|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
81-696 |
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: 1199.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01380 1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGSN-AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd01380 161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 320 QMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARD 399
Cdd:cd01380 241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 400 ALAKKIYAHLFDFIVERINQALQF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 477
Cdd:cd01380 321 ALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNR-NPLFEKPRMSNTSFVIQHFADKVE 556
Cdd:cd01380 401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 557 YKCEGFLEKNRDTVYDMLVEILRASK---------FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRA 627
Cdd:cd01380 481 YQVEGFLEKNRDTVSEEHLNVLKASKnrkktvgsqFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRA 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545112 628 CGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd01380 561 CGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
62-707 |
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: 943.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 62 NPDILVGENDLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVA 141
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 142 EEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:smart00242 80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVgSVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 221 YTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDR 300
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 301 AEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNE-RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIV 379
Cdd:smart00242 240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 380 TSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:smart00242 320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 460 QQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEK 538
Cdd:smart00242 400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHH-KKHPHFSK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 539 P-RMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK---------------------------FRSSLYLL 590
Cdd:smart00242 479 PkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKnpliaslfpsgvsnagskkrfqtvgsqFKEQLNEL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 591 METLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFS-DKK 669
Cdd:smart00242 559 MDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGgDAK 638
|
650 660 670
....*....|....*....|....*....|....*...
gi 2462545112 670 EVCKVVLHRLIQDSNQYQFGKTKIFFRAGQVAYLEKLR 707
Cdd:smart00242 639 KACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
70-696 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 880.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 70 NDLTALSYLHEPAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYK-SDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSN---AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF 226
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 227 DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVET 306
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 307 QKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVV 386
Cdd:pfam00063 241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 387 KPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF-SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 465
Cdd:pfam00063 321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPR-MSN 543
Cdd:pfam00063 401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRlQGE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS-----------------------------------------K 582
Cdd:pfam00063 480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSsdpllaelfpdyetaesaaanesgkstpkrtkkkrfitvgsQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 583 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK-Q 661
Cdd:pfam00063 560 FKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKtW 639
|
650 660 670
....*....|....*....|....*....|....*
gi 2462545112 662 ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:pfam00063 640 PKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
12-1279 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 880.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 12 RVWIPDPEEVWKSAEIAK-DYRVGDKVLRLLLEDGtELDySVNPESLPPLR-NPDILVGENDLTALSYLHEPAVLHNLRI 89
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDG-ESV-SVKKKVLGNDRiKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 90 RFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTV 169
Cdd:COG5022 89 RY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 170 SARYAMRYFATVSKSGSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLLEKSRV 247
Cdd:COG5022 168 NAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 248 VFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKIL 327
Cdd:COG5022 248 VHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKIL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 328 AAILHLGNVQITAVGNERSSVSeDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYA 407
Cdd:COG5022 328 AAILHIGNIEFKEDRNGAAIFS-DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 408 HLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDF 487
Cdd:COG5022 407 NLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 488 YDNQPVIDLIEAK--MGILELLDEECLLPHGTDENWLQKLYNNF-VNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLE 564
Cdd:COG5022 487 FDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRLnKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVEGFLD 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 565 KNRDTVYDMLVEILRAS--------------------------KFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDS 618
Cdd:COG5022 567 KNKDPLNDDLLELLKAStnefvstlfddeenieskgrfptlgsRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDN 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 619 KRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM-----TKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKI 693
Cdd:COG5022 647 QMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSpskswTGEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKV 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 694 FFRAGQVAYLEKLRLDKLRQSCVMVQKHMRGWLQRKKFLRERRaaliIQQYFRGQQTVRKAITAVAlKEAW--AAIIIQK 771
Cdd:COG5022 727 FFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALK----RIKKIQVIQHGFRLRRLVD-YELKwrLFIKLQP 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 772 HCRGYLVRSlYQLIRMATITMQAYS--RGFLARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRL 849
Cdd:COG5022 802 LLSLLGSRK-EYRSYLACIIKLQKTikREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELA 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 850 QKKLEDQNKEnhglVEKLTSLAALRAGDVEKIQKLEAELEKaaTHRRNYEEKgkryrdavEEKLAKLQKHN--------S 921
Cdd:COG5022 881 ERQLQELKID----VKSISSLKLVNLELESEIIELKKSLSS--DLIENLEFK--------TELIARLKKLLnnidleegP 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 922 ELETQKEQIQLKLQEKTEELKE---KMDNLTKQLfdDVQKEERQRMLLE-KSFELKTQDYEKQIQSLKEEIKALKDEKMQ 997
Cdd:COG5022 947 SIEYVKLPELNKLHEVESKLKEtseEYEDLLKKS--TILVREGNKANSElKNFKKELAELSKQYGALQESTKQLKELPVE 1024
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 998 LQHLVEGEHVTSDgLKAEVARLSKQVKTISEFEKEIELLQAQKIDVekhvqSQKREMREKMSeitkqlLESYDIEDVRSR 1077
Cdd:COG5022 1025 VAELQSASKIISS-ESTELSILKPLQKLKGLLLLENNQLQARYKAL-----KLRRENSLLDD------KQLYQLESTENL 1092
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1078 LSVedlehLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVT 1157
Cdd:COG5022 1093 LKT-----INVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEA 1167
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1158 RLTsenmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKlidki 1237
Cdd:COG5022 1168 LPS-----PPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYS----- 1237
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....
gi 2462545112 1238 QEMQEASDHLKKQFETESEVKCNFRQEASRL--TLENRDLEEEL 1279
Cdd:COG5022 1238 TSLKGFNNLNKKFDTPASMSNEKLLSLLNSIdnLLSSYKLEEEV 1281
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
81-696 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 842.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMG-DMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd00124 1 AAILHNLRERYARDL-IYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 160 SGESGAGKTVSARYAMRYFATVSKSGSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQII 233
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSGSSKSsssassIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 234 GANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEE----FNYTRMGGNTVIEGVNDRAEMVETQKT 309
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 310 FTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNE--RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVK 387
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 388 PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 465
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNT 544
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILR-ASKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQ 623
Cdd:cd00124 480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRsGSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLE 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 624 QLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK-QELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd00124 560 QLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGaTEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
81-696 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 726.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01377 1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGSNAH--------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd01377 80 GESGAGKTENTKKVIQYLASVAASSKKKKesgkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 233 IGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTL 312
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 313 LGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 393 QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQ 472
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMS--NTSFVI 548
Cdd:cd01377 400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKksEAHFIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 549 QHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK----------------------------------FRSSLYLLMETL 594
Cdd:cd01377 480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSdplvaslfkdyeesgggggkkkkkggsfrtvsqlHKEQLNKLMTTL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 595 NATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM-TKQELSFSDKKEVCK 673
Cdd:cd01377 560 RSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILApNAIPKGFDDGKAACE 639
|
650 660
....*....|....*....|...
gi 2462545112 674 VVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd01377 640 KILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
81-696 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 690.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd01384 1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 160 SGESGAGKTVSARYAMRYFATVSK--SGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANM 237
Cdd:cd01384 80 SGESGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 238 STYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKE 317
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 318 DFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDS---HLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd01384 240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKsefHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEE 474
Cdd:cd01384 320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 475 YMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd01384 400 YTKEEIDWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPRSTHETFAQKLYQTLKD-HKRFSKPKLSRTDFTIDHYAG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 554 KVEYKCEGFLEKNRDTVYDMLVEILRASK----------------------------FRSSLYLLMETLNATTPHYVRCI 605
Cdd:cd01384 479 DVTYQTDLFLDKNKDYVVAEHQALLNASKcpfvaglfpplpregtsssskfssigsrFKQQLQELMETLNTTEPHYIRCI 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 606 KPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLiqDSNQ 685
Cdd:cd01384 559 KPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKA--GLKG 636
|
650
....*....|.
gi 2462545112 686 YQFGKTKIFFR 696
Cdd:cd01384 637 YQIGKTKVFLR 647
|
|
| Myo5c_CBD |
cd15476 |
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ... |
1324-1691 |
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: 679.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1324 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1403
Cdd:cd15476 1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1404 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1483
Cdd:cd15476 81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1484 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1563
Cdd:cd15476 143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1564 NISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1643
Cdd:cd15476 205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462545112 1644 RKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKL 1691
Cdd:cd15476 285 RKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
82-696 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 670.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01378 2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSGSN--AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd01378 81 ESGAGKTEASKRIMQYIAAVSGGSESevERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd01378 161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 320 QMDVFKILAAILHLGNVQITAVGNERSSVSeDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSE---TVVKPMTRPQAVN 396
Cdd:cd01378 241 QDSIFRILAAILHLGNIQFAEDEEGNAAIS-DTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd01378 320 ARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 476 MKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLyNNFVNRNPLFEKP----RMSNTSFVIQ 549
Cdd:cd01378 400 VREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLTAGdATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRIK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRAS--------------------------KFRSSLYLLMETLNATTPHYVR 603
Cdd:cd01378 479 HYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSsnpflrslfpegvdldskkrpptagtKFKNSANALVETLMKKQPSYIR 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 604 CIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFS-DKKEVCKVVLHRLIQD 682
Cdd:cd01378 559 CIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDgTWQGGVESILKDLNIP 638
|
650
....*....|....
gi 2462545112 683 SNQYQFGKTKIFFR 696
Cdd:cd01378 639 PEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
81-696 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 668.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDmdPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01383 1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSkSGSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTY 240
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALG-GGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQ 320
Cdd:cd01383 156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 321 MDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDA 400
Cdd:cd01383 236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 401 LAKKIYAHLFDFIVERINQALQFSGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKED 479
Cdd:cd01383 316 LAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 480 IPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNRNPLFEKPRmsNTSFVIQHFADKVEYK 558
Cdd:cd01383 396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 559 CEGFLEKNRDTVYDMLVEILR-------------------------------------ASKFRSSLYLLMETLNATTPHY 601
Cdd:cd01383 473 TSGFLEKNRDLLHSDLIQLLSscscqlpqlfaskmldasrkalpltkasgsdsqkqsvATKFKGQLFKLMQRLENTTPHF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 602 VRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQ 681
Cdd:cd01383 553 IRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTSVAILQQFNI 632
|
650
....*....|....*
gi 2462545112 682 DSNQYQFGKTKIFFR 696
Cdd:cd01383 633 LPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
82-696 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 661.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAEsKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01381 2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSksGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYL 241
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS--GQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQM 321
Cdd:cd01381 159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 322 DVFKILAAILHLGNVQITA--VGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARD 399
Cdd:cd01381 239 DIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 400 ALAKKIYAHLFDFIVERINQAL-QFSGKQH--TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 476
Cdd:cd01381 319 AFVKGIYGRLFIWIVNKINSAIyKPRGTDSsrTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 477 KEDIPWTLIDFYDNQPVIDLI-EAKMGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRM-SNTSFVIQHFADK 554
Cdd:cd01381 399 KEGINWQHIEFVDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGN-NKNYLKPKSdLNTSFGINHFAGV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 555 VEYKCEGFLEKNRDTVYDMLVEILRASK----------------------------FRSSLYLLMETLNATTPHYVRCIK 606
Cdd:cd01381 478 VFYDTRGFLEKNRDTFSADLLQLVQSSKnkflkqlfnedismgsetrkksptlssqFRKSLDQLMKTLSACQPFFVRCIK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 607 PNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL------MTKQELSFSDKKEVCKVVLHrli 680
Cdd:cd01381 558 PNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLvpgippAHKTDCRAATRKICCAVLGG--- 634
|
650
....*....|....*.
gi 2462545112 681 qDSNqYQFGKTKIFFR 696
Cdd:cd01381 635 -DAD-YQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
82-696 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 630.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14883 2 GINTNLKVRYK-KDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSGSnaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYL 241
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAVTNNHS--WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 242 LEKSRVVFQSENERNYHIFYQLCASAQQS-EFKH-LKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd14883 159 LEQSRITFQAPGERNYHVFYQLLAGAKHSkELKEkLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 320 QMDVFKILAAILHLGNVQITAVGNERSSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNAR 398
Cdd:cd14883 239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEiLKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 399 DALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE 478
Cdd:cd14883 319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 479 DIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKP--RMSNTSFVIQHFADKV 555
Cdd:cd14883 399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 556 EYKCEGFLEKNRDTVYDMLVEILRASK------------------------------------------FRSSLYLLMET 593
Cdd:cd14883 478 TYTVQGFLDKNKDTQQDDLFDLMSRSKnkfvkelftypdllaltglsislggdttsrgtskgkptvgdtFKHQLQSLVDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 594 LNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK-QELSFSDKKEVC 672
Cdd:cd14883 558 LSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRaRSADHKETCGAV 637
|
650 660
....*....|....*....|....
gi 2462545112 673 KVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14883 638 RALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
81-696 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 595.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14872 1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSksGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTY 240
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVA--GSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 241 LLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQ 320
Cdd:cd14872 158 LLEKSRVVYQIKGERNFHIFYQLLASPDPA--SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 321 MDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCE---LLGLESGRVAQWLCNRKI-VTSSETVVKPMTRPQAVN 396
Cdd:cd14872 236 NNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMeIKGCDPTRIPLTPAQATD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 397 ARDALAKKIYAHLFDFIVERINQAL-QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd14872 316 ACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 476 MKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNF-VNRNPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd14872 396 QSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 554 KVEYKCEGFLEKNRDTVYDMLVEILRASK-------------------------FRSSLYLLMETLNATTPHYVRCIKPN 608
Cdd:cd14872 476 DVTYDITGFLEKNKDTLQKDLYVLLSSSKnkliavlfppsegdqktskvtlggqFRKQLSALMTALNATEPHYIRCVKPN 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 609 DEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSF-SDKKEVCKVVLHRLIQDSNQYQ 687
Cdd:cd14872 556 QEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRVgPDDRQRCDLLLKSLKQDFSKVQ 635
|
....*....
