNIRDLEdevQMLKTNGLLHTEDREeeikqmEVYK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 917 LTSENMmipdfKQQISELekqKQDLEiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNE---IHTKEKEKLID 993
Cdd:pfam10174 282 SHSKFM-----KNKIDQL---KQELS-KKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQraaILQTEVDALRL 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 994 KIQEMQEASDHLKKQFETESEvkcnfrqEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLS 1055
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
673-1056 |
1.43e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 673 KLQKHNSELETQKEQI-------------QLKL----QEKTEELKEKMDNLTKQLFDDVQKE--------ERQRML---- 723
Cdd:PRK04778 26 RNYKRIDELEERKQELenlpvndelekvkKLNLtgqsEEKFEEWRQKWDEIVTNSLPDIEEQlfeaeelnDKFRFRkakh 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 724 LEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVarLSKQVK---TISEFEKEIELLQAQ--- 797
Cdd:PRK04778 106 EINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL--LANRFSfgpALDELEKQLENLEEEfsq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 798 ---------KIDVEKHVQSQKREM---REKMSEItKQLLESY---------DIEDVRSRLSVE--DLEHLNEDGELwfay 854
Cdd:PRK04778 184 fveltesgdYVEAREILDQLEEELaalEQIMEEI-PELLKELqtelpdqlqELKAGYRELVEEgyHLDHLDIEKEI---- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 855 EGLKKATRvleshfQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDinesIRHEVTRLtsenmmIPDFKQQISEL 934
Cdd:PRK04778 259 QDLKEQID------ENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVK----ARKYVEKN------SDTLPDFLEHA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 935 EKQKQDLEI---------RLN----EQAEKMKGKLEELSNQLHRSQEEEGTQRKAL-EAQNEIhtKEKEKLIDKIQEMQ- 999
Cdd:PRK04778 323 KEQNKELKEeidrvkqsyTLNeselESVRQLEKQLESLEKQYDEITERIAEQEIAYsELQEEL--EEILKQLEEIEKEQe 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545116 1000 EASDHLKKQFETESEVKCN---FRQEAS--RLTLENRDL----EEELDMKDRVIKKLQDQVKTLSK 1056
Cdd:PRK04778 401 KLSEMLQGLRKDELEAREKlerYRNKLHeiKRYLEKSNLpglpEDYLEMFFEVSDEIEALAEELEE 466
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
691-1065 |
1.45e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 691 KLQEKTEELKEKMDNLTKQLFD-DVQKEERQRMLLE--------KSFELKTQDYEKQIQSLKEEIKALKDEKmqlqhlve 761
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNiDYLEEKLKSSNLElenikkqiADDEKSHSITLKEIERLSIEYNNAMDDY-------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 762 gehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV----QSQKREMR-------EKMSEITKQLLESYDIE 830
Cdd:PRK01156 235 ------NNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNnyykELEERHMKiindpvyKNRNYINDYFKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 831 DVRSRLSvedlehlNEDGELWFAYEGLKKATrVLESHF------QSQKDCYEKEIEAL---NFKVVHLSQEINHLQKLFR 901
Cdd:PRK01156 309 NKKQILS-------NIDAEINKYHAIIKKLS-VLQKDYndyikkKSRYDDLNNQILELegyEMDYNSYLKSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 902 EENDINESIRHEVTRLTSENMMIPD-FKQQISELEKQKQDLEIR---LNEQAEKMKGKLEELSnqlhRSQEEEGTQRKAL 977
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDaIKKELNEINVKLQDISSKvssLNQRIRALRENLDELS----RNMEMLNGQSVCP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 978 EAQNEIHTKEKEKLIDKIQEmqEASDHLKKQFETESEVKC---NFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL 1054
Cdd:PRK01156 457 VCGTTLGEEKSNHIINHYNE--KKSRLEEKIREIEIEVKDideKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDI 534
|
410
....*....|.
gi 2462545116 1055 SKTIGKANDVH 1065
Cdd:PRK01156 535 KIKINELKDKH 545
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
924-1002 |
1.51e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 924 IPDFKQQISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1000
Cdd:COG3883 18 IQAKQKELSELQAELEAAQaelDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
..
gi 2462545116 1001 AS 1002
Cdd:COG3883 98 SG 99
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
669-798 |
1.93e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 669 EKLAK--LQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK--------- 737
Cdd:PRK12704 37 EEEAKriLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKreeelekke 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 738 -QIQSLKEEIKALKDE--KMQLQHLVEGEHVTsdGLKAEVAR--LSKQVK---------TISEFEKEIElLQAQK 798
Cdd:PRK12704 117 kELEQKQQELEKKEEEleELIEEQLQELERIS--GLTAEEAKeiLLEKVEeearheaavLIKEIEEEAK-EEADK 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
784-1001 |
2.39e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 784 ISEFEKEIELLQAQKidveKHVQSQKREMREKMSEITKQLLE-SYDIEDVRSRLSV--EDLEHLNEDgelwfayegLKKA 860
Cdd:COG3883 18 IQAKQKELSELQAEL----EAAQAELDALQAELEELNEEYNElQAELEALQAEIDKlqAEIAEAEAE---------IEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 861 TRVLESHFQSQkdcYEKeiealnfkvvhlSQEINHLQKLFrEENDINESIR--HEVTRLTS-ENMMIPDFKQQISELEKQ 937
Cdd:COG3883 85 REELGERARAL---YRS------------GGSVSYLDVLL-GSESFSDFLDrlSALSKIADaDADLLEELKADKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 938 KQDLEIRLNEqAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEA 1001
Cdd:COG3883 149 KAELEAKLAE-LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
558-1091 |
4.56e-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: 44.96 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 558 LARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAalragdvE 637
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS-------K 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 638 KIQKLEAE-----------------------------LEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQI 688
Cdd:pfam02463 258 QEIEKEEEklaqvlkenkeeekekklqeeelkllakeEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 689 QLKLQEKTE--ELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQdYEKQIQSLKEEIKALKDEKMQ----LQHLVEG 762
Cdd:pfam02463 338 EELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE-RLSSAAKLKEEELELKSEEEKeaqlLLELARQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 763 EHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKmseITKQLLESYDIEDVRSRLSVEDLE 842
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK---SEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 843 HLNEDGELWFAYEGLKKATRVLESHFQSQKDCYE------KEIEALNFKVVHLS----------QEINHLQKLFREENDI 906
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGGRIISAhgrlgdLGVAVENYKVAISTavivevsataDEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 907 NESIRHEVTRLTSENM-----MIPDFKQQISELEKQKQDLEIRLNEQAEK---MKGKLEELSNQLHRSQEEEGTQRKALE 978
Cdd:pfam02463 574 PLGARKLRLLIPKLKLplksiAVLEIDPILNLAQLDKATLEADEDDKRAKvveGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 979 AQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL---- 1054
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEaqdk 733
|
570 580 590
....*....|....*....|....*....|....*..