gi 2462545112 688 FGKTKIFFR 696
Cdd:cd14872 636 VGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
82-696 |
0e+00 |
|
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: 580.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMAR----NNRNQS 156
Cdd:cd14890 2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 157 IIVSGESGAGKTVSARYAMRYFATVSK-----------SGSNAH------VEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSgfaqgasgegeAASEAIeqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 220 KYTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVND 299
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLR-GECSSIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 300 RAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVgnERSSVSEDDS---HLKVFCELLGLESGRVAQWLCNR 376
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATtlqSLKLAAELLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 377 KIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYAN 456
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 457 EKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM----GILELLDEECLLpHGTDEN--WLQKLYNNF- 529
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLDDCWRF-KGEEANkkFVSQLHASFg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 530 -----------VNRNPLFEKPRMSNT-SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS-----------KFRSS 586
Cdd:cd14890 477 rksgsggtrrgSSQHPHFVHPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSrrsirevsvgaQFRTQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 587 LYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQElsfs 666
Cdd:cd14890 557 LQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAE---- 632
|
650 660 670
....*....|....*....|....*....|
gi 2462545112 667 DKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14890 633 NIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
81-696 |
0e+00 |
|
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: 578.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14903 1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 160 SGESGAGKTVSARYAMRYFATVSkSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIA-GGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEfkHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDF 319
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 320 QMDVFKILAAILHLGNVQITAVGN--ERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNA 397
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIQSKPNddEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 398 RDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 477
Cdd:cd14903 317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFADKVEY 557
Cdd:cd14903 397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 558 KCEGFLEKNRDTVYDMLVEILRAS------------------------------------------KFRSSLYLLMETLN 595
Cdd:cd14903 477 ESLGFLEKHKDALLPDLSDLMRGSskpflrmlfkekvespaaastslargarrrrggalttttvgtQFKDSLNELMTTIR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 596 ATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVV 675
Cdd:cd14903 557 STNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVPVAERCEAL 636
|
650 660
....*....|....*....|..
gi 2462545112 676 LHRL-IQDSNQYQFGKTKIFFR 696
Cdd:cd14903 637 MKKLkLESPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
84-696 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 572.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01382 4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 163 SGAGKTVSARYAMRYFaTVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd01382 83 SGAGKTESTKYILRYL-TESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLklgsaeefnytrmggnTVIEGVNDRAEMVETQKTFTLLGFKEDFQMD 322
Cdd:cd01382 162 EKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------------LKDPLLDDVGDFIRMDKAMKKIGLSDEEKLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 323 VFKILAAILHLGNVQITAVGNER---SSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSE----TVVK-PMTRPQ 393
Cdd:cd01382 226 IFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQsLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKVEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 394 AVNARDALAKKIYAHLFDFIVERINQALQFSGKQHtFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd01382 306 ANNARDALAKAIYSKLFDHIVNRINQCIPFETSSY-FIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 474 EYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMS---------- 542
Cdd:cd01382 385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKN-HFRLSIPRKSklkihrnlrd 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 543 NTSFVIQHFADKVEYKCEGFLEKNRDTVYD---MLVE-----ILRA-------------------------SKFRSSLYL 589
Cdd:cd01382 464 DEGFLIRHFAGAVCYETAQFIEKNNDALHAsleSLICeskdkFIRSlfesstnnnkdskqkagklsfisvgNKFKTQLNL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 590 LMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKqELSFSDKK 669
Cdd:cd01382 544 LMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPP-KLARLDPR 622
|
650 660
....*....|....*....|....*..
gi 2462545112 670 EVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd01382 623 LFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
81-696 |
0e+00 |
|
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: 571.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd01379 1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTY 240
Cdd:cd01379 80 GESGAGKTESANLLVQQLTVLGKA-NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 241 LLEKSRVVFQSENERNYHIFYQLCAS-AQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVND---RAEMVETQKTFTLLGFK 316
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNsgnREKFEEIEQCFKVIGFT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 317 EDFQMDVFKILAAILHLGNVQITAVGNE----RSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd01379 239 KEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 393 QAVNARDALAKKIYAHLFDFIVERINQALQFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd01379 319 EATDARDAMAKALYGRLFSWIVNRINSLLKPDrsasDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvnRNPLFEKPRMSNTSFV 547
Cdd:cd01379 398 AWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSNALSFG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK-----------FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEF 616
Cdd:cd01379 476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSEnplvrqtvatyFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 617 DSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSnqYQFGKTKIFFR 696
Cdd:cd01379 556 DREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| Myo5_CBD |
cd15470 |
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
1324-1690 |
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: 566.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1324 EDEAKLIQNLILDLKPRGVVvNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1403
Cdd:cd15470 1 EDESRLIKNLITDLKPRGAV-GLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1404 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1483
Cdd:cd15470 80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1484 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1563
Cdd:cd15470 142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1564 NISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1643
Cdd:cd15470 204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2462545112 1644 RKVQALLNSREDSS--QLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFK 1690
Cdd:cd15470 284 RKVQARLNERADSNqlQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
84-696 |
0e+00 |
|
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: 565.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGES 163
Cdd:cd01385 4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 164 GAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLLE 243
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 244 KSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDV 323
Cdd:cd01385 163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 324 FKILAAILHLGNVQI---TAVGNERSSVSEDDShLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDA 400
Cdd:cd01385 243 FSVLSAVLHLGNIEYkkkAYHRDESVTVGNPEV-LDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 401 LAKKIYAHLFDFIVERINQALQ----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 476
Cdd:cd01385 322 MAKCLYSALFDWIVLRINHALLnkkdLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKlYNNFVNRNPLFEKPRMSNTSFVIQHFADKV 555
Cdd:cd01385 402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 556 EYKCEGFLEKNRDTVYDMLVEILRASK----------------------------------------------------- 582
Cdd:cd01385 481 KYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligidpvavfrwavlrafframaafreagrrraqrtaghsltlhdrt 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 583 -------------------FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPS 643
Cdd:cd01385 561 tksllhlhkkkkppsvsaqFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 644 RWTYIEFYSRYGILMTKQELSfsdKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd01385 641 RYTFQEFITQFQVLLPKGLIS---SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
87-696 |
0e+00 |
|
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: 563.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 87 LRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMD---PHIFAVAEEAYKQM----ARNNRNQSIIV 159
Cdd:cd14892 7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASsppPHVFSIAERAYRAMkgvgKGQGTPQSIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 160 SGESGAGKTVSARYAMRYFATVSKSGS---------NAH--VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14892 86 SGESGAGKTEASKYIMKYLATASKLAKgastskgaaNAHesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 229 QNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQK 308
Cdd:cd14892 166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKV--FCELLGLESGRVAQWLCNRKIVTSSETVV 386
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVakAAGLLGVDAAELMFKLVTQTTSTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 387 K-PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQ----------FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYA 455
Cdd:cd14892 326 EiKLTAREAKNALDALCKYLYGELFDWLISRINACHKqqtsgvtggaASPTFSPFIGILDIFGFEIMPTNSFEQLCINFT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 456 NEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPH-GTDENWLQKLYNNFVNRN 533
Cdd:cd14892 406 NEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKRkTTDKQLLTIYHQTHLDKH 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 534 PLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRA-SKFRSSLYLLMETLNATTPHYVRCIKPNDEKL 612
Cdd:cd14892 486 PHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSsSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKF 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 613 PFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL---MTKQELSFSDK------KEVCKVVLHRLiqDS 683
Cdd:cd14892 566 PGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLarnKAGVAASPDACdattarKKCEEIVARAL--ER 643
|
650
....*....|...
gi 2462545112 684 NQYQFGKTKIFFR 696
Cdd:cd14892 644 ENFQLGRTKVFLR 656
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
81-694 |
0e+00 |
|
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: 560.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGD---MDPHIFAVAEEAYKQMARNNR- 153
Cdd:cd14901 1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 154 ---NQSIIVSGESGAGKTVSARYAMRYFATVS---KSGSNA----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14901 80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsatTHGQNAtereNVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 224 ISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTV-IEGVNDRAE 302
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 303 MVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTS 381
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 382 SETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF--SGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKL 459
Cdd:cd14901 320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYseSTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 460 QQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPL-FE 537
Cdd:cd14901 400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFsVS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 538 KPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS-----------KFRSSLYLLMETLNATTPHYVRCIK 606
Cdd:cd14901 480 KLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSsnaflsstvvaKFKVQLSSLLEVLNATEPHFIRCIK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 607 PNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQElsfSDKKEVCKVVLHR-------- 678
Cdd:cd14901 560 PNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGA---SDTWKVNELAERLmsqlqhse 636
|
650
....*....|....*..
gi 2462545112 679 -LIQDSNQYQFGKTKIF 694
Cdd:cd14901 637 lNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
82-696 |
2.85e-179 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 554.36 E-value: 2.85e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd01387 2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSGSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMSTYL 241
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNL-VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQM 321
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 322 DVFKILAAILHLGNV-----QITAvGNERSSVSEDdSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd01387 239 SIFRILASVLHLGNVyfhkrQLRH-GQEGVSVGSD-AEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 476
Cdd:cd01387 317 ARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 477 KEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMSNTSFVIQHFADKV 555
Cdd:cd01387 397 REQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMPLPEFTIKHYAGQV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 556 EYKCEGFLEKNRDTVYDMLVEILRASK----------------------------------------FRSSLYLLMETLN 595
Cdd:cd01387 476 WYQVHGFLDKNRDQLRQDVLELLVSSRtrvvahlfsshraqtdkapprlgkgrfvtmkprtptvaarFQDSLLQLLEKME 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 596 ATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMtKQELSFSDKKEVCKVV 675
Cdd:cd01387 556 RCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLV-ALKLPRPAPGDMCVSL 634
|
650 660
....*....|....*....|...
gi 2462545112 676 LHRL--IQDSNQYQFGKTKIFFR 696
Cdd:cd01387 635 LSRLctVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
82-696 |
3.32e-178 |
|
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: 551.32 E-value: 3.32e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14873 2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSK-------SGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQII 233
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQqslelslKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 234 GANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLL 313
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 314 GFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSsvseDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEfITAGGAQVS----FKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 393 QAVNARDALAKKIYAHLFDFIVERINQALQfsGKQH-TFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLE 471
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRIK--GKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 472 QEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHF 551
Cdd:cd14873 395 QLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHAN-NHFYVKPRVAVNNFGVKHY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 552 ADKVEYKCEGFLEKNRDTVYDMLVEILR----------------------------------ASKFRSSLYLLMETLNAT 597
Cdd:cd14873 474 AGEVQYDVRGILEKNRDTFRDDLLNLLResrfdfiydlfehvssrnnqdtlkcgskhrrptvSSQFKDSLHSLMATLSSS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 598 TPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMtKQELSFSDKKEVCKVVLH 677
Cdd:cd14873 554 NPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLM-RNLALPEDVRGKCTSLLQ 632
|
650
....*....|....*....
gi 2462545112 678 RLIQDSNQYQFGKTKIFFR 696
Cdd:cd14873 633 LYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
81-696 |
7.69e-173 |
|
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: 536.83 E-value: 7.69e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14904 1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 160 SGESGAGKTVSARYAMRYFATVSkSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd14904 80 SGESGAGKTETTKIVMNHLASVA-GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGN---TVIEGVNDRAEMVETQKTFTLLGFK 316
Cdd:cd14904 159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQY--LGDSlaqMQIPGLDDAKLFASTQKSLSLIGLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 317 EDFQMDVFKILAAILHLGNVQITAVGnERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd14904 237 NDAQRTLFKILSGVLHLGEVMFDKSD-ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd14904 316 NRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 476 MKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNR--NPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd14904 396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKkdNESIDFPKVKRTQFIINHYAG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 554 KVEYKCEGFLEKNRDTV------------YDMLVEILRA-----------------------SKFRSSLYLLMETLNATT 598
Cdd:cd14904 476 PVTYETVGFMEKHRDTLqndlldlvllssLDLLTELFGSseapsetkegksgkgtkapkslgSQFKTSLSQLMDNIKTTN 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 599 PHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIlMTKQELSFSDKKEVCKVVLHR 678
Cdd:cd14904 556 THYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI-MFPPSMHSKDVRRTCSVFMTA 634
|
650
....*....|....*....