gi 2462545116 1055 SKTIGKANDVHSSSGPKEYLGMLQYKREDEAKLIQNL 1091
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
640-743 |
4.84e-04 |
|
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: 43.72 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 640 QKLEAELEKAATHRRnyEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEer 719
Cdd:cd16269 192 ALTEKEKEIEAERAK--AEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKE-- 267
|
90 100
....*....|....*....|....
gi 2462545116 720 QRMLLEKSFELKTQDYEKQIQSLK 743
Cdd:cd16269 268 QEALLEEGFKEQAELLQEEIRSLK 291
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
610-831 |
5.21e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.56 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 610 KLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE-TQKEQI 688
Cdd:pfam06008 41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFaLPSSDL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 689 QLKLQEKTEELKE-KMDNLTKQLFDDVQKEERQRMLLEKSfelktqdyEKQIQSLKEEIKALKDekmQLQHLVeGEHvtS 767
Cdd:pfam06008 121 SRMLAEAQRMLGEiRSRDFGTQLQNAEAELKAAQDLLSRI--------QTWFQSPQEENKALAN---ALRDSL-AEY--E 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 768 DGLKAEVARLSKQVKTISEFEkeiELLQAQKIDVEKHvQSQKREMREKMSEITKQLLESYDIED 831
Cdd:pfam06008 187 AKLSDLRELLREAAAKTRDAN---RLNLANQANLREF-QRKKEEVSEQKNQLEETLKTARDSLD 246
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
863-1060 |
5.54e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 863 VLESHFQSQKDCYEKEIEALNFKVvhlSQEINHLQKLFREENDINESIRHEVTRLTSEnmmipdfkqqISELEKQKQDLE 942
Cdd:PHA02562 188 MKIDHIQQQIKTYNKNIEEQRKKN---GENIARKQNKYDELVEEAKTIKAEIEELTDE----------LLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 943 I---RLNEQAEKMKGKLEELSNQLHR----------SQEEEGTQRKALEAQNEIH--TKEKEKLIDKIQEMQEASDHLKK 1007
Cdd:PHA02562 255 AalnKLNTAAAKIKSKIEQFQKVIKMyekggvcptcTQQISEGPDRITKIKDKLKelQHSLEKLDTAIDELEEIMDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 1008 QFETESEVKC---NFRQEASRLTLENRDLEEELD--MKDRV-----IKKLQDQVKTLSKTIGK 1060
Cdd:PHA02562 335 QSKKLLELKNkisTNKQSLITLVDKAKKVKAAIEelQAEFVdnaeeLAKLQDELDKIVKTKSE 397
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
908-1058 |
7.28e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 908 ESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSqEEEGTQRKALEAQNEIHTKE 987
Cdd:PRK02224 247 EERREELETLEAE---IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREELEDR 322
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 988 KEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1058
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
665-775 |
7.32e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 665 DAVEEKLAKLQKHNSELETQKEQI----QLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK--Q 738
Cdd:COG0542 407 DSKPEELDELERRLEQLEIEKEALkkeqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRygK 486
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462545116 739 IQSLKEEIKALKDEKMQLQHLVEgEHVTSDglkaEVA 775
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLR-EEVTEE----DIA 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
555-749 |
7.62e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 555 RGFLARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAG 634
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 635 DVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQI--QLKLQEKTEELKEKMDNLTKQLFD 712
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERleEELEEEALEEQLEAEREELLEELL 742
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462545116 713 DVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKAL 749
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
665-850 |
8.21e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 8.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 665 DAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvqkEERQRMLLEksFELKTQDYEKQIQSLKE 744
Cdd:PHA02562 191 DHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEI------EELTDELLN--LVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 745 EIKALKDEKMQLQ---HLVEGEHV---TSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV------QSQKREM 812
Cdd:PHA02562 263 AAAKIKSKIEQFQkviKMYEKGGVcptCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdefneqSKKLLEL 342
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462545116 813 REKMSEItKQLLESY-----DIEDVRSRLSVedlEHLNEDGEL 850
Cdd:PHA02562 343 KNKISTN-KQSLITLvdkakKVKAAIEELQA---EFVDNAEEL 381
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
599-842 |
8.39e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEE------KLA 672
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLE 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 673 KLQKHNSELETQKEQIQLKLQEKTEELKEKMDNL---TKQLFDDVQ---------KE-------------ERQRMLLEKS 727
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQdgkddylkqKEtelntvnaqleecEKHQEKINED 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 728 FELKTQDYEKQIQS------------LKEEIKALKDEKMqlQHLVEGEHVTSDGLKAEVARLSKQVKTIsefEKEIELLQ 795
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELK--QHLKEMGQMQVLQMKQEHQKLEENIDLI---KRNHVLAL 1074
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462545116 796 AQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLE 842
Cdd:TIGR00606 1075 GRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
736-951 |
9.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 736 EKQIQSLKEEIKALKDEKMQLQHLVegehvtsDGLKAEVARLSKQVKTIsefEKEIELLQAQKIDVEKHVQSQKREMREK 815
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEL-------DALQAELEELNEEYNEL---QAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 816 MSEITKQ----------------LLESYDIEDVRSRLSVedLEHLNE-DGELwfaYEGLKKATRVLEshfqSQKDCYEKE 878
Cdd:COG3883 85 REELGERaralyrsggsvsyldvLLGSESFSDFLDRLSA--LSKIADaDADL---LEELKADKAELE----AKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 879 IEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLtsenmmipdfKQQISELEKQKQDLEIRLNEQAEK 951
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA----------EAQLAELEAELAAAEAAAAAAAAA 218
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
637-828 |
9.39e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 637 EKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLTKQL----FD 712
Cdd:COG1340 29 EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD-ELNEKLNELREELDELRKELaelnKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 713 DVQKEERQRML--LEKSFELKTQDYEK------QIQSLKEEIKALKDEKMQLQHLVEgehvtsdgLKAEVARLSKQVkti 784
Cdd:COG1340 108 GGSIDKLRKEIerLEWRQQTEVLSPEEekelveKIKELEKELEKAKKALEKNEKLKE--------LRAELKELRKEA--- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462545116 785 SEFEKEIELL--QAQKIDVEKHVQSQKR-EMREKMSEITKQLLESYD 828
Cdd:COG1340 177 EEIHKKIKELaeEAQELHEEMIELYKEAdELRKEADELHKEIVEAQE 223
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
896-1054 |
9.56e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 896 LQKLFREENDINE---SIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLhRSQEEEGT 972
Cdd:COG3883 25 LSELQAELEAAQAeldALQAELEELNEE---YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA-RALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 973 QRKALE----------------AQNEIHTKEKEkLIDKIQEMQEASDHLKKQFETESEvkcNFRQEASRLTLENRDLEEE 1036
Cdd:COG3883 101 SVSYLDvllgsesfsdfldrlsALSKIADADAD-LLEELKADKAELEAKKAELEAKLA---ELEALKAELEAAKAELEAQ 176
|
170
....*....|....*...
gi 2462545116 1037 LDMKDRVIKKLQDQVKTL 1054
Cdd:COG3883 177 QAEQEALLAQLSAEEAAA 194
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
606-1042 |
9.88e-04 |
|
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: 44.01 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 606 RLQKKLEDQNKENHGLVEKLTSLaalragdvEKIQK----LEAElEKAATHRrNYEEKGKRYRDAvEEKLAKLQKHNSEL 681
Cdd:pfam01576 577 RLQQELDDLLVDLDHQRQLVSNL--------EKKQKkfdqMLAE-EKAISAR-YAEERDRAEAEA-REKETRALSLARAL 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 682 ETQKEQIQlKLQEKTEELKEKMDNLTKQLfDDVQKE----ERQRMLLEKSF-ELKTQdyekqIQSLKEEIKALKDEKMQL 756
Cdd:pfam01576 646 EEALEAKE-ELERTNKQLRAEMEDLVSSK-DDVGKNvhelERSKRALEQQVeEMKTQ-----LEELEDELQATEDAKLRL 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 757 QhlvegehVTSDGLKAEvarlskqvktiseFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQL---------LESy 827
Cdd:pfam01576 719 E-------VNMQALKAQ-------------FERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRaqavaakkkLEL- 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 828 DIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCY------EKEIEALNFKVVHLSQEINHLQKLFR 901
Cdd:pfam01576 778 DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILaqskesEKKLKNLEAELLQLQEDLAASERARR 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 902 EENDINESIRHEVTRLTSENMMIPDFKQQIS--------ELEKQKQDLEIrLNEQAEKMKGKLEELSNQL----HRSQEE 969
Cdd:pfam01576 858 QAQQERDELADEIASGASGKSALQDEKRRLEariaqleeELEEEQSNTEL-LNDRLRKSTLQVEQLTTELaaerSTSQKS 936
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 970 EGTqRKALEAQNeihtkeKEkLIDKIQEMqeasdhlkkqfetESEVKCNFRQEASRLTLENRDLEEELDMKDR 1042
Cdd:pfam01576 937 ESA-RQQLERQN------KE-LKAKLQEM-------------EGTVKSKFKSSIAALEAKIAQLEEQLEQESR 988
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
598-842 |
1.01e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 598 IQLTYRVQRLQKKLEDQNKENHGLVEKLTSlaalragdvEKIQKLEAELEKAATHRrnYEEKGkryrdaVEEKLAKLQKH 677
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALN---------EMIEKLKKEIDLEYTEA--VIAMG------LQERLENLREE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 678 NSELETQKEQIQLKLQEKTEELKEKMD-NLT--------KQLFDDVQKEERQRMLLE---KSFELKtQDYEKQIQS---- 741
Cdd:PLN03229 495 FSKANSQDQLMHPVLMEKIEKLKDEFNkRLSrapnylslKYKLDMLNEFSRAKALSEkksKAEKLK-AEINKKFKEvmdr 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 742 --LKEEIKALKDEKMQLQHLVEGEhvTSDGLKAEVARLSKQV-----KTISEFEKEIELLQAQKIDVEKHVQSQkrEMRE 814
Cdd:PLN03229 574 peIKEKMEALKAEVASSGASSGDE--LDDDLKEKVEKMKKEIelelaGVLKSMGLEVIGVTKKNKDTAEQTPPP--NLQE 649
|
250 260 270
....*....|....*....|....*....|..
gi 2462545116 815 KMS----EITKQLLESYDIEDVRSRLSVEDLE 842
Cdd:PLN03229 650 KIEslneEINKKIERVIRSSDLKSKIELLKLE 681
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
616-825 |
1.19e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 43.13 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 616 KENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAatHRRNYEEKGKRYRDAVEEKLAKLQKHNSELET--QKEQIQLKLQ 693
Cdd:pfam15742 107 KSQNSLQEKLAQEKSRVADAEEKILELQQKLEHA--HKVCLTDTCILEKKQLEERIKEASENEAKLKQqyQEEQQKRKLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 694 EKT-EELKEKMDNL----------TKQLFDDVQKEERQRMLLEKsfELKTQD-YEKQIQSLKEEIKALKDEK----MQLQ 757
Cdd:pfam15742 185 DQNvNELQQQVRSLqdkeaqlemtNSQQQLRIQQQEAQLKQLEN--EKRKSDeHLKSNQELSEKLSSLQQEKealqEELQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 758 HLV-----------EGEHVTSDGLKAEVARLSKQV----KTISEFEKEIELLQaQKIDVEKHVQSQKREMREKMSEITKQ 822
Cdd:pfam15742 263 QVLkqldvhvrkynEKHHHHKAKLRRAKDRLVHEVeqrdERIKQLENEIGILQ-QQSEKEKAFQKQVTAQNEILLLEKRK 341
|
...
gi 2462545116 823 LLE 825
Cdd:pfam15742 342 LLE 344
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
605-754 |
1.20e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 605 QRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQ 684
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKK 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 685 KEQIQLKLQEKTEELkEKMDNLTKQLFDDVQKEERQRmlleksfeLKTQDYE-KQIQSLKEEIKALKDEKM 754
Cdd:smart00787 227 LEELEEELQELESKI-EDLTNKKSELNTEIAEAEKKL--------EQCRGFTfKEIEKLKEQLKLLQSLTG 288
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
617-749 |
1.21e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 41.73 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 617 ENHGLVEKLTSLAALRAgdvEKIQKLEAELEKaathRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKT 696
Cdd:pfam06785 66 EKSFLEEKEAKLTELDA---EGFKILEETLEE----LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFR 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462545116 697 EELKEKMDNLTKQLFDDVQKEERQRMLLEKSFElKTQDYEKQIQSLKEEIKAL 749
Cdd:pfam06785 139 LESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD-QIENLESKVRDLNYEIKTL 190
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
928-1058 |
1.52e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 928 KQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSqEEEGTQRKALEAQNEIHTKEKEKLID----------KIQE 997
Cdd:pfam05667 334 EEELEELQEQLEDLE----SSIQELEKEIKKLESSIKQV-EEELEELKEQNEELEKQYKVKKKTLDllpdaeeniaKLQA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 998 MQEASD----HLKKQFET----------ESEVKCNFRQEASRLTLEN--------RDLEEELDMKDRVIKKLQDQVKTLS 1055
Cdd:pfam05667 409 LVDASAqrlvELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEikelrekiKEVAEEAKQKEELYKQLVAEYERLP 488
|
...