gi 2462545112 679 LIQDSN-QYQFGKTKIFFR 696
Cdd:cd14904 635 IGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
81-696 |
1.12e-171 |
|
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: 534.27 E-value: 1.12e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14888 1 ASILHSLNLRFDIDE-IYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 160 SGESGAGKTVSARYAMRYFATVsksGSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN---- 230
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLACA---GSEDikkrsLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKskrm 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 231 -----QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQS-------EFKHLKLG----------------SAEE 282
Cdd:cd14888 156 sgdrgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyEENDEKLAkgadakpisidmssfePHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 283 FNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQ-ITAVGNERSSV--SEDDSHLKVFC 359
Cdd:cd14888 236 FRYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVvsASCTDDLEKVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 360 ELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHT-FIGVLDIYG 438
Cdd:cd14888 316 SLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLlFCGVLDIFG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 439 FETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGT 517
Cdd:cd14888 396 FECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 518 DENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK--------------- 582
Cdd:cd14888 476 DQGLCNKLCQKHKG-HKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKnpfisnlfsaylrrg 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 583 ----------------FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWT 646
Cdd:cd14888 555 tdgntkkkkfvtvsseFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLS 634
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 647 YIEFYSRYGILMTKQE-LSFSdkkevckvvlhrliqdsnQYQFGKTKIFFR 696
Cdd:cd14888 635 HAEFYNDYRILLNGEGkKQLS------------------IWAVGKTLCFFK 667
|
|
| Myo5b_CBD |
cd15477 |
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ... |
1323-1694 |
2.87e-162 |
|
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: 497.46 E-value: 2.87e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1323 REDEAKLIQNLILDLKPRgVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSN 1402
Cdd:cd15477 1 KEDEALLIRNLVTDLKPQ-AVSATVPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1403 TCHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISG 1482
Cdd:cd15477 80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1483 LKPTGFRKRSSSIDDTD-GYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQI 1561
Cdd:cd15477 160 VKPMGYRKRSSSMADGDnSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1562 RCNISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPS 1641
Cdd:cd15477 240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 1642 FVRKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKLGFL 1694
Cdd:cd15477 320 FIRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
82-696 |
9.63e-162 |
|
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: 508.34 E-value: 9.63e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14927 2 SVLHNLRRRYS-RWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSGSN-------------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDE 228
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGpgkkaqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 229 QNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQ 307
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-LSGKKPELQDMLLVSMNPYDYHFCSqGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 308 KTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVK 387
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 388 PMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHV 467
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSN--- 543
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKkrk 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 544 --TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS--KFRSSLY------------------------------- 588
Cdd:cd14927 480 yeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSqnKLLATLYenyvgsdstedpksgvkekrkkaasfqtvsq 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 589 -------LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ 661
Cdd:cd14927 560 lhkenlnKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSA 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 2462545112 662 --ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14927 640 ipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1323-1697 |
2.47e-160 |
|
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: 492.62 E-value: 2.47e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1323 REDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSN 1402
Cdd:cd15478 1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1403 TCHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISG 1482
Cdd:cd15478 81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1483 LKPTGFRKRSSSIDDTDGYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIR 1562
Cdd:cd15478 161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1563 CNISYLEEWLKDKNLQNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSF 1642
Cdd:cd15478 241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462545112 1643 VRKVQALLNSREDSSQLMLDTKYLFQVTFPFTPSPHALEMIQIPSSFKLGFLNRL 1697
Cdd:cd15478 321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-696 |
9.90e-158 |
|
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: 497.23 E-value: 9.90e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14920 2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKS--GSNAH-----VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIG 234
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASShkGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 235 ANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQETMEAMHIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14920 240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14920 320 DFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPRM--SNTSFV 547
Cdd:cd14920 400 EYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQE-QGSHSKFQKPRQlkDKADFC 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK--------------------------------------------- 582
Cdd:cd14920 479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdrfvaelwkdvdrivgldqvtgmtetafgsayktkkgmfrtvgql 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 583 FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ- 661
Cdd:cd14920 559 YKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAi 638
|
650 660 670
....*....|....*....|....*....|....*
gi 2462545112 662 ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14920 639 PKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
81-696 |
1.37e-157 |
|
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: 496.42 E-value: 1.37e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14929 1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGAN 236
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 237 MSTYLLEKSRVVFQSENERNYHIFYQLCASAQqsEFKHLKLGSA--EEFNYTRMGGNTViEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKK--ELRDLLLVSAnpSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14929 237 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEE 474
Cdd:cd14929 317 TYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 475 YMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQ---- 549
Cdd:cd14929 397 YRKEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelv 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRASKFR--------------------------------SSLY-----LLME 592
Cdd:cd14929 477 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRllaslfenyistdsaiqfgekkrkkgasfqtvASLHkenlnKLMT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 593 TLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK--QELSFSDKKE 670
Cdd:cd14929 557 NLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRtfPKSKFVSSRK 636
|
650 660
....*....|....*....|....*.
gi 2462545112 671 VCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14929 637 AAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-696 |
2.48e-157 |
|
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: 495.90 E-value: 2.48e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14909 1 ASVLHNLRQRY-YAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKS-------GSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQII 233
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVGASkktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 234 GANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTFTL 312
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLLSDNIYDYYIVSqGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 313 LGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 393 QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQ 472
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 473 EEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTS-----F 546
Cdd:cd14909 399 EEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaahF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 547 VIQHFADKVEYKCEGFLEKNR----DTVYD--------MLVEILR--------------------------ASKFRSSLY 588
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKdplnDTVVDqfkksqnkLLIEIFAdhagqsgggeqakggrgkkgggfatvSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 589 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDK 668
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEEDP 638
|
650 660
....*....|....*....|....*...
gi 2462545112 669 KEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14909 639 KKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
81-696 |
1.59e-156 |
|
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: 493.80 E-value: 1.59e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14913 1 PAVLYNLKDRYT-SWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGSNAH---------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDLAKkkdskmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTF 310
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQIL-SNKKPELIELLLITTNPYDYPFISqGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 311 TLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRM----SNTS 545
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVvkgrAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK-------------------------------------FRSSLY 588
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSnrllahlyatfatadadsgkkkvakkkgssfqtvsalFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 589 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ--ELSFS 666
Cdd:cd14913 559 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAipEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 2462545112 667 DKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14913 639 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
81-696 |
2.56e-155 |
|
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: 490.96 E-value: 2.56e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY------SGQNM---GDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14908 1 PAILHSLSRRFFRGI-IYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAHVE----------DKVLASNPITEAVGNAKTTRNDNSSRFGK 220
Cdd:cd14908 80 IRaSQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 221 YTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGS--------AEEFNYTRMGGNT 292
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 293 VIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVS---EDDSHLKVFCELLGLESGRV 369
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 370 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ--HTFIGVLDIYGFETFDVNSF 447
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 448 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLP-HGTDENWLQKL 525
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 526 YNNFVNRNP--LFEKPRMSNTS-------FVIQHFADKVEYKCE-GFLEKNRDTVyDMLVEILRAS--KFRSSLYLLMET 593
Cdd:cd14908 480 YETYLPEKNqtHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKDEI-PLTADSLFESgqQFKAQLHSLIEM 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 594 LNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMT---KQELSFSDK-- 668
Cdd:cd14908 559 IEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPlipEVVLSWSMErl 638
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462545112 669 -------KEVCKV-VLHRLIQD--------SNQYQFGKTKIFFR 696
Cdd:cd14908 639 dpqklcvKKMCKDlVKGVLSPAmvsmknipEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
83-696 |
6.94e-154 |
|
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: 485.35 E-value: 6.94e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDM-DPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14897 3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYL 241
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPS-DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 242 LEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRAEMVETQKTFT-------LLG 314
Cdd:cd14897 161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILR-DDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 315 F-KEDFQMdVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14897 240 FsEEDISV-IFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 394 AVNARDALAKKIYAHLFDFIVERINQAL----QFSGK-QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMtRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 469 KLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLyNNFVNRNPLFEKPRMSNTSFV 547
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK-----------FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEF 616
Cdd:cd14897 478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNnefisdlftsyFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKF 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 617 DSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHrlIQDSNQYQFGKTKIFFR 696
Cdd:cd14897 558 DDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
81-696 |
1.91e-152 |
|
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: 481.85 E-value: 1.91e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFA-ESKLIYTYSGIILVAMNPYKQLPiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNN---RNQS 156
Cdd:cd14891 1 AGILHNLEERSKlDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 157 IIVSGESGAGKTVSARYAMRYFATVS-----------------KSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFG 219
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 220 KYTEISF-DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVN 298
Cdd:cd14891 158 KFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 299 DRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI----TAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLC 374
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 375 NRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFD-VNSFEQFCIN 453
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLIN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 454 YANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFvNR 532
Cdd:cd14891 398 YANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTH-KR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 533 NPLF--EKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS-KFRSSLYLLMETLNATTPHYVRCIKPND 609
Cdd:cd14891 477 HPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSaKFSDQMQELVDTLEATRCNFIRCIKPNA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 610 EKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSF--SDKKEVCKVVLHRLIQDSNQYQ 687
Cdd:cd14891 557 AMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLfaENDRTLTQAILWAFRVPSDAYR 636
|
....*....
gi 2462545112 688 FGKTKIFFR 696
Cdd:cd14891 637 LGRTRVFFR 645
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
82-696 |
5.78e-151 |
|
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: 479.09 E-value: 5.78e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14911 2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVS-----KSGSNAH-----------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEIS 225
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkGSGAVPHpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 226 FDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRmGGNTVIEGVNDRAEMVE 305
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 306 TQKTFTLLGF-KEDFQMdVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSET 384
Cdd:cd14911 240 TVKSMNIMGMtSEDFNS-IFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 385 VVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQF 463
Cdd:cd14911 319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 464 NMHVFKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMS 542
Cdd:cd14911 399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDFR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 543 NTS-FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK----------------------------------FRSSL 587
Cdd:cd14911 478 GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQdpfvvniwkdaeivgmaqqaltdtqfgartrkgmFRTVS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 588 YL-------LMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK 660
Cdd:cd14911 558 HLykeqlakLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN 637
|
650 660 670
....*....|....*....|....*....|....*..
gi 2462545112 661 Q-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14911 638 ViPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
83-696 |
6.19e-149 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 473.36 E-value: 6.19e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP---------IYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14907 3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 154 NQSIIVSGESGAGKTVSARYAMRYFATVS------------------KSGSNAHVEDKVLASNPITEAVGNAKTTRNDNS 215
Cdd:cd14907 82 KQAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevltltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 216 SRFGKYTEISFDEQNQ-IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL---GSAEEFNYTRMGGN 291
Cdd:cd14907 162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLknqLSGDRYDYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 292 TVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI---TAVGNERSSVSeDDSHLKVFCELLGLESGR 368
Cdd:cd14907 242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddsTLDDNSPCCVK-NKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 369 VAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL--QFSGKQHTF------IGVLDIYGFE 440
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 441 TFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTL--IDFYDNQPVIDLIE-AKMGILELLDEECLLPHGT 517
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDkPPIGIFNLLDDSCKLATGT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 518 DENWLQKLYNNFvNRNPLFEKPRMSN-TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS--------------- 581
Cdd:cd14907 481 DEKLLNKIKKQH-KNNSKLIFPNKINkDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSknriissifsgedgs 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 582 --------------------KFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSY 641
Cdd:cd14907 560 qqqnqskqkksqkkdkflgsKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGY 639
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2462545112 642 PSRWTYIEFYSRYGILmtkqelsfsdkkevckvvlhrliqdSNQYQFGKTKIFFR 696
Cdd:cd14907 640 PYRKSYEDFYKQYSLL-------------------------KKNVLFGKTKIFMK 669
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
81-696 |
3.51e-147 |
|
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: 468.43 E-value: 3.51e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14917 1 PAVLYNLKERYA-SWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGSNAH---------VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDRSKkdqtpgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTF 310
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQIL-SNKKPELLDMLLITNNPYDYAFISqGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 311 TLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSNTS 545
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnikgKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKF-------------------------------------RSSLY 588
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLkllsnlfanyagadapiekgkgkakkgssfqtvsalhRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 589 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ--ELSFS 666
Cdd:cd14917 559 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAipEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 2462545112 667 DKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14917 639 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
83-696 |
7.14e-146 |
|
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: 464.77 E-value: 7.14e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQM----ARNNRNQSII 158
Cdd:cd14889 3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 159 VSGESGAGKTVSARYAMRYFATVSKSgsNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMS 238
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRG--NSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKED 318
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 319 FQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSH-LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNA 397
Cdd:cd14889 239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGwLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 398 RDALAKKIYAHLFDFIVERINQAL----QFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14889 319 RDSIAKVAYGRVFGWIVSKINQLLapkdDSSVELRE-IGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 474 EYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFvNRNPLFEKPRMSNTSFVIQHFA 552
Cdd:cd14889 398 EYKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKLNIHF-KGNSYYGKSRSKSPKFTVNHYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 553 DKVEYKCEGFLEKNRDTV-----------YDMLVEILRAS--------------------------------KFRSSLYL 589
Cdd:cd14889 477 GKVTYNASGFLEKNRDTIpasirtlfinsATPLLSVLFTAtrsrtgtlmpraklpqagsdnfnstrkqsvgaQFKHSLGV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 590 LMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSdkK 669
Cdd:cd14889 557 LMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEPALPGT--K 634
|
650 660
....*....|....*....|....*..
gi 2462545112 670 EVCKVVLHRliQDSNQYQFGKTKIFFR 696
Cdd:cd14889 635 QSCLRILKA--TKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-696 |
6.58e-144 |
|
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: 459.88 E-value: 6.58e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14932 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSG-----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRAEMVETQK 308
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL---EDYSKYRFlsNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHV 467
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPR--M 541
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGN-NPKFQKPKklK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 542 SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS--KFRSSLYL------------------------------ 589
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQStdKFVSELWKdvdrivgldkvagmgeslhgafktrkgmfr 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 590 ------------LMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL 657
Cdd:cd14932 557 tvgqlykeqlmnLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2462545112 658 M-TKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14932 637 TpNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
82-696 |
6.85e-144 |
|
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: 459.49 E-value: 6.85e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14934 2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSGSNA-----HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGAN 236
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 237 MSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKL-GSAEEFNYTRMGgNTVIEGVNDRAEMVETQKTFTLLGF 315
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 316 KEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAV 395
Cdd:cd14934 240 SAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 396 NARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEY 475
Cdd:cd14934 320 NSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 476 MKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKP-----RMSNTSFVIQ 549
Cdd:cd14934 400 KREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGPEAHFELV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILRASK--------------------------------FRSSLYLLMETLNAT 597
Cdd:cd14934 480 HYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSlgllallfkeeeapagskkqkrgssfmtvsnfYREQLNKLMTTLHST 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 598 TPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ-ELSFSDKKEVCKVVL 676
Cdd:cd14934 560 APHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNViPQGFVDNKKASELLL 639
|
650 660
....*....|....*....|
gi 2462545112 677 HRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14934 640 GSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
81-696 |
1.88e-143 |
|
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: 458.81 E-value: 1.88e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14912 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQK 308
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMLLITTNPYDYPFVSqGEISVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14912 319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRM----SN 543
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK----------------------------------------F 583
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAmktlaylfsgaqtaegasagggakkggkkkgssfqtvsalF 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 584 RSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ-- 661
Cdd:cd14912 559 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAip 638
|
650 660 670
....*....|....*....|....*....|....*
gi 2462545112 662 ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14912 639 EGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
81-696 |
2.35e-143 |
|
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: 458.37 E-value: 2.35e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14916 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSG----------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAIGdrskkenpnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCaSAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKT 309
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQIL-SNKKPELLDMLLVTNNPYDYAFVSqGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 310 FTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 390 TRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFK 469
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSNT 544
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKF--------------------------------------RSS 586
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLklmatlfstyasadtgdsgkgkggkkkgssfqtvsalhREN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 587 LYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL--MTKQELS 664
Cdd:cd14916 559 LNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpAAIPEGQ 638
|
650 660 670
....*....|....*....|....*....|..