gi 2462545116 1056 KTI 1058
Cdd:pfam05667 489 KDV 491
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
645-1038 |
1.59e-03 |
|
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: 43.24 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 645 ELEKAathRRNYEEKGKRYRDAVEEKLAKLQ-----KHNSELETQ--KEQIQLKLQEKTEELKEKMDNLTKQL------F 711
Cdd:pfam01576 682 ELERS---KRALEQQVEEMKTQLEELEDELQatedaKLRLEVNMQalKAQFERDLQARDEQGEEKRRQLVKQVreleaeL 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 712 DDVQKEERQRMLLEKSFELKTQDYEKQIQSL----KEEIKALKDEKMQLQHL---VEGEHVTSDGLKAEVARLSKQVKTI 784
Cdd:pfam01576 759 EDERKQRAQAVAAKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQMKDLqreLEEARASRDEILAQSKESEKKLKNL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 785 sefekEIELLQAQKI-----DVEKHVQSQKREMREkmsEITKQLLESYDIEDVRSRLS--VEDLEHLNEDgelwfayegl 857
Cdd:pfam01576 839 -----EAELLQLQEDlaaseRARRQAQQERDELAD---EIASGASGKSALQDEKRRLEarIAQLEEELEE---------- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 858 kkatrvLESHFQSQKDCYEK---EIEALNfkvVHLSQEINHLQKlfreendiNESIRhevtrltsenmmipdfkqqiSEL 934
Cdd:pfam01576 901 ------EQSNTELLNDRLRKstlQVEQLT---TELAAERSTSQK--------SESAR--------------------QQL 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 935 EKQKQDLEIRLNEQAEKMKGK-------LEELSNQLHRSQEEEGTQRKAleAQNEIHTKEK--EKLIDKIQEMQEASDHL 1005
Cdd:pfam01576 944 ERQNKELKAKLQEMEGTVKSKfkssiaaLEAKIAQLEEQLEQESRERQA--ANKLVRRTEKklKEVLLQVEDERRHADQY 1021
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2462545116 1006 KKQFE-TESEVKCNFRQ------EASRLTLENRDLEEELD 1038
Cdd:pfam01576 1022 KDQAEkGNSRMKQLKRQleeaeeEASRANAARRKLQRELD 1061
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
664-976 |
1.63e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 42.37 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 664 RDAVEEKLAKLQKHNSELE-------TQKEQIQLKLQEKTEELKEKMDNL--TKQLFDDVQKEERQRMLLeksfelktqD 734
Cdd:pfam04108 37 RRGLSVQLANLEKVREGLEkvlnelkKDFKQLLKDLDAALERLEETLDKLrnTPVEPALPPGEEKQKTLL---------D 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 735 Y--EKQIQSLKEEIKALKDEkmqlqhlvegehvtsdgLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREM 812
Cdd:pfam04108 108 FidEDSVEILRDALKELIDE-----------------LQAAQESLDSDLKRFDDDLRDLQKELESLSSPSESISLIPTLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 813 REK------MSEITKQLLESYDiedvrsrLSVEDLEHLNEDGELWFAYegLKKATRVLESHFQSQKDCYE---------- 876
Cdd:pfam04108 171 KELesleeeMASLLESLTNHYD-------QCVTAVKLTEGGRAEMLEV--LENDARELDDVVPELQDRLDemennyerlq 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 877 KEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLE----------IRLN 946
Cdd:pfam04108 242 KLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEGFPsaygslllevERRR 321
|
330 340 350
....*....|....*....|....*....|
gi 2462545116 947 EQAEKMKGKLEELSNQLHRSQEEEGTQRKA 976
Cdd:pfam04108 322 EWAEKMKKILRKLAEELDRLQEEERKRREK 351
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
485-1021 |
1.67e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 485 QRKKFLRERRAALIIQQyfrgQQTVRKAITAVALKEAWAAIIIQKHcrgylvrslyQLIRMATITMQAYSRGFLARRRYR 564
Cdd:COG1196 309 ERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEEAE----------EELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 565 KMLEEHKAVILQKYARAwLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEA 644
Cdd:COG1196 375 AEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 645 ELEKAATHRRNYEEKGKRY---RDAVEEKLAKLQKHNSELETQKEQIQLKLQE----KTEELKEKMDNLTKQLFDDVQKE 717
Cdd:COG1196 454 LEEEEEALLELLAELLEEAallEAALAELLEELAEAAARLLLLLEAEADYEGFlegvKAALLLAGLRGLAGAVAVLIGVE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 718 ERQRMLLEKSFELKTQDY--------EKQIQSLKEE------------IKALKDEKMQLQHLVEGEHVtsDGLKAEVARL 777
Cdd:COG1196 534 AAYEAALEAALAAALQNIvveddevaAAAIEYLKAAkagratflpldkIRARAALAAALARGAIGAAV--DLVASDLREA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 778 SKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGElwfAYEGL 857
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE---LAERL 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 858 KKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQ 937
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 938 KQDLEIRL------NEQAekmkgkLEELsnqlhrsqEEEGTQRKALEAQNEIHTKEKEKLIDKIQEM-QEASDHLKKQFE 1010
Cdd:COG1196 769 LERLEREIealgpvNLLA------IEEY--------EELEERYDFLSEQREDLEEARETLEEAIEEIdRETRERFLETFD 834
|
570
....*....|.
gi 2462545116 1011 tesEVKCNFRQ 1021
Cdd:COG1196 835 ---AVNENFQE 842
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
523-541 |
1.94e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 36.92 E-value: 1.94e-03
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
608-756 |
2.10e-03 |
|
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein signal and a hydrolase domain. It is similar to cell wall binding proteins and might also be recognisable by a host immune defence system. It is thus likely to belong to pathways important for pathogenicity.
Pssm-ID: 431235 [Multi-domain] Cd Length: 185 Bit Score: 40.65 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 608 QKKLEDQNKENHGLVEKLTSLAAlraGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKeq 687
Cdd:pfam10368 24 QEPLVELEKKEQELYEEIIELGM---DEFDEIKKLSDEALENVEEREELLEKEKESIEEAKEEFKKIKEIIEEIEDEE-- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 688 iqlkLQEKTEELKEKMDNLTK---QLFDDVQK---EERQ--RMLLEKSFELKtqDYEKQIQSLKEEIKALKDEKMQL 756
Cdd:pfam10368 99 ----LKKEAEELIDAMEERYEaydELYDAYKKaleLDKElyEMLKDEDLTLE--ELQEQIEKINESYEEVKEANEQF 169
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
801-1034 |
2.19e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 801 VEKHVQSQKREMREKMSEITKQLlesydiEDVRSRLsvEDLEHlnedgelwfAYEGLKKATRVLEShfQSQKDCYEKEIE 880
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQL------PELRKEL--EEAEA---------ALEEFRQKNGLVDL--SEEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 881 ALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLtSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELS 960
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 961 NQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQfetesevkcnfRQEASRLtleNRDLE 1034
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL-----------EAELRRL---EREVE 361
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
661-1058 |
2.35e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 661 KRYRDAVEEKLA--KLQKHNSELETQKEQIQLKLQeKTEELKEKMDNLtkQLFDDVQKEERQRMLLEKSFELKTQDYEKQ 738
Cdd:TIGR01612 466 KRFFEIFEEEWGsyDIKKDIDENSKQDNTVKLILM-RMKDFKDIIDFM--ELYKPDEVPSKNIIGFDIDQNIKAKLYKEI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 739 IQSLKEEIKALKD-EKMQLQHLVEGEHVTSDGLKaevarLSKQVKTIseFEKEIELlqaqkIDVEKHVQSQKREMREKMS 817
Cdd:TIGR01612 543 EAGLKESYELAKNwKKLIHEIKKELEEENEDSIH-----LEKEIKDL--FDKYLEI-----DDEIIYINKLKLELKEKIK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 818 EITKQ---LLESYDIEDV--RSRLSVEDLEHLNEdgelWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQE 892
Cdd:TIGR01612 611 NISDKneyIKKAIDLKKIieNNNAYIDELAKISP----YQVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKE 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 893 --INHLQKLFREEnDINESIRHEVTRLtsENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGkleELSNQLHRSQEEe 970
Cdd:TIGR01612 687 naIDNTEDKAKLD-DLKSKIDKEYDKI--QNMETATVELHLSNIENKKNELLDIIVEIKKHIHG---EINKDLNKILED- 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 971 gtqrkaleaqneIHTKEKEkLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQ 1050
Cdd:TIGR01612 760 ------------FKNKEKE-LSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIK 826
|
....*...
gi 2462545116 1051 VKTLSKTI 1058
Cdd:TIGR01612 827 EDEIFKII 834
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
673-844 |
2.51e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 673 KLQKHNSELETQK----------EQIQLKLQEKTEELKEKMDNLTKQlfddvqkeerqrMLLEKSFELKTQDYEkqiQSL 742
Cdd:smart00787 120 QLVKTFARLEAKKmwyewrmkllEGLKEGLDENLEGLKEDYKLLMKE------------LELLNSIKPKLRDRK---DAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 743 KEEIKALKdekmqlQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQS---QKREMREKMSEI 819
Cdd:smart00787 185 EEELRQLK------QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEA 258
|
170 180
....*....|....*....|....*...
gi 2462545116 820 TKQLLES--YDIEDVRS-RLSVEDLEHL 844
Cdd:smart00787 259 EKKLEQCrgFTFKEIEKlKEQLKLLQSL 286
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
523-541 |
2.56e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 36.53 E-value: 2.56e-03
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
600-1038 |
2.61e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 600 LTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRA--------GDVEKIQKLEAELEKAAT--HRRNYEEKGKRyRDAVEE 669
Cdd:pfam15964 236 LESQVKSLRKDLAESQKTCEDLKERLKHKESLVAastssrvgGLCLKCAQHEAVLAQTHTnvHMQTIERLTKE-RDDLMS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 670 KLAKLQKHNSELETQK----EQIQLKLQEKTEELKEKMDNLTKqlFDDVQKE-ERQRMLLEKSFELKTQDYEKQIQSLKE 744
Cdd:pfam15964 315 ALVSVRSSLAEAQQREssayEQVKQAVQMTEEANFEKTKALIQ--CEQLKSElERQKERLEKELASQQEKRAQEKEALRK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 745 EIKALKDEKMQLQhLVEGEHVTSdgLKAEVARLSKQ-VKTISEFEKEIELLQAQKIDVEK----------HVQSQK---- 809
Cdd:pfam15964 393 EMKKEREELGATM-LALSQNVAQ--LEAQVEKVTREkNSLVSQLEEAQKQLASQEMDVTKvcgemryqlnQTKMKKdeae 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 810 REMREKMSEITKQL-LESYDIEDVRSRL--SVEDLEHLNEDG-----ELWFAYEGLKKATRVLESHFQ---SQKDCYEKE 878
Cdd:pfam15964 470 KEHREYRTKTGRQLeIKDQEIEKLGLELseSKQRLEQAQQDAarareECLKLTELLGESEHQLHLTRLekeSIQQSFSNE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 879 IEALNFKVVHLSQEINhlQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKqkqdleiRLNEQAEKMKGKLEE 958
Cdd:pfam15964 550 AKAQALQAQQREQELT--QKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAK-------KLEEITQKSRSEVEQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 959 LSNQ---LHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEmqeasdhLKKQFETESEVKCNFRQEASRLTLENRDLEE 1035
Cdd:pfam15964 621 LSQEkeyLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQ-------LDKHCQATAQQLVQLLSKQNQLFKERQNLTE 693
|
...