gi 2462545112 665 FSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14916 639 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
81-696 |
1.95e-142 |
|
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: 455.73 E-value: 1.95e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14918 1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKTF 310
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 311 TLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMT 390
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 471 EQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRM----SNTS 545
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK-------------------------------------FRSSLY 588
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAmktlaslfstyasaeadsgakkgakkkgssfqtvsalFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 589 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ--ELSFS 666
Cdd:cd14918 559 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAipEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 2462545112 667 DKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14918 639 DSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
81-696 |
3.67e-142 |
|
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: 454.96 E-value: 3.67e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14910 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQK 308
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPDLIEMLLITTNPYDYAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14910 319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSN---- 543
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgkve 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK--------------------------------------FRS 585
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSmktlallfsgaaaaeaeegggkkggkkkgssfqtvsalFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 586 SLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ--EL 663
Cdd:cd14910 559 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAipEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 2462545112 664 SFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14910 639 QFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-696 |
8.06e-141 |
|
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: 451.45 E-value: 8.06e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14923 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGS----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAVTGDkkkeqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQKT 309
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQI-MSNKKPELIDLLLISTNPFDFPFVSqGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 310 FTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPM 389
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 390 TRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFK 469
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 470 LEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSNT 544
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpakgKAEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK---------------------------------------FRS 585
Cdd:cd14923 479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSlkllsflfsnyagaeagdsggskkggkkkgssfqtvsavFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 586 SLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ--EL 663
Cdd:cd14923 559 NLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAipEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 2462545112 664 SFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14923 639 QFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
81-696 |
1.25e-140 |
|
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: 450.72 E-value: 1.25e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14915 1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGS-----------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLcASAQQSEFKHLKLGSAEEFNYTRMG-GNTVIEGVNDRAEMVETQK 308
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-MSNKKPELIEMLLITTNPYDFAFVSqGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd14915 239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVF 468
Cdd:cd14915 319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 469 KLEQEEYMKEDIPWTLIDF-YDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR----MSN 543
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKpakgKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK--------------------------------------FRS 585
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGmktlaflfsggqtaeaeggggkkggkkkgssfqtvsalFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 586 SLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ--EL 663
Cdd:cd14915 559 NLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAipEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 2462545112 664 SFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14915 639 QFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
82-696 |
5.62e-138 |
|
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: 443.69 E-value: 5.62e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14921 2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSGSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIG 234
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGkkdtsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 235 ANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEF-NYTRMG-GNTVIEGVNDRAEMVETQKTFTL 312
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLL---EGFnNYTFLSnGFVPIPAAQDDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 313 LGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRP 392
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 393 QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLE 471
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 472 QEEYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRM--SNTS 545
Cdd:cd14921 398 QEEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGN-HPKFQKPKQlkDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 546 FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK------------------------------------------- 582
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkdvdrivgldqmakmtesslpsasktkkgmfrtvg 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 583 --FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTK 660
Cdd:cd14921 557 qlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 636
|
650 660 670
....*....|....*....|....*....|....*..
gi 2462545112 661 Q-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14921 637 AiPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
81-696 |
6.58e-137 |
|
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: 442.41 E-value: 6.58e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY--------SGQNMGDMDPHIFAVAEEAYKQMARN 151
Cdd:cd14902 1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 152 NR-NQSIIVSGESGAGKTVSARYAMRYFATV-------SKSGSNA-HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14902 80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsstEQEGSDAvEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 223 EISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEF----NYTRMGGNTVIEGVN 298
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellnSYGPSFARKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 299 DRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVS---EDDSHLKVFCELLGLESGRVAQWLCN 375
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvtaASRFHLAKCAELMGVDVDKLETLLSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 376 RKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTF---------IGVLDIYGFETFDVNS 446
Cdd:cd14902 320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 447 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKL 525
Cdd:cd14902 400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 526 YNNFVNRNplfekprmsntSFVIQHFADKVEYKCEGFLEKNRDTV------------YDMLVEI---------------- 577
Cdd:cd14902 480 YRYHGGLG-----------QFVVHHFAGRVCYNVEQFVEKNTDALpadasdilssssNEVVVAIgadenrdspgadngaa 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 578 -------LRA----SKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWT 646
Cdd:cd14902 549 grrrysmLRApsvsAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLA 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 647 YIEFYSRYGILMTKQELSFSDKK-------------EVCKVVLHRLIQDSNQ-------------------------YQF 688
Cdd:cd14902 629 HASFIELFSGFKCFLSTRDRAAKmnnhdlaqalvtvLMDRVLLEDGVEREEKnpgaltavtgdgsgtafendcrrkdVQV 708
|
....*...
gi 2462545112 689 GKTKIFFR 696
Cdd:cd14902 709 GRTLVFCK 716
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
71-746 |
1.76e-136 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 444.47 E-value: 1.76e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 71 DLTALSYLHEPAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQMA 149
Cdd:PTZ00014 100 DIGLLPHTNIPCVLDFLKHRY-LKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 150 RNNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQ 229
Cdd:PTZ00014 179 GVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 230 NQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRAEMVETQK 308
Cdd:PTZ00014 259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLdVPGIDDVKDFEEVME 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITavGNERSSVSE----DDSHLKVF---CELLGLESGRVAQWLCNRKIVTS 381
Cdd:PTZ00014 337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIE--GKEEGGLTDaaaiSDESLEVFneaCELLFLDYESLKKELTVKVTYAG 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 382 SETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:PTZ00014 415 NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 462 QFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKM-GILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR 540
Cdd:PTZ00014 495 NFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGkSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKV 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 541 MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS---------------------------KFRSSLYLLMET 593
Cdd:PTZ00014 575 DSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASpnplvrdlfegvevekgklakgqligsQFLNQLDSLMSL 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 594 LNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL-MTKQELSFSDKKEVC 672
Cdd:PTZ00014 655 INSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAVSNDSSLDPKEKA 734
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545112 673 KVVLHRLIQDSNQYQFGKTKIFFR---AGQVAYLEKLRLDKLRQSCVMVQKHMRGWLQRKKFLRERRAALIIQQYFR 746
Cdd:PTZ00014 735 EKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-696 |
4.48e-136 |
|
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: 438.37 E-value: 4.48e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14930 2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKS-------GSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIG 234
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSpkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 235 ANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTviEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14930 319 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPR--MSNTSFV 547
Cdd:cd14930 399 EYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE-QGGHPKFQRPRhlRDQADFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK-------------------------------------------FR 584
Cdd:cd14930 478 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTdrltaeiwkdvegivgleqvsslgdgppggrprrgmfrtvgqlYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 585 SSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ-EL 663
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAiPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 2462545112 664 SFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
83-657 |
6.81e-136 |
|
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: 436.27 E-value: 6.81e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 150
Cdd:cd14900 3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 151 --NNR--NQSIIVSGESGAGKTVSARYAMRYFA---------TVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSR 217
Cdd:cd14900 82 glNGVmsDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 218 FGKYTEISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKhlklgsaeEFNYTRMggntviegv 297
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK--------RDMYRRV--------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 298 ndraemvetQKTFTLLGFKEDFQMDVFKILAAILHLGNVQItAVGNERSSVSEDDSHLKVFCE--------LLGLESGRV 369
Cdd:cd14900 225 ---------MDAMDIIGFTPHERAGIFDLLAALLHIGNLTF-EHDENSDRLGQLKSDLAPSSIwsrdaaatLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 370 AQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQF--SGKQHT---FIGVLDIYGFETFDV 444
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMddSSKSHGglhFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 445 NSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQ 523
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 524 KLYNNFVNrNPLFEKPRMSNTS--FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS-KFRSSLYLLMETLNATTPH 600
Cdd:cd14900 455 KLYRACGS-HPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGlQFKEQLTTLLETLQQTNPH 533
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545112 601 YVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL 657
Cdd:cd14900 534 YVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
81-696 |
1.08e-134 |
|
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: 435.92 E-value: 1.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDaiIHAYSGQNMGDMD--PHIFAVAEEAYKQMARNN------ 152
Cdd:cd14895 1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPGLYD--LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRRLhepgas 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 153 -RNQSIIVSGESGAGKTVSARYAMRYFATVSKSG--------SNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTE 223
Cdd:cd14895 78 kKNQTILVSGESGAGKTETTKFIMNYLAESSKHTtatssskrRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 224 ISF-----DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFK--HLKLGSAEEFNYTRMGGNTVI-E 295
Cdd:cd14895 158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelQLELLSAQEFQYISGGQCYQRnD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 296 GVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVqitAVGNERSSVSEDDS---------------------H 354
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNV---LFVASSEDEGEEDNgaasapcrlasaspssltvqqH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 355 LKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQA---LQFSGKQHT-- 429
Cdd:cd14895 315 LDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAspqRQFALNPNKaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 430 ------FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MG 502
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 503 ILELLDEECLLPHGTDENWLQKLYNNFVNRNPlFEKPR--MSNTSFVIQHFADKVEYKCEGFLEKNRDT----VYDM--- 573
Cdd:cd14895 475 IFSLLDEECVVPKGSDAGFARKLYQRLQEHSN-FSASRtdQADVAFQIHHYAGAVRYQAEGFCEKNKDQpnaeLFSVlgk 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 574 ----------------------------------LVEILRASKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSK 619
Cdd:cd14895 554 tsdahlrelfeffkasesaelslgqpklrrrssvLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMA 633
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545112 620 RIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKvVLHRLiqdsnQYQFGKTKIFFR 696
Cdd:cd14895 634 KVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIE-TLKVD-----HAELGKTRVFLR 704
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
82-696 |
1.69e-134 |
|
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: 434.14 E-value: 1.69e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14919 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSGSN----AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANM 237
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSkkdqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 238 STYLLEKSRVVFQSENERNYHIFYQLCASAQQsefkHLKLG-SAEEFNYTRM--GGNTVIEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE----HLKTDlLLEPYNKYRFlsNGHVTIPGQQDKDMFQETMEAMRIMG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14919 237 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 395 VNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14919 317 DFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 474 EYMKEDIPWTLIDF-YDNQPVIDLIEAKM---GILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPRM--SNTSFV 547
Cdd:cd14919 397 EYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQE-QGTHPKFQKPKQlkDKADFC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 548 IQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS--KFRSSLY------------------------------------- 588
Cdd:cd14919 476 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdKFVSELWkdvdriigldqvagmsetalpgafktrkgmfrtvgql 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 589 ------LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQ- 661
Cdd:cd14919 556 ykeqlaKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSi 635
|
650 660 670
....*....|....*....|....*....|....*
gi 2462545112 662 ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14919 636 PKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
81-694 |
6.69e-134 |
|
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: 431.72 E-value: 6.69e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSG-QNMGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14876 1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 160 SGESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMST 239
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 240 YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYtrMGGNTV-IEGVNDRAEMVETQKTFTLLGFKED 318
Cdd:cd14876 160 FLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKF--LNPKCLdVPGIDDVADFEEVLESLKSMGLTEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 319 FQMDVFKILAAILHLGNVQITA-----VGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14876 238 QIDTVFSIVSGVLLLGNVKITGkteqgVDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 394 AVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14876 318 AEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 474 EYMKEDIPWTLIDFYDNQPVID-LIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFA 552
Cdd:cd14876 398 LYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSNINFIVVHTI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 553 DKVEYKCEGFLEKNRDTVYDMLVEILRASK---------------------------FRSSLYLLMETLNATTPHYVRCI 605
Cdd:cd14876 478 GDIQYNAEGFLFKNKDVLRAELVEVVQASTnpvvkalfegvvvekgkiakgsligsqFLKQLESLMGLINSTEPHFIRCI 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 606 KPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGIL-MTKQELSFSDKKEVCKVVLHRLIQDSN 684
Cdd:cd14876 558 KPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLdLGIANDKSLDPKVAALKLLESSGLSED 637
|
650
....*....|
gi 2462545112 685 QYQFGKTKIF 694
Cdd:cd14876 638 EYAIGKTMVF 647
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
82-696 |
6.21e-133 |
|
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: 429.87 E-value: 6.21e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd15896 2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKS-----------GSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLgsaEEFNYTRM--GGNTVIEGVNDRAEMVETQK 308
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL---ENYNNYRFlsNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 309 TFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKP 388
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 389 MTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHV 467
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 468 FKLEQEEYMKEDIPWTLIDF-YDNQPVIDLIE---AKMGILELLDEECLLPHGTDENWLQKLYNNfVNRNPLFEKPR--M 541
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQE-QGTHPKFFKPKklK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 542 SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS--KFRSSLY------------------------------- 588
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQStdKFVSELWkdvdrivgldkvsgmsempgafktrkgmfrt 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 589 ----------LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILM 658
Cdd:cd15896 557 vgqlykeqlsKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670
....*....|....*....|....*....|....*....
gi 2462545112 659 TKQ-ELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd15896 637 PNAiPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
83-694 |
6.68e-132 |
|
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: 426.57 E-value: 6.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFAESkLIYTYSGIILVAMNPYKQLP-IYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYK--QMARNNRNQSII 158
Cdd:cd14880 3 VLRCLQARYTAD-TFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 159 VSGESGAGKTVSARYAMRYFATVSKSGSN-------AHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14880 82 VSGESGAGKTWTSRCLMKFYAVVAASPTSweshkiaERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 232 IIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEgvnDRAEMveTQKTFT 311
Cdd:cd14880 162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE---DCFEV--TREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 312 LLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSS---VSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVV-- 386
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVfk 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 387 KPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNM 465
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSIcADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 466 HVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMS-N 543
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSpISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSrE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 544 TSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEIL----------------------------RA------SKFRSSLYL 589
Cdd:cd14880 477 PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLqqsqdpllqklfpanpeektqeepsgqsRApvltvvSKFKASLEQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 590 LMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKK 669
Cdd:cd14880 557 LLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLRPHTSSGPH 636
|
650 660
....*....|....*....|....*
gi 2462545112 670 EVCKVVLHrliqdSNQYQFGKTKIF 694
Cdd:cd14880 637 SPYPAKGL-----SEPVHCGRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
83-696 |
1.42e-128 |
|
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: 416.98 E-value: 1.42e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQNMG-----DMDPHIFAVAEEAYKQMARNNRNQS 156
Cdd:cd14886 3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 157 IIVSGESGAGKTVSARYAMRYFATVSKSGSNAhVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGAN 236
Cdd:cd14886 82 CIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 237 MSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFK 316
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKLFSK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 317 EDFQmDVFKILAAILHLGNVQ---ITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14886 241 NEID-SFYKCISGILLAGNIEfseEGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 394 AVNARDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQE 473
Cdd:cd14886 320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 474 EYMKEDIPWTLIDFYDNQPVIDLIEA-KMGILELLDEECLLPHGTDENWLQKLYNNFvnRNPLFEKPRMSNTSFVIQHFA 552
Cdd:cd14886 400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSCKSKI--KNNSFIPGKGSQCNFTIVHTA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 553 DKVEYKCEGFLEKNRDTVYDMLVEILR--------------------------ASKFRSSLYLLMETLNATTPHYVRCIK 606
Cdd:cd14886 478 ATVTYNTEEFVDKNKHKLSVDILELLMgstnpivnkafsdipnedgnmkgkflGSTFQLSIDQLMKTLSATKSHFIRCIK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 607 PNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSF---SDKKEVCKVVLHRLIQDS 683
Cdd:cd14886 558 TNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQnagEDLVEAVKSILENLGIPC 637
|
650
....*....|...
gi 2462545112 684 NQYQFGKTKIFFR 696
Cdd:cd14886 638 SDYRIGKTKVFLR 650
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
81-696 |
9.48e-125 |
|
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: 406.09 E-value: 9.48e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14896 1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGSNAHVE--DKVLasnPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMS 238
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKED 318
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 319 FQMDVFKILAAILHLGNVQITAVGNERSSVSE--DDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSSSERESQEVAAvsSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQHTF--IGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEE 474
Cdd:cd14896 316 ARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 475 YMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNrNPLFEKPRMSNTSFVIQHFAD 553
Cdd:cd14896 396 CQRELLPWVPIPQPPRESCLDLLVDQpHSLLSILDDQTWLSQATDHTFLQKCHYHHGD-HPSYAKPQLPLPVFTVRHYAG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 554 KVEYKCEGFLEKNRDTVYDMLVEILR---------------------------ASKFRSSLYLLMETLNATTPHYVRCIK 606
Cdd:cd14896 475 TVTYQVHKFLNRNRDQLDPAVVEMLAqsqlqlvgslfqeaepqyglgqgkptlASRFQQSLGDLTARLGRSHVYFIHCLN 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 607 PNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLHRLIQDSNQY 686
Cdd:cd14896 555 PNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRERCGAILSQVLGAESPLY 634
|
650
....*....|
gi 2462545112 687 QFGKTKIFFR 696
Cdd:cd14896 635 HLGATKVLLK 644
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
83-689 |
1.64e-121 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 399.74 E-value: 1.64e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIVS 160
Cdd:cd14906 3 ILNNLGKRY-KSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSGS---------NAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQ 231
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNQqqnnnnnnnNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 232 II-GANMSTYLLEKSRVVFQSENER-NYHIFYQLCASAQQSEFKHLKLGS-AEEFNY-------------TRMGGNTVIE 295
Cdd:cd14906 162 KIdGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdPSKYRYldarddvissfksQSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 296 GVNDRAEMVE--TQKTFTLLGFKEDFQmDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVF---CELLGLESGRVA 370
Cdd:cd14906 242 NKTESIESFQllKQSMESMSINKEQCD-AIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 371 QWLCNRKIVTSSETVV--KPMTRPQAVNARDALAKKIYAHLFDFIVERINQ-----------ALQFSGKQHTFIGVLDIY 437
Cdd:cd14906 321 QALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 438 GFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHG 516
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 517 TDENWLQKLYNNFVNRNPLFEKPrMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS--------------- 581
Cdd:cd14906 481 SEQSLLEKYNKQYHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASsnflkkslfqqqits 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 582 ----------------KFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRW 645
Cdd:cd14906 560 ttnttkkqtqsntvsgQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRR 639
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462545112 646 TYIEFYSRYGILMTKQELSfSDKKEVCKVVLHRLIQDSNQYQFG 689
Cdd:cd14906 640 DFNQFFSRYKCIVDMYNRK-NNNNPKLASQLILQNIQSKLKTMG 682
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
82-695 |
2.28e-113 |
|
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: 374.58 E-value: 2.28e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAESkLIYTY-SGIILVAMNPYKQLPIYGDAIIHAY-------SGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14879 5 AITSHLASRFRSD-LPYTRlGSSALVAVNPYKYLSSNSDASLGEYgseyydtTSGSKEPLPPHAYDLAARAYLRMRRRSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 154 NQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAH-VEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd14879 84 DQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 233 IGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYT-RMGGNTVIEGV--NDRAEMVETQKT 309
Cdd:cd14879 164 IGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLPLGPgsDDAEGFQELKTA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 310 FTLLGFKEDFQMDVFKILAAILHLGNVQIT--AVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNR-KIVtSSEtVV 386
Cdd:cd14879 244 LKTLGFKRKHVAQICQLLAAILHLGNLEFTydHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKtKLV-RKE-LC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 387 KPMTRP-QAVNARDALAKKIYAHLFDFIVERINQALQFSGKQ-HTFIGVLDIYGFETFD---VNSFEQFCINYANEKLQQ 461
Cdd:cd14879 322 TVFLDPeGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDfATFISLLDFPGFQNRSstgGNSLDQFCVNFANERLHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 462 QFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMG--ILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKP 539
Cdd:cd14879 402 YVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGglLGILDDQTRRMPKKTDEQMLEALRKRFGNHSSFIAVG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 540 RMSNTS----FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILR-ASKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPF 614
Cdd:cd14879 482 NFATRSgsasFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRgATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 615 EFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKevckvVLHRLIQDSNQYQFGKTKIF 694
Cdd:cd14879 562 SFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAERIRQC-----ARANGWWEGRDYVLGNTKVF 636
|
.
gi 2462545112 695 F 695
Cdd:cd14879 637 L 637
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
83-696 |
1.42e-110 |
|
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: 367.21 E-value: 1.42e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFAESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAY-SGQNMGDMDPHIFAVAEEAYKQM-ARNNRNQSIIVS 160
Cdd:cd14875 3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVS----KSGSNAHVEDKVLA----SNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 233 -IGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHL-KLGSAEEFNYTRmGGNTVI------EGVNDRAEMV 304
Cdd:cd14875 163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLN-GGNTFVrrgvdgKTLDDAHEFQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 305 ETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNERSSVsEDDSHLKVFCELLGLESGRVAQWLcnrkIVTSSET 384
Cdd:cd14875 242 NVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQI-ADETPFLTACRLLQLDPAKLRECF----LVKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 385 VVKPMTRPQ-AVNARDALAKKIYAHLFDFIVERINQAL--QFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQ 461
Cdd:cd14875 317 LVTILANKTeAEGFRNAFCKAIYVGLFDRLVEFVNASItpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 462 QFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR 540
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 541 MS-NTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS------------------------KFRSSLYLLMETLN 595
Cdd:cd14875 477 STiPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNStdefirtllstekglarrkqtvaiRFQRQLTDLRTELE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 596 ATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSF---SDKKEVC 672
Cdd:cd14875 557 STETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLfkqEKYSEAA 636
|
650 660
....*....|....*....|....*...
gi 2462545112 673 KVVL---HRLIQ-DSNQYQFGKTKIFFR 696
Cdd:cd14875 637 KDFLayyQRLYGwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
82-654 |
3.06e-109 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 365.19 E-value: 3.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 150
Cdd:cd14899 2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 151 NNRNQSIIVSGESGAGKTVSARYAMRYFATVSKSG----------------SNAHVEDKVLASNPITEAVGNAKTTRNDN 214
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGnnnltnsesisppaspSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 215 SSRFGKYTEISF-DEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQL------CASAQQSEFKHLKLGSAEEFNYTR 287
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 288 MGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQITAVGNER------------SSVSEDDSHL 355
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGddtvfadearvmSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 356 KVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGK--------- 426
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 427 ------QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAK 500
Cdd:cd14899 401 vddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 501 -MGILELLDEECLLPHGTDENWLQKLYNNFVNR--NPLFEKPRM--SNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLV 575
Cdd:cd14899 481 pIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKnsHPHFRSAPLiqRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 576 EILRAS---------------------------------------------KFRSSLYLLMETLNATTPHYVRCIKPNDE 610
Cdd:cd14899 561 QLLAGSsnpliqalaagsndedangdseldgfggrtrrraksaiaavsvgtQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2462545112 611 KLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 654
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
82-657 |
1.36e-108 |
|
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: 358.44 E-value: 1.36e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQlpIYGDAIIHAYSgQNMGDMDPHIFAVAEEAYKQMARNNrNQSIIVSG 161
Cdd:cd14898 2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFatVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDeqNQIIGANMSTYL 241
Cdd:cd14898 77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 242 LEKSRVVFQSENERNYHIFYQLCASaqqsefKHLKLGSaEEFNYTRMGGNT-VIEGVNDRAEMVETQ-KTFTLLGFKEdf 319
Cdd:cd14898 153 LEKSRVTHHEKGERNFHIFYQFCAS------KRLNIKN-DFIDTSSTAGNKeSIVQLSEKYKMTCSAmKSLGIANFKS-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 320 qmdVFKILAAILHLGNVQITavgNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARD 399
Cdd:cd14898 224 ---IEDCLLGILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 400 ALAKKIYAHLFDFIVERINQALQFSGKQHtfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKED 479
Cdd:cd14898 298 SMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 480 IPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKL--YNN-FVNRNplfekprmSNTSFVIQHFADKVE 556
Cdd:cd14898 376 IEWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNgFINTK--------ARDKIKVSHYAGDVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 557 YKCEGFLEKNRD----TVYDMLVEILRASK------FRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLR 626
Cdd:cd14898 448 YDLRDFLDKNREkgqlLIFKNLLINDEGSKedlvkyFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLA 527
|
570 580 590
....*....|....*....|....*....|.
gi 2462545112 627 ACGVLETIRISAQSYPSRWTYIEFYSRYGIL 657
Cdd:cd14898 528 ECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
81-696 |
4.37e-97 |
|
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: 330.46 E-value: 4.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAES-------KLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14887 1 PNLLENLYQRYNKAyinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 154 NQSIIVSGESGAGKTVSARYAMRYFATVS---KSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQN 230
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 231 QIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSefKHLKLGSAEEFNYTrmggntviegvndrAEMVETQKTF 310
Cdd:cd14887 161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAA--ATQKSSAGEGDPES--------------TDLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 311 TLLGFKEDFQMDVFKILAAILHLGNVQIT----------------AVGNE-----RSSVSE-------------DDSHLK 356
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTtdqepetskkrkltsvSVGCEetaadRSHSSEvkclssglkvteaSRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 357 VFCELLGLESGRVAQWLCNRKIVTSS--ETVvKPMTRPQAVNARDALAKKIYAHLFDFIVERINQALQFSGK-------- 426
Cdd:cd14887 305 TVARLLGLPPGVEGEEMLRLALVSRSvrETR-SFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsde 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 427 ------QHTFIGVLDIYGFETF---DVNSFEQFCINYANEKLqqqfnmHVFKLEQ----EE--YMKEDIPWTLIDFYDNQ 491
Cdd:cd14887 384 dtpsttGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERL------HCFLLEQlilnEHmlYTQEGVFQNQDCSAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 492 P-------------VIDLI-EAKMGILELLDEECLLPH----------GTDENW------------LQKLYNNFVNRNPL 535
Cdd:cd14887 458 SfplastltsspssTSPFSpTPSFRSSSAFATSPSLPSslsslssslsSSPPVWegrdnsdlfyekLNKNIINSAKYKNI 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 536 FEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRA---------------------------SKFRSSLY 588
Cdd:cd14887 538 TPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLAcstytrlvgskknsgvraissrrstlsAQFASQLQ 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 589 LLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDK 668
Cdd:cd14887 618 QVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREALTP 697
|
730 740
....*....|....*....|....*...