gi 2462545116 1036 ELD 1038
Cdd:pfam15964 694 EVQ 696
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
558-1056 |
3.37e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 558 LARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRfvlNIQLTYRVQRLQKKLEDQNKENHGLVE----KLTSLAALRA 633
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDR---NQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 634 GDVEKIQKLE----------------------AELEKAATH------RRNYEEKGKRYRDAvEEKLAKLQKHNSELETQK 685
Cdd:pfam05557 91 KLNEKESQLAdarevisclknelselrrqiqrAELELQSTNseleelQERLDLLKAKASEA-EQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 686 EQIQ-----LKLQEK-TEELKE---------KMDNLTKQLFDDV---------------QKEERQRML------------ 723
Cdd:pfam05557 170 QRIKelefeIQSQEQdSEIVKNskselaripELEKELERLREHNkhlnenienklllkeEVEDLKRKLereekyreeaat 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 724 --LEKS-FELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVtsdgLKAEVARLSKQVK----TISEFEKEIELLQA 796
Cdd:pfam05557 250 leLEKEkLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIV----LKEENSSLTSSARqlekARRELEQELAQYLK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 797 QKIDVE---KHVQSQKREMREKMSEITK------QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVlesh 867
Cdd:pfam05557 326 KIEDLNkklKRHKALVRRLQRRVLLLTKerdgyrAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEA---- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 868 fqsQKDCYEKEIEALNFKVVHLSQEInhlqKLFREENDINE--SIRHEVTRLTSENmmiPDFKQQISELEKQKQDLEIRL 945
Cdd:pfam05557 402 ---QLSVAEEELGGYKQQAQTLEREL----QALRQQESLADpsYSKEEVDSLRRKL---ETLELERQRLREQKNELEMEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 946 neqaekMKGKLEELSNQ-----LHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVkcNFR 1020
Cdd:pfam05557 472 ------ERRCLQGDYDPkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTM--NFK 543
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462545116 1021 qeasrltlENRDLEEELDMKDRVIKKLQDQVKTLSK 1056
Cdd:pfam05557 544 --------EVLDLRKELESAELKNQRLKEVFQAKIQ 571
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
603-737 |
3.44e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.60 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSLAAlragdveKIQKLEAELEKAathrrnyEEKGKRYRDAVEEKLAK------LQK 676
Cdd:pfam12718 15 RAEELEEKVKELEQENLEKEQEIKSLTH-------KNQQLEEEVEKL-------EEQLKEAKEKAEESEKLktnnenLTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545116 677 HNSELETQKEQIQLKLQEKTEELKEkMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK 737
Cdd:pfam12718 81 KIQLLEEELEESDKRLKETTEKLRE-TDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
699-967 |
3.47e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 699 LKEKMDNLTKQL-------FDDVQKEErQRMLLEKSFELKTQDYEK--QIQSLKEEIKALKDEKMQLQHLVegehvTSDG 769
Cdd:PRK05771 14 LKSYKDEVLEALhelgvvhIEDLKEEL-SNERLRKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVKS-----LEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 770 LKAEVARLSKQVKTISEFEKEIELLQaqkidvekhvqSQKREMREKMSEITKqlLESYDIedvrsrlsveDLEHLNeDGE 849
Cdd:PRK05771 88 IKDVEEELEKIEKEIKELEEEISELE-----------NEIKELEQEIERLEP--WGNFDL----------DLSLLL-GFK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 850 LWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFRE-------ENDINESIrhEVTRLtsenm 922
Cdd:PRK05771 144 YVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEElkklgfeRLELEEEG--TPSEL----- 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462545116 923 mIPDFKQQISELEKQKQDLEIRLNEQAEK----MKGKLEELSNQLHRSQ 967
Cdd:PRK05771 217 -IREIKEELEEIEKERESLLEELKELAKKyleeLLALYEYLEIELERAE 264
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
599-789 |
3.96e-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: 41.42 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQK----------KLEDQNKENHGLVEKLT----SLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR 664
Cdd:pfam07888 77 ELESRVAELKEelrqsrekheELEEKYKELSASSEELSeekdALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 665 DAVEEKLAKLQkhnsELETQKEQIQLKLQEKTEELKEKMDNLtkQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKE 744
Cdd:pfam07888 157 ERAKKAGAQRK----EEEAERKQLQAKLQQTEEELRSLSKEF--QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462545116 745 EIKALKDEKMQLQHLVEGEHVTSDGLKAEVARL-SKQVKTISEFEK 789
Cdd:pfam07888 231 ENEALLEELRSLQERLNASERKVEGLGEELSSMaAQRDRTQAELHQ 276
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
665-825 |
4.12e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 665 DAVEEKLAKLQkhnSELETQKEQIQLKLQEKtEELKEKMDNLTKQLFDdvQKEERQRMLLE-----KSFELKTQDYEKQi 739
Cdd:PRK04778 278 DEAEEKNEEIQ---ERIDQLYDILEREVKAR-KYVEKNSDTLPDFLEH--AKEQNKELKEEidrvkQSYTLNESELESV- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 740 QSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEI-ELLQAQKIDvEKHVQSQKREMREKMSE 818
Cdd:PRK04778 351 RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLsEMLQGLRKD-ELEAREKLERYRNKLHE 429
|
....*..