gi 2462545112 669 KEVCKVVLHRLIQDSNQYQFGKTKIFFR 696
Cdd:cd14887 698 KMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
82-695 |
7.33e-95 |
|
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: 321.29 E-value: 7.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAESKLiYTYSGIILVAMNPYKQLPiygdAIIHAYSGQNMGDMdPHIFAVAEEAYKQMARNNRNQSIIVSG 161
Cdd:cd14881 2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYRDVG----NPLTLTSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 162 ESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEqnqiiGANMST-- 239
Cdd:cd14881 76 TSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYRTki 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 240 --YLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKT-FTLLGFK 316
Cdd:cd14881 151 hcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAcLGILGIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 317 edFqMDVFKILAAILHLGNVQITAvGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVN 396
Cdd:cd14881 231 --F-LDVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 397 ARDALAKKIYAHLFDFIVERINQALQFSGKQHT-----FIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLE 471
Cdd:cd14881 307 TRDALAKALYCRTVATIVRRANSLKRLGSTLGThatdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 472 QEEYMKEDIPWTL-IDFYDNQPVIDLIEA-KMGILELLDEECLlPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQ 549
Cdd:cd14881 387 IESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDRMFGIR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 550 HFADKVEYKCEGFLEKNRDTVYDMLVEILR-----------ASKFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDS 618
Cdd:cd14881 466 HFAGRVVYDASDFLDTNRDVVPDDLVAVFYkqncnfgfathTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDR 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 619 KRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEV--CKVVL-----HRLIQDSN---QYQF 688
Cdd:cd14881 546 GTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALedCALILqfleaQPPSKLSSvstSWAL 625
|
....*..
gi 2462545112 689 GKTKIFF 695
Cdd:cd14881 626 GKRHIFL 632
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
82-696 |
1.21e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 318.30 E-value: 1.21e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAY---SGQNMGDMDPHIFAVAEEAYKQMARNNRNQSII 158
Cdd:cd14878 2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 159 VSGESGAGKTVSARYAMRYFATVSKSgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISF-DEQNQIIGANM 237
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 238 STYLLEKSRVVFQSENERNYHIFYQLC--ASAQQSEFKHLKLGSAEEF-NYTRMGGNTVIEGVNDRAEMVETQKTFTLLG 314
Cdd:cd14878 160 YTYMLEKSRLVSQPPGQSNFLIFYLLMdgLSAEEKYGLHLNNLCAHRYlNQTMREDVSTAERSLNREKLAVLKQALNVVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 315 FKEDFQMDVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQA 394
Cdd:cd14878 240 FSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 395 VNARDALAKKIYAHLFDFIVERINQALQ----FSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14878 320 EFYRDLLAKSLYSRLFSFLVNTVNCCLQsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 471 EQEEYMKEDIPWTLIDFYDNQP-VIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYN-------NFV-------NRNP 534
Cdd:cd14878 400 EQTECVQEGVTMETAYSPGNQTgVLDFFFQKpSGFLSLLDEESQMIWSVEPNLPKKLQSllessntNAVyspmkdgNGNV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 535 lfeKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILR------------------ASKFRSSLYLLMETLNA 596
Cdd:cd14878 480 ---ALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKtsenvvinhlfqsklvtiASQLRKSLADIIGKLQK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 597 TTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYG-----ILMTKQELSfsdKKEV 671
Cdd:cd14878 557 CTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKpladtLLGEKKKQS---AEER 633
|
650 660
....*....|....*....|....*
gi 2462545112 672 CKVVLHRLIQDSnqYQFGKTKIFFR 696
Cdd:cd14878 634 CRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
83-696 |
9.02e-92 |
|
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: 312.33 E-value: 9.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLpiygDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14937 3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 163 SGAGKTVSARYAMRYFatVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd14937 78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTrMGGNTVIEGVNDRAEMVETQKTFTLLGFkEDFQMD 322
Cdd:cd14937 156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYI-VNKNVVIPEIDDAKDFGNLMISFDKMNM-HDMKDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 323 VFKILAAILHLGNVQITAV-GNERSSVSE-DDSHLKVFCE---LLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNA 397
Cdd:cd14937 234 LFLTLSGLLLLGNVEYQEIeKGGKTNCSElDKNNLELVNEisnLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 398 RDALAKKIYAHLFDFIVERINQALQFSGKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 477
Cdd:cd14937 314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 478 EDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNTSFVIQHFADKVEY 557
Cdd:cd14937 394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINKNFVIKHTVSDVTY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 558 KCEGFLEKNRDTVYDMLVEILRAS--------------------------KFRSSLYLLMETLNATTPHYVRCIKPNDEK 611
Cdd:cd14937 474 TITNFISKNKDILPSNIVRLLKVSnnklvrslyedvevseslgrknlitfKYLKNLNNIISYLKSTNIYFIKCIKPNENK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 612 LPFEFDSKRIVQQLRACGVLETIRISAqSYPSRWTYIEFYSRYGIL--MTKQELSFSDKKEVCKVVLHRLiqDSNQYQFG 689
Cdd:cd14937 554 EKNNFNQKKVFPQLFSLSIIETLNISF-FFQYKYTFDVFLSYFEYLdySTSKDSSLTDKEKVSMILQNTV--DPDLYKVG 630
|
....*..
gi 2462545112 690 KTKIFFR 696
Cdd:cd14937 631 KTMVFLK 637
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
83-696 |
1.36e-85 |
|
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: 296.14 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFAeSKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd01386 3 VLHTLRQRYG-ANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 163 SGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 243 EKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRA-EMVETQKTFTLLGFKEDFQM 321
Cdd:cd01386 162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAaAFSKLQAAMKTLGISEEEQR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 322 DVFKILAAILHLGNVQITAVGNERSSVSEDDSHLKVFCELLGLE-------------SGRVAQWLCNRkivTSSETVVKP 388
Cdd:cd01386 242 AIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTleelssaifkhhlSGGPQQSTTSS---GQESPARSS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 389 MTRPQ--AVNARDALAKKIYAHLFDFIVERINQALqfSGKQHTF--IGVLDIYGFEtfdvN----------SFEQFCINY 454
Cdd:cd01386 319 SGGPKltGVEALEGFAAGLYSELFAAVVSLINRSL--SSSHHSTssITIVDTPGFQ----NpahsgsqrgaTFEDLCHNY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 455 ANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDN-QPVIDLI---------------EAKMGILELLDEECLLPHGTD 518
Cdd:cd01386 393 AQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYPGSSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 519 ENWLQKLYNNF----VNRNPLFEKPRMSNTSFVIQHF--ADKVEYKCEGFLEKNRDTVYDM-LVEILRASKF------RS 585
Cdd:cd01386 473 DTFLERLFSHYgdkeGGKGHSLLRRSEGPLQFVLGHLlgTNPVEYDVSGWLKAAKENPSAQnATQLLQESQKetaavkRK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 586 SLYL--------LMETLNATTPHYVRCIKPN------DEKLPFEFDSKRIVQ------QLRACGVLETIRISAQSYPSRW 645
Cdd:cd01386 553 SPCLqikfqvdaLIDTLRRTGLHFVHCLLPQhnagkdERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHM 632
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545112 646 TYIEFYSRYGILMTKQELSFSDKKEVC--KVVLHRLIQ----DSNQYQFGKTKIFFR 696
Cdd:cd01386 633 PLGEFRRRFQVLAPPLTKKLGLNSEVAdeRKAVEELLEeldlEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
81-687 |
2.87e-83 |
|
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: 289.11 E-value: 2.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFAESKlIYTYSGIILVAMNPYKQLP-IYGDAIIHAYS-------GQNMGDMDPHIFAVAEEAYKQMARNN 152
Cdd:cd14884 1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 153 RNQSIIVSGESGAGKTVSARYAMRYFATVSKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQI 232
Cdd:cd14884 80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 233 I---------GANMSTYLLEKSRVVFQSENERNYHIFYQL---CASAQQSE------FKHLKLGSAEEFNYTRMGGNTVI 294
Cdd:cd14884 160 QknmfngcfrNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARrnlvrnCGVYGLLNPDESHQKRSVKGTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 295 EGVN----DRAEMVETQKTFTLL-------GFKEDFQMDVFKILAAILHLGNvqitavgnerssvseddSHLKVFCELLG 363
Cdd:cd14884 240 LGSDsldpSEEEKAKDEKNFVALlhglhyiKYDERQINEFFDIIAGILHLGN-----------------RAYKAAAECLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 364 LESGRVAQWLCNRKIVTSSETVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL------------QFSGKQHTFI 431
Cdd:cd14884 303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 432 GVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEEC 511
Cdd:cd14884 383 SILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAKIFRRLDDITKLK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 512 LLPHG-TDENWLQKLYNN-------------FVN---RNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDML 574
Cdd:cd14884 463 NQGQKkTDDHFFRYLLNNerqqqlegkvsygFVLnhdADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNSDKIETSI 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 575 VEILRASKFR-----------------SSLYL-----LMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLE 632
Cdd:cd14884 543 ETLISCSSNRflreannggnkgnflsvSKKYIkeldnLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNE 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2462545112 633 TIRISAQSYPSRwtyiefysrygilMTKQELSFSDKKEVCKVVLHRLIQDSNQYQ 687
Cdd:cd14884 623 MIKILNRGLSHK-------------IPKKETAAALKEQIAKELEKCNSNTDIEYQ 664
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
83-696 |
5.95e-77 |
|
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: 269.30 E-value: 5.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 83 VLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGE 162
Cdd:cd14882 3 ILEELRHRY-LMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 163 SGAGKTVSARYAMRYFATVSKsgSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLL 242
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGD--GNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 243 EKSRVVFQSENERNYHIFYQLCASAQQSE-FKHLKLGSAEEFNYTRMGGNTVIEGV----NDRAEMVETQKTFT----LL 313
Cdd:cd14882 160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNrLKEYNLKAGRNYRYLRIPPEVPPSKLkyrrDDPEGNVERYKEFEeilkDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 314 GFKEDFQMDVFKILAAILHLGNVQItaVGNERSSVSEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSETVVKPMTRPQ 393
Cdd:cd14882 240 DFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 394 AVNARDALAKKIYAHLFDFIVERINQALQFS----GKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFK 469
Cdd:cd14882 318 ARDARDVLASTLYSRLVDWIINRINMKMSFPravfGDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 470 LEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKmgilelldeecllPHG----TDENWLQKLYNNFV------NRNPlFEKP 539
Cdd:cd14882 397 SEMLEMEEEDIPTINLRFYDNKTAVDQLMTK-------------PDGlfyiIDDASRSCQDQNYImdrikeKHSQ-FVKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 540 rMSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASK----------------------FRSSLYLLMETL--- 594
Cdd:cd14882 463 -HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLdesvklmftnsqvrnmrtlaatFRATSLELLKMLsig 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 595 -NATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCK 673
Cdd:cd14882 542 aNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMTKDNCR 621
|
650 660
....*....|....*....|...
gi 2462545112 674 VVLHRLIQDSnqYQFGKTKIFFR 696
Cdd:cd14882 622 LLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
93-696 |
3.83e-76 |
|
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: 267.73 E-value: 3.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 93 ESKLIYTYSGIILVAMNPYKQLP-IYGDAIIHAYSgQNMGdMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSA 171
Cdd:cd14905 12 KKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 172 RYAMRYFATVSKSGSNaHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFDEQNQIIGANMSTYLLEKSRVVFQS 251
Cdd:cd14905 90 KIIIQYLLTTDLSRSK-YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 252 ENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGVNDRAEMVETQKTFTLLGFKEDFQMDVFKILAAIL 331
Cdd:cd14905 169 KGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 332 HLGNVQITAvGNERSSVsEDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSEtvvkpmtrpqAVNARDALAKKIYAHLFD 411
Cdd:cd14905 249 ILGNVTFFQ-KNGKTEV-KDRTLIESLSHNITFDSTKLENILISDRSMPVNE----------AVENRDSLARSLYSALFH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 412 FIVERINQALQFSGKQHTfIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPW-TLIDFYDN 490
Cdd:cd14905 317 WIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFKDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 491 QPVIDLIEAKMGILELLDEECllpHGTDENWLQKLyNNFVNRNPLF-EKPrmsnTSFVIQHFADKVEYKCEGFLEKNRD- 568
Cdd:cd14905 396 EESVEMMEKIINLLDQESKNI---NSSDQIFLEKL-QNFLSRHHLFgKKP----NKFGIEHYFGQFYYDVRGFIIKNRDe 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 569 ----------------------------TVYDM----------------LVEILRA------------------------ 580
Cdd:cd14905 468 ilqrtnvlhknsitkylfsrdgvfninaTVAELnqmfdakntakksplsIVKVLLScgsnnpnnvnnpnnnsgggggggn 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 581 ----SKFRSSLYLLMETLNATTP------HYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEF 650
Cdd:cd14905 548 sgggSGSGGSTYTTYSSTNKAINnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIF 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2462545112 651 YSRYGILMTKQElSFSDKKEvcKVVLHRLIQDS---NQYQFGKTKIFFR 696
Cdd:cd14905 628 FDRFSFFFQNQR-NFQNLFE--KLKENDINIDSilpPPIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
82-696 |
5.11e-75 |
|
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: 263.27 E-value: 5.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 82 AVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYsgqnmgdmdpHIFAVAEEAYKQMARNNRN-QSIIVS 160
Cdd:cd14874 2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 161 GESGAGKTVSARYAMRYFATVSKSG-SNAHVEdkvlASNPITEAVGNAKTTRNDNSSRFGKYTEISFdEQNQIIGANMS- 238
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKvTTKHSS----AIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKy 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 239 TYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNT--VIEGVNDRAEMVETQKTftlLGFK 316
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTenIQSDVNHFKHLEDALHV---LGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 317 EDFQMDVFKILAAILHLGNVQITAVGNerSSVSED------DSHLKVFCELLGLEsgrVAQWLcnrKIVTSSETVVKPMT 390
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRN--PNVEQDvveignMSEVKWVAFLLEVD---FDQLV---NFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 391 RPQAVNARDALAKKIYAHLFDFIVERINQALQFSgKQHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKL 470
Cdd:cd14874 295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCP-LHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 471 EQEEYMKEDIPwtlIDF-----YDNQPVIDLIEAK-MGILELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPRMSNT 544
Cdd:cd14874 374 QLVDYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 545 SFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRASKfRSSLYLLMET--------------------------LNATT 598
Cdd:cd14874 451 EFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSK-NPIIGLLFESyssntsdmivsqaqfilrgaqeiadkINGSH 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 599 PHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRYGILMTKQELSFSDKKEVCKVVLH- 677
Cdd:cd14874 530 AHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQg 609
|
650
....*....|....*....