gi 2462545116 819 ItKQLLE 825
Cdd:PRK04778 430 I-KRYLE 435
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
639-1004 |
4.30e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 639 IQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQK---------HNSELETQKEQIQLKLQEKteelKEKMDNLtKQ 709
Cdd:TIGR01612 1120 IKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvadkaisndDPEEIEKKIENIVTKIDKK----KNIYDEI-KK 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 710 LFDDVQKEERQRMLLEKSFELKTQdYEKQIQSLKEEikALKDEKMQLQHLV---EGEHVTSDGLKAEVARLSKQVKTISE 786
Cdd:TIGR01612 1195 LLNEIAEIEKDKTSLEEVKGINLS-YGKNLGKLFLE--KIDEEKKKSEHMIkamEAYIEDLDEIKEKSPEIENEMGIEMD 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 787 FEKEIELLQAQKIDVEKH-VQSQKR-----EMREKMSEITKQLLESYDIEDVRSRLSvedlehlnedgelwfayeglkka 860
Cdd:TIGR01612 1272 IKAEMETFNISHDDDKDHhIISKKHdenisDIREKSLKIIEDFSEESDINDIKKELQ----------------------- 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 861 TRVLESH-FQSQKDCYEKEIEALnFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISeLEKQKQ 939
Cdd:TIGR01612 1329 KNLLDAQkHNSDINLYLNEIANI-YNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDIN-LEECKS 1406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545116 940 DLEIRL-----NEQAEKMKGK-----LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDH 1004
Cdd:TIGR01612 1407 KIESTLddkdiDECIKKIKELknhilSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDH 1481
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
933-1060 |
4.37e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 933 ELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEK---EKLIDKIQEMQEASDHLK 1006
Cdd:pfam15905 160 ELMKLRNKLEAKMKEvmaKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKsetEKLLEYITELSCVSEQVE 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 1007 KQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1060
Cdd:pfam15905 240 KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEE 293
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
603-842 |
4.42e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLED---QNKENHGLVEKLTSLA----ALRAGdVEKIQKLEAELEkaaTHRRNYEEKG--KRYRDAVEEKLA- 672
Cdd:pfam05622 88 KCEELEKEVLElqhRNEELTSLAEEAQALKdemdILRES-SDKVKKLEATVE---TYKKKLEDLGdlRRQVKLLEERNAe 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 673 ----------KLQKHN---SELETQKEQIQ---LKLQE---KTEELKEKMDNLTKQLfDDVQKeERQRMLLEK------- 726
Cdd:pfam05622 164 ymqrtlqleeELKKANalrGQLETYKRQVQelhGKLSEeskKADKLEFEYKKLEEKL-EALQK-EKERLIIERdtlretn 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 727 ------------------------------SFELKTQDYEKQIQSLKEEIKALK--------DEKMQLQHLVEGEHVTSD 768
Cdd:pfam05622 242 eelrcaqlqqaelsqadallspssdpgdnlAAEIMPAEIREKLIRLQHENKMLRlgqegsyrERLTELQQLLEDANRRKN 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 769 GLKAEvARLSKQvktisefekEIELLQAQKIDVEKHVQSQ--KRE----MREKMSEITKQLLESYDiEDVRSRLSVEDLE 842
Cdd:pfam05622 322 ELETQ-NRLANQ---------RILELQQQVEELQKALQEQgsKAEdsslLKQKLEEHLEKLHEAQS-ELQKKKEQIEELE 390
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
603-851 |
4.70e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 603 RVQRLQKKLEDQNKENHGLVEKLTSLAALRA------GDVEKIQKLEAELEKA---ATHRRNYEEKgkryrdaVEEKLAK 673
Cdd:COG1340 72 KVKELKEERDELNEKLNELREELDELRKELAelnkagGSIDKLRKEIERLEWRqqtEVLSPEEEKE-------LVEKIKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 674 LQKhnsELETQKEQIQLKlqEKTEELKEKMDNLTKQLfddvqKEERQRMlleksfelktQDYEKQIQSLKEEIKALKDEK 753
Cdd:COG1340 145 LEK---ELEKAKKALEKN--EKLKELRAELKELRKEA-----EEIHKKI----------KELAEEAQELHEEMIELYKEA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 754 MQLQHLVEGEHVTSDGLKAEVARLSKQ----VKTISEFEKEIELLQAQKIDVEKhvQSQKREMREKMSEITKQLLESydi 829
Cdd:COG1340 205 DELRKEADELHKEIVEAQEKADELHEEiielQKELRELRKELKKLRKKQRALKR--EKEKEELEEKAEEIFEKLKKG--- 279
|
250 260
....*....|....*....|..
gi 2462545116 830 edvrSRLSVEDLEHLNEDGELW 851
Cdd:COG1340 280 ----EKLTTEELKLLQKSGLLE 297
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
738-999 |
4.78e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 738 QIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKA---EVARLSKQV----KTISEFEKEIELLQAQKIDVEKHVQSQKR 810
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSsnlELENIKKQIaddeKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 811 EMREKMS-EITKQLLESyDIEDVRSRLSVEdLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHL 889
Cdd:PRK01156 240 ALNELSSlEDMKNRYES-EIKTAESDLSME-LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 890 SQEINHLQKLFREENDInESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEqAEKMKGKLEELSNQLHRSQEE 969
Cdd:PRK01156 318 DAEINKYHAIIKKLSVL-QKDYNDYIKKKSR---YDDLNNQILELEGYEMDYNSYLKS-IESLKKKIEEYSKNIERMSAF 392
|
250 260 270
....*....|....*....|....*....|
gi 2462545116 970 EGTQRKALEAQNEIHTKEKEKLIDKIQEMQ 999
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
716-1013 |
6.35e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.01 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 716 KEERQRML-LEKSFELKTQDYEKQIQSLKEEIKALKDEKmqlQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELL 794
Cdd:pfam02029 16 REERRRQKeEEEPSGQVTESVEPNEHNSYEEDSELKPSG---QGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 795 QAqkiDVEKHVQSQKREMREKMSEITKQ------LLESYDIEDVRSRlSVEDLEHLNEDGELWFAYEGLKKATRVLESHF 868
Cdd:pfam02029 93 IA---DEKESVAERKENNEEEENSSWEKeekrdsRLGRYKEEETEIR-EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 869 QSQKDCYEKEIEALNFK---------VVHLSQEINHL-QKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQK 938
Cdd:pfam02029 169 VPTENFAKEEVKDEKIKkekkvkyesKVFLDQKRGHPeVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 939 QDLEIRL------NEQAEKMKGK-------LEEL---SNQLHRSQEEEGTQRKALEAQNEIHTKE-KEKLIDKIqEMQEA 1001
Cdd:pfam02029 249 KLEELRRrrqekeSEEFEKLRQKqqeaeleLEELkkkREERRKLLEEEEQRRKQEEAERKLREEEeKRRMKEEI-ERRRA 327
|
330
....*....|..
gi 2462545116 1002 SDHLKKQFETES 1013
Cdd:pfam02029 328 EAAEKRQKLPED 339
|
|
| TBCA |
pfam02970 |
Tubulin binding cofactor A; |
857-961 |
6.99e-03 |
|
Tubulin binding cofactor A;
Pssm-ID: 460769 [Multi-domain] Cd Length: 99 Bit Score: 37.49 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 857 LKKATRVLEsHFQSQKDCYEKEIEalnfkvvhlsQEINHLQKLFREENDINEsIRHEVTRLTSENMMIPDFKQQIselEK 936
Cdd:pfam02970 6 LKIKTGVVK-RLVKEEASYEKELE----------EQEARLEKLKADGADEYD-LKKQEEVLEETKAMIPDLKKRL---EE 70
|
90 100
....*....|....*....|....*
gi 2462545116 937 QKQDLEIRLNEQAEKMKGkLEELSN 961
Cdd:pfam02970 71 AVEDLEEFLEEEEDLGAD-TEELTA 94
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
915-1065 |
7.17e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 915 TRLTSENMMIPDFKQQISELEKQKQDLEIR---LNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKL 991
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKrdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545116 992 IDKIQEMQEASDHLKKQFEtESEVKCNFRQEASRLTLENRDLEEELDMKD---RVIKKLQDQVKTLSKTIGKANDVH 1065
Cdd:COG1340 81 DELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVlspEEEKELVEKIKELEKELEKAKKAL 156
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
599-867 |
7.51e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQkhn 678
Cdd:COG4372 77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 679 sELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKmqLQH 758
Cdd:COG4372 154 -ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL--EAK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 759 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 838
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
250 260
....*....|....*....|....*....
gi 2462545116 839 EDLEHLNEDGELWFAYEGLKKATRVLESH 867
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAEL 339
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
544-564 |
7.98e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 34.99 E-value: 7.98e-03
|
| DUF6262 |
pfam19776 |
Family of unknown function (DUF6262); This family of proteins, functionally uncharacterized, ... |
655-756 |
8.19e-03 |
|
Family of unknown function (DUF6262); This family of proteins, functionally uncharacterized, is found in bacteria. Proteins in this family are typically between 124 and 143 amino acids in length. Some members included in this family are hypothetical transposases, associated with transposon Tn554. There is a conserved sequence GV/LSR/K and a highly conserved tyrosine residue.