gi 2462545112 678 RLIQDSNQYQFGKTKIFFR 696
Cdd:cd14874 610 QGVKYENDFKIGTEYVFLR 628
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1324-1650 |
1.17e-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: 236.14 E-value: 1.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1324 EDEAKLIQNLILDLKPRGVVVnmiPGLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1403
Cdd:cd14945 1 SEEDSLLRGIVTDFEPSSGDH---KLTPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1404 CHFLNCLKQYSGEEEFMKHNSPQQNKNCLNNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPiivpgmleyeslqgisgl 1483
Cdd:cd14945 78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1484 kptgfrkrsssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRC 1563
Cdd:cd14945 140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1564 NISYLEEWLKDKNLqNSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPIDDFEKRVTPSFV 1643
Cdd:cd14945 202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280
|
....*..
gi 2462545112 1644 RKVQALL 1650
Cdd:cd14945 281 RTLAAEV 287
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
84-654 |
5.14e-58 |
|
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: 215.61 E-value: 5.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 84 LHNLRIRFAESKlIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN----------MGDMDPHIFAVAEEAYKQMARNNR 153
Cdd:cd14893 4 LYTLRARYRMEQ-VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 154 NQSIIVSGESGAGKTVSARYAMRYFATV-----------SKSGSNAHVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYT 222
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIgdeteprpdseGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 223 EISFDEQNQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQ--SEFKHLKLG-SAEEFNYTRMGGNTVIEGVND 299
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMNkCVNEFVMLKQADPLATNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 300 RAEMVETQKTFTLLGFKEDFQMDVFKILAAILHLGNVQI---------------TAVGNERSSVSEDDSHLKVFCELLGL 364
Cdd:cd14893 243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDPAQILLAAKLLEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 365 ESGRVAQWLCNRKIVT--SSETV--VKPMTRPQAVNARDALAKKIYAHLFDFIVERINQAL-----QFSGK----QHTFI 431
Cdd:cd14893 323 EPVVLDNYFRTRQFFSkdGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSniviNSQGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 432 GVLDIYGFETFD--VNSFEQFCINYANEK-----LQQQFNMHVFKLEQEEYMKED--IPWTLIDF-YDNQPVIDLIEAK- 500
Cdd:cd14893 403 HVLDMVGFENLTpsQNSFDQLCFNYWSEKvhhfyVQNTLAINFSFLEDESQQVENrlTVNSNVDItSEQEKCLQLFEDKp 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 501 MGILELLDEECLLPHGTDENWLQKLYN-------------NFVNRNPLFEKPRMSNTSFVIQHFADKVEYKCEGFLEKNR 567
Cdd:cd14893 483 FGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglsrpnmGADTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKNM 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 568 DTVYDMLVEILRASK---------------------------------FRSSLY---------------------LLMET 593
Cdd:cd14893 563 LSISSTCAAIMQSSKnavlhavgaaqmaaassekaakqteergstsskFRKSASsaresknitdsaatdvynqadALLHA 642
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 594 LNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSRY 654
Cdd:cd14893 643 LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
104-227 |
3.30e-44 |
|
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: 158.28 E-value: 3.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 104 ILVAMNPYKQLPIYGDA-IIHAYSGQNMGDMDPHIFAVAEEAYKQMARNNRNQSIIVSGESGAGKTVSARYAMRYFATVS 182
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545112 183 KSGSNA--------------HVEDKVLASNPITEAVGNAKTTRNDNSSRFGKYTEISFD 227
Cdd:cd01363 81 FNGINKgetegwvylteitvTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
81-694 |
5.52e-39 |
|
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: 156.92 E-value: 5.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 81 PAVLHNLRIRFaESKLIYTYSGIILVAMNPYKQLPIYGDAIIHAYSGQN-MGDMDPHIFAVAEEAYKQMARNNRNQSIIV 159
Cdd:cd14938 1 PSVLYHLKERF-KNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 160 SGESGAGKTVSARYAMRYFATVSK------SGSNAHVEDKVLAS----------------NPITEAVGNAKTTRNDNSSR 217
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAYQVKgsrrlpTNLNDQEEDNIHNEentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 218 FGKYTEISFDEQnQIIGANMSTYLLEKSRVVFQSENERNYHIFYQLCASAQQSEFKHLKLGSAEEFNYTRMGGNTVIEGv 297
Cdd:cd14938 160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFS- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 298 NDRAEMVETQKTFTLLgFKEDFQMD-VFKILAAILHLGNVQITAV---------------------------GNERSSVS 349
Cdd:cd14938 238 DYSGKILELLKSLNYI-FDDDKEIDfIFSVLSALLLLGNTEIVKAfrkksllmgknqcgqninyetilseleNSEDIGLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 350 EDDSHLKVFCELLGLESGRVAQWLCNRKIVTSSeTVVKPMTRPQAVNARDALAKKIYAHLFDFIVERINQ---ALQFSGK 426
Cdd:cd14938 317 ENVKNLLLACKLLSFDIETFVKYFTTNYIFNDS-ILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNINI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 427 QHTFIGVLDIYGFETFDVNSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEDIPWTL-IDFYDNQPVID-LIEAKMGIL 504
Cdd:cd14938 396 NTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 505 ELLDEECLLPHGTDENWLQKLYNNFVNRNPLFEKPR---MSNTSFVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS 581
Cdd:cd14938 476 FSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 582 K-------------------------------------------------FRSSLYLLMETLNATTPHYVRCIKPNDEK- 611
Cdd:cd14938 556 EneymrqfcmfynydnsgniveekrrysiqsalklfkrrydtknqmavslLRNNLTELEKLQETTFCHFIVCMKPNESKr 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 612 LPFEFDSKRIVQQLRACGVLETIRISAQSYPSRWTYIEFYSrygILMTKQElsfsDKKEVCKVVLHRLIQDSNQYQFGKT 691
Cdd:cd14938 636 ELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLS---IFDIKNE----DLKEKVEALIKSYQISNYEWMIGNN 708
|
...
gi 2462545112 692 KIF 694
Cdd:cd14938 709 MIF 711
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1529-1630 |
4.99e-34 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 126.55 E-value: 4.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1529 QAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWLKDKNLQnSLAKETLEPLSQAAWLLQVKKTTDSDAKE 1608
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGLE-SEARDHLAPLIQAAQLLQLRKSTLEDLDS 79
|
90 100
....*....|....*....|..
gi 2462545112 1609 IYERCTSLSAVQIIKILNSYTP 1630
Cdd:pfam01843 80 ILQVCPALNPLQLHRLLTLYQP 101
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
187-658 |
3.04e-28 |
|
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: 123.70 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 187 NAHVEDK---VLASNPITEAVGNAKTTRNDNSSRFGKYT--EISFDE---QNQIIGANMSTYLLEKSRVVFQ------SE 252
Cdd:cd14894 239 NPHAAKKlsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTtlQVAFGLhpwEFQICGCHISPFLLEKSRVTSErgresgDQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 253 NERNYHIFYQLCASAQQSEF-----KHLKLGSAEEFNYTRMG-GNTVIEGV--------NDRAEMVETQKTFTLLGFKED 318
Cdd:cd14894 319 NELNFHILYAMVAGVNAFPFmrllaKELHLDGIDCSALTYLGrSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPD 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 319 FQMDVFKILAAILHLGNVQIT--AVGNE--RSSVSEDDSHLKVfCELLGLESGRVAQWLCNRKIVT---SSETVVKPMTR 391
Cdd:cd14894 399 EQKTIFKVLSAVLWLGNIELDyrEVSGKlvMSSTGALNAPQKV-VELLELGSVEKLERMLMTKSVSlqsTSETFEVTLEK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 392 PQAVNARDALAKKIYAHLFDFIVERINQALQFS-----GKQH------------TFIGVLDIYGFETFDVNSFEQFCINY 454
Cdd:cd14894 478 GQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSalstdGNKHqmdsnasapeavSLLKIVDVFGFEDLTHNSLDQLCINY 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 455 ANEKLQQqfnmhvfKLEQEEYMKEDIPWTLIDFYDNQPVIDLIEAKMGILELLDEECLLPHGTDENWLQ-----KLY-NN 528
Cdd:cd14894 558 LSEKLYA-------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQeekrnKLFvRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 529 FVNRNP--LFEKPR-MSNTS-----------FVIQHFADKVEYKCEGFLEKNRDTVYDMLVEILRAS------------- 581
Cdd:cd14894 631 IYDRNSsrLPEPPRvLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSnsshfcrmlness 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 582 ----------------------------KFRSSLYLLMETLNATTPHYVRCIKPNDEKLPFEFDSKRIVQQLRACGV--- 630
Cdd:cd14894 711 qlgwspntnrsmlgsaesrlsgtksfvgQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLirq 790
|
570 580
....*....|....*....|....*....
gi 2462545112 631 LETIRISAQSYPS-RWTYIEFYSRYGILM 658
Cdd:cd14894 791 MEICRNSSSSYSAiDISKSTLLTRYGSLL 819
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1324-1684 |
3.84e-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: 105.33 E-value: 3.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1324 EDEAKLIQNLILDLKPRGVVVNMIPgLPAHILFMCVRYADSLNDANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNT 1403
Cdd:cd15473 7 EDELPRILDLLITNMTPQRSPSQRP-VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1404 C---HFLNCLKQYsgeeefmkhnspqqnknclnNFDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLqgi 1480
Cdd:cd15473 86 TlllHYLKKDAGL--------------------VEATPEFQQELAELINEIFVLIIRDAERRIDKLLDASPRNITSL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1481 sglkptgfrkrsssiddtdgytMTSVLQQLSYFYttmcqngLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQ 1560
Cdd:cd15473 143 ----------------------LSSTLYVLELYD-------VHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1561 IRCNISYLEEWLKDKNLQ-------NSLAKETLEPLSQAAWLLQVKKT-TDSDA-KEIYERCTSLSAVQIIKILNSYTPi 1631
Cdd:cd15473 194 IRMNLSALEDWARSNNLQpekgespPRIARSHLAPVIQLLQWLQCLSSlDDFESlIATIQQLDALNPLQLLRAVKDYRY- 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 1632 DDFEKRVTPSFVRKVQALLNSRedssqlmLDTKYLFQVTFPFTPsphalEMIQ 1684
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 ... |
1351-1661 |
2.64e-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: 103.81 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1351 PAHILFMCvryadsLNDanMLK--------SLMNSTINGIKQVVKEhLEDFEMLS---FWLSNTcHFLNCLKQYSgEEEF 1419
Cdd:cd15480 48 PAHLIILI------LSE--MWRlgltkeseRFLANVMQTIQQHVMS-LKGEDAIVpgaFWLSNV-HELLSFVCLA-ESDI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1420 MKHNSPqqnKNCLNNFDLSEYRQILSDV-------AIRIYHQFIIIMEKNIQPiivpgmleyeslqgisglkptgfrkrs 1492
Cdd:cd15480 117 LQGIGP---GKDMREEEWEEYERLVTVVkhdleslEYNIYHTWMKELKKRLEK--------------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1493 ssiddtdgyTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWL 1572
Cdd:cd15480 167 ---------TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1573 K-----DKNLQnslaketLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTpIDDFEKRVTPSFVRKVQ 1647
Cdd:cd15480 238 KshdipEGTLQ-------LEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVA 309
|
330
....*....|....