Pssm-ID: 466180 [Multi-domain] Cd Length: 110 Bit Score: 37.60 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 655 NYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQL-KLQEKT----------EELKEKMDNLTKQlfddvQKE--ERQR 721
Cdd:pfam19776 1 KYDKMVELNRKESEEKIELAKKAIQEMLEEGEKITVpELVKRTglsrgffyknPEVRRELDEAIEQ-----QGGmvNPKR 75
|
90 100 110
....*....|....*....|....*....|....*
gi 2462545116 722 MLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQL 756
Cdd:pfam19776 76 EILDMALEKRIELLKKEIKELKRENEELKKENEKL 110
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
765-1048 |
8.33e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 765 VTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE----SYDIEDVRSRLSveD 840
Cdd:pfam15905 56 VKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREktslSASVASLEKQLL--E 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 841 LEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKlfreenDINESiRHEVTRLTSE 920
Cdd:pfam15905 134 LTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQK------NLEHS-KGKVAQLEEK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 921 NMMIPDFKQQiSELEKQKQDLEIR----LNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQ 996
Cdd:pfam15905 207 LVSTEKEKIE-EKSETEKLLEYITelscVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCK 285
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 997 EMQEASDHLKKQFETESEvkcnfrqeasRLTLENRDLEEELDMKDRVIKKLQ 1048
Cdd:pfam15905 286 LLESEKEELLREYEEKEQ----------TLNAELEELKEKLTLEEQEHQKLQ 327
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
667-881 |
8.43e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.40 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 667 VEEKLAKLQKH---NSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEER-----QRMLLEKSFELktQDYEKQ 738
Cdd:pfam05701 231 AEEELQRLNQQllsAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKtstsiQAALASAKKEL--EEVKAN 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 739 IQSLKEEIKALKDEKMQLQHLVEGEhvtsdglKAEVARLSKQ----VKTISEFEKEIELLQaQKIDVekhVQSQKREMRE 814
Cdd:pfam05701 309 IEKAKDEVNCLRVAAASLRSELEKE-------KAELASLRQRegmaSIAVSSLEAELNRTK-SEIAL---VQAKEKEARE 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 815 KMSEITKQLLE-SYDIEDVRS--RLSVEDLEHLNEDGELwfayegLKKATRVLESHFQSQKdcyeKEIEA 881
Cdd:pfam05701 378 KMVELPKQLQQaAQEAEEAKSlaQAAREELRKAKEEAEQ------AKAAASTVESRLEAVL----KEIEA 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
599-823 |
9.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 599 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR--DAVEEKLAKLQK 676
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIAALLAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 677 HNSELETQKEQIQLKLQEKtEELKEKMDNLTKQLfDDVQKEERQRMLLEKSFELKT--QDYEKQIQSLKEEIKALKDEKM 754
Cdd:COG4717 379 AGVEDEEELRAALEQAEEY-QELKEELEELEEQL-EELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545116 755 QLQHLVE--GEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKR-EMREKMSEITKQL 823
Cdd:COG4717 457 ELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
901-1010 |
9.05e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 901 REENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSQEEEgtqRKALEAQ 980
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE----AELEEKDERIERLERELSEARSEE---RREIRKD 464
|
90 100 110
....*....|....*....|....*....|..
gi 2462545116 981 NEIHTKEKE--KLIDKIQEMQEASDHLKKQFE 1010
Cdd:COG2433 465 REISRLDREieRLERELEEERERIEELKRKLE 496
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
672-755 |
9.38e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 37.95 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 672 AKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQlfddvQKEERqrmllEKSFELKTQDYEKQIQSLKEEIKALKD 751
Cdd:smart00935 21 KQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEA-----AREKK-----EKELQKKVQEFQRKQQKLQQDLQKRQQ 90
|
....
gi 2462545116 752 EKMQ 755
Cdd:smart00935 91 EELQ 94
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
636-782 |
9.54e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.96 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 636 VEKIQKLEAELEKAATHRRNYEEKGKRY---RDAVEEKLAKLQKHNSELETQKEqiqlKLQEKTEELKEKmdnltKQLFD 712
Cdd:pfam02841 154 LEERDKLEAKYNQVPRKGVKAEEVLQEFlqsKEAVEEAILQTDQALTAKEKAIE----AERAKAEAAEAE-----QELLR 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545116 713 DVQKEERQRMlleksfELKTQDYEKQIQSLKEEIKALKD------EKMQLQHLVEGEHVTSDGLKAEVARLSKQVK 782
Cdd:pfam02841 225 EKQKEEEQMM------EAQERSYQEHVKQLIEKMEAEREqllaeqERMLEHKLQEQEELLKEGFKTEAESLQKEIQ 294
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
665-746 |
9.56e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 38.66 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 665 DAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQ--LFDDVQKEERQRML--LEKSFELKTQDYEKQIQ 740
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEaaTLSEEERQKKERELqkKQQELQRKQQEAQQDLQ 111
|
....*.
gi 2462545116 741 SLKEEI 746
Cdd:COG2825 112 KRQQEL 117
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
855-1062 |
9.98e-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: 40.33 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 855 EGLKKATRVLESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDI-NESIRHEVTRLTSENMMIPDFKQQISE 933
Cdd:COG5185 186 LGLLKGISELKKAEPSGTVNSIKESETGN-LGSESTLLEKAKEIINIEEALKgFQDPESELEDLAQTSDKLEKLVEQNTD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545116 934 LEK----QKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEK-LIDKIQEMQEASDHLKKQ 1008
Cdd:COG5185 265 LRLeklgENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQeLEESKRETETGIQNLTAE 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462545116 1009 FETESEvKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAN 1062
Cdd:COG5185 345 IEQGQE-SLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIP 397
|
|
| |