gi 2462545112 1648 ALLNSREDSSQLML 1661
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 ... |
1351-1649 |
3.88e-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: 100.19 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1351 PAHILFMC---VRYADSLNDANMLKSLmNSTINGIKQVVKEHLEDFEMLS--FWLSNTcH----FLNCLKQ---YSGEEE 1418
Cdd:cd15474 34 LGHVNFLIysqMWKSLLELLTQSERFL-SHVLSYIASIVDSLPKKETIPDgaFWLANL-HelrsFVVYLLSlieHSSSDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1419 FMKHNSPQQNKNclnnfdLSEYRQILSdvaiRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISGlkptgFRKRSSSIDDT 1498
Cdd:cd15474 112 FSKESEEYWNTL------FDKTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDLSE-----LIDLNKEFFNK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1499 DGYTMTSVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKDMCSCRKGMQIRCNISYLEEWLKDKNLq 1578
Cdd:cd15474 177 PKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQISYNVSRLKEWCHQHGL- 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 1579 nSLAKETLEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPiDDFEKRVTPSFVRKVQAL 1649
Cdd:cd15474 256 -SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQP-ANYEAPVPKEFLNALEKL 324
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1333 |
7.19e-19 |
|
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: 93.58 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAV---EEKLAKLQ 917
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlELQIASLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 918 KHNSELETQKEQIQ----------------------LKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSfELKTQ 975
Cdd:TIGR02168 400 NEIERLEARLERLEdrrerlqqeieellkkleeaelKELQAELEELEEELEELQEELERLEEALEELREELEEA-EQALD 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 976 DYEKQIQSLKEEIKALKDekMQLQHLVEGEHVT-----SDGLKAEVARLSKQVKTISEFEKEIEL-------------LQ 1037
Cdd:TIGR02168 479 AAERELAQLQARLDSLER--LQENLEGFSEGVKallknQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavvvenLN 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1038 AQKIDVE--------------------KHVQSQKREMREKMSEITKQL--LESYDIE---DVRSRLS----VEDLEHLNE 1088
Cdd:TIGR02168 557 AAKKAIAflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAkdLVKFDPKlrkALSYLLGgvlvVDDLDNALE 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1089 --------------DGELWF-----AYEGLKKATRVLEshfqsqkdcYEKEIEalnfkvvHLSQEINHLQKLFREENDIN 1149
Cdd:TIGR02168 637 lakklrpgyrivtlDGDLVRpggviTGGSAKTNSSILE---------RRREIE-------ELEEKIEELEEKIAELEKAL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1150 ESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLnEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKE 1229
Cdd:TIGR02168 701 AELRKELEELEEE---LEQLRKELEELSRQISALRKDL-ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1230 KEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAN-DVHS 1308
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSeDIES 856
|
570 580
....*....|....*....|....*
gi 2462545112 1309 SSGPKEYLGMLQYKREDEAKLIQNL 1333
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNE 881
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
768-1338 |
9.17e-18 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 90.18 E-value: 9.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 768 IIQKHCRGYLVRSLYQLIRMATITMQAYSRGFLARRRYRKMLEE-HKAVILqkyARAWLARRRFQSIRRFVLNIQLTYRV 846
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVL---ANSELTEARTERDQFSQESGNLDDQL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 847 QRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKaathrRNYEekgkryrdaVEEKLAKLQKHNSELETQ 926
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD-----RNME---------VQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 927 KEQIQLKLQEKTEELkEKMDNLTKQLFDD-------VQKEERQRMLLEKS------FELKTQDYEKQIQSLKEEIKALK- 992
Cdd:pfam15921 446 MERQMAAIQGKNESL-EKVSSLTAQLESTkemlrkvVEELTAKKMTLESSertvsdLTASLQEKERAIEATNAEITKLRs 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 993 --DEKMQ-LQHL-VEGEHVTSDGLKAEVARLSkqvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEitKQLLES 1068
Cdd:pfam15921 525 rvDLKLQeLQHLkNEGDHLRNVQTECEALKLQ-----MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE--KAQLEK 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1069 yDIEDvrSRLSVEDLEHLNEdgelwfayeglKKATRVLESHFQSQkdcyekEIEALNFKVVHLSQEINHLQKLFREEND- 1147
Cdd:pfam15921 598 -EIND--RRLELQEFKILKD-----------KKDAKIRELEARVS------DLELEKVKLVNAGSERLRAVKDIKQERDq 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1148 -INE--SIRHEVTRLTSE-NMMIPDFKQQISELEKQKQDLEIRLneqaEKMKGKLEELSNQLHRSQEEEGTQRK-ALEAQ 1222
Cdd:pfam15921 658 lLNEvkTSRNELNSLSEDyEVLKRNFRNKSEEMETTTNKLKMQL----KSAQSELEQTRNTLKSMEGSDGHAMKvAMGMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1223 NEIHTK--EKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1300
Cdd:pfam15921 734 KQITAKrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
570 580 590
....*....|....*....|....*....|....*...
gi 2462545112 1301 GKAndvhsSSGPKEYLGMLQYKREDEAKLIQNLILDLK 1338
Cdd:pfam15921 814 DKA-----SLQFAECQDIIQRQEQESVRLKLQHTLDVK 846
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1299 |
2.09e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.58 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLE---AELEKAATHRRNYEEKGKRYRDaVEEKLAKLQKHNS 921
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvKELKELKEKAEEYIKLSEFYEE-YLDELREIEKRLS 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 922 ELETQKEQIQLKLQE------KTEELKEKMDNLTKQ---LFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALK 992
Cdd:PRK03918 318 RLEEEINGIEERIKEleekeeRLEELKKKLKELEKRleeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 993 DEKMQLQHLVEGEHVTSDGLKAEVARLSKQV-----------------------KTISEFEKEIELLQAQKIDVEKHVQS 1049
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERK 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1050 QKREMREKMSEITKQ-----LLESYD-IEDVRSRLSVEDLEHLNEDGELwfaYEGLKKATRVLESHFQSQKD------CY 1117
Cdd:PRK03918 478 LRKELRELEKVLKKEselikLKELAEqLKELEEKLKKYNLEELEKKAEE---YEKLKEKLIKLKGEIKSLKKelekleEL 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1118 EKEIEALNFKVVHLSQEINHLQKLFREENdiNESIRHEVTRLTSenmMIPDFKQQIsELEKQKQDLEIRLNEQaEKMKGK 1197
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELG--FESVEELEERLKE---LEPFYNEYL-ELKDAEKELEREEKEL-KKLEEE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1198 LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEK-EKLIDKIQEMQEASDHLKKQFETESEVkcnfRQEASRlTLEnrDLE 1276
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKR----REEIKK-TLE--KLK 700
|
490 500
....*....|....*....|...
gi 2462545112 1277 EELDMKDRVIKKLQDQVKTLSKT 1299
Cdd:PRK03918 701 EELEEREKAKKELEKLEKALERV 723
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
841-1304 |
3.99e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 87.38 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQKKLEdqNKENhglveKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 920
Cdd:TIGR04523 37 QLEKKLKTIKNELK--NKEK-----ELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 SELETQKEQIqLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFElKTQDYEKQIQSLKEEIKALKDEKMQLQH 1000
Cdd:TIGR04523 110 SEIKNDKEQK-NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN-KYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 LVegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 1080
Cdd:TIGR04523 188 NI-------DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1081 EDLEHLNEDGELWFAYEGLKKATRVLESHFQSqkdcYEKEIEALNfkvvhlSQEINHLQKLFREE-NDINESIRHEVTRL 1159
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSEISDLN------NQKEQDWNKELKSElKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1160 TSENMMIPDFKQQISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLHRSQEEE---GTQRKALEAQNEIHTKEKEKL 1233
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEIEKLKKENQSYKQEIknlESQINDLESKIQNQEKLNQQK 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 1234 IDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAN 1304
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1304 |
2.52e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.12 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEKGKRyrdaVEEKLAKLQKHNSELE 924
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRE----LEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 925 TQKEQIQlKLQEKTEE---LKEKMDNLTKQLFDdVQKE----ERQRMLLEKSFElKTQDYEKQIQSLKEEIKALKDEKMQ 997
Cdd:PRK03918 280 EKVKELK-ELKEKAEEyikLSEFYEEYLDELRE-IEKRlsrlEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 998 LQHLVEgEHVTSDGLKAEVARLSKQVK--TISEFEKEIELLQAQKIDVEKHVqsqkREMREKMSEITkqllesydiedvr 1075
Cdd:PRK03918 357 LEERHE-LYEEAKAKKEELERLKKRLTglTPEKLEKELEELEKAKEEIEEEI----SKITARIGELK------------- 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1076 srlsvedlehlNEDGELWFAYEGLKKATRVL--------ESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEnd 1147
Cdd:PRK03918 419 -----------KEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL-- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1148 inESIRHEVTRLTSENMMIPDFKQQISELEK-QKQDLEiRLNEQAEKMKGKLEELSNQLhRSQEEEGTQRKALEaqneih 1226
Cdd:PRK03918 486 --EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELE-KKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELK------ 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1227 tKEKEKLIDKIQEMQEASDHLKKQ-----FETESEVKCNFR--QEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKT 1299
Cdd:PRK03918 556 -KKLAELEKKLDELEEELAELLKEleelgFESVEELEERLKelEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
....*
gi 2462545112 1300 IGKAN 1304
Cdd:PRK03918 635 LAETE 639
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1305 |
2.83e-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: 85.11 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 920
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 SELETQKEQIQLkLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEkSFELKTQDYEKQIQSLKEEIKALKDEKMQLQH 1000
Cdd:TIGR02168 337 EELAELEEKLEE-LKEELESLEAELEELEAELEELESRLEELEEQLE-TLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 LVEGEH--VTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKqllESYDIEDVRSRL 1078
Cdd:TIGR02168 415 RRERLQqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA---AERELAQLQARL 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1079 -SVEDLEHLNED-----GELWFAYEGLKKATRVLESHFQSQKDcYEKEIEA-----LNFKVVHLSQE----INHLQK--- 1140
Cdd:TIGR02168 492 dSLERLQENLEGfsegvKALLKNQSGLSGILGVLSELISVDEG-YEAAIEAalggrLQAVVVENLNAakkaIAFLKQnel 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1141 ---LFREENDINESIRHEVTRLTSENmmIPDFKQQISELEKQKQDLEIRLN------------EQAEKMKGKLEEL---- 1201
Cdd:TIGR02168 571 grvTFLPLDSIKGTEIQGNDREILKN--IEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGyriv 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1202 ---------------------SNQLHRSQE--EEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVK 1258
Cdd:TIGR02168 649 tldgdlvrpggvitggsaktnSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2462545112 1259 CNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1305
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1298 |
1.30e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.27 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKenhglVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 924
Cdd:PTZ00121 1303 KADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 925 TQKEQIQLKLQE--KTEELKEKMDNLTKQLfDDVQKEERQRmllEKSFELKTQDYEK----QIQSLKEEIKALKDEKMQL 998
Cdd:PTZ00121 1378 KKADAAKKKAEEkkKADEAKKKAEEDKKKA-DELKKAAAAK---KKADEAKKKAEEKkkadEAKKKAEEAKKADEAKKKA 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 999 QHLVEGEHVTSdglKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV-QSQKREMREKMSEITKQLLESYDIEDVRSR 1077
Cdd:PTZ00121 1454 EEAKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1078 LSVEDLEHLNEDGELWFAYEgLKKATRVLESHFQSQKDCYEKEIEALNF---KVVHLSQ----EINHLQKLFREENDIN- 1149
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEAKKAEEDKNMalrKAEEAKKaeeaRIEEVMKLYEEEKKMKa 1609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1150 -ESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEgtQRKALEAQNEIHTK 1228
Cdd:PTZ00121 1610 eEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDE 1687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1229 EK--EKLIDKIQEMQEASDHLKK---------QFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLS 1297
Cdd:PTZ00121 1688 KKaaEALKKEAEEAKKAEELKKKeaeekkkaeELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
.
gi 2462545112 1298 K 1298
Cdd:PTZ00121 1768 K 1768
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
809-1240 |
1.34e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 809 LEEHKAVILQKYARAWLARRRFQSIRrfvlniQLTYRVQRLQKKLEDQNKENhgLVEKLTSLAalragdvEKIQKLEAEL 888
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAK------AKKEELERLKKRLTGLTPEK--LEKELEELE-------KAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 889 EKAATHRRNYEEKGKRYRDAVEE-KLAKLQ--KHNSEL-ETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRM 964
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEElKKAKGKcpVCGRELtEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 965 LLEKSFEL-KTQDYEKQIQSLKEEIKALKDEKM-QLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLqaqkid 1042
Cdd:PRK03918 488 VLKKESELiKLKELAEQLKELEEKLKKYNLEELeKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL------ 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1043 vekhvQSQKREMREKMSEITKQLLES--YDIEDVRSRLsvEDLEhlnedgELWFAYEGLKKATRVLESHFQSQKDCYE-- 1118
Cdd:PRK03918 562 -----EKKLDELEEELAELLKELEELgfESVEELEERL--KELE------PFYNEYLELKDAEKELEREEKELKKLEEel 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1119 ----KEIEALNFKVVHLSQEINHLQKLFREENdiNESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEirlnEQAEKM 1194
Cdd:PRK03918 629 dkafEELAETEKRLEELRKELEELEKKYSEEE--YEELREEYLELSRE---LAGLRAELEELEKRREEIK----KTLEKL 699
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 1195 KGKLEELSnqlhRSQEEEGTQRKALEAQNEIHTK-------EKEKLIDKIQEM 1240
Cdd:PRK03918 700 KEELEERE----KAKKELEKLEKALERVEELREKvkkykalLKERALSKVGEI 748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
879-1242 |
2.39e-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: 78.96 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 879 EKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfdDVQK 958
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE-KLKERLEELEEDLSSL------EQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 959 EERQRMLleKSFELKTQDYEKQIQSLKEEIKALKDekMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQA 1038
Cdd:TIGR02169 754 ENVKSEL--KELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1039 QKIDVEKHVQSQKREMREKMSEITKQLLESY-DIEDVRSRLSvedlEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCY 1117
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNgKKEELEEELE----ELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1118 EKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTrLTSENMMIPDFKQQISELEKqkqdlEIRlneqaekmkgK 1197
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVEE-----EIR----------A 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2462545112 1198 LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1242
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
850-1280 |
3.93e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 850 QKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR------DAVEEKLAKLQKHNSEL 923
Cdd:PRK02224 191 QLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreelETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 924 ETQKEQIQLKLQEKTEELKEKMDNLTKQL----FDDV--------------QKEERQRMLLEKSfeLKTQDYEKQIQSLK 985
Cdd:PRK02224 271 EREREELAEEVRDLRERLEELEEERDDLLaeagLDDAdaeavearreeledRDEELRDRLEECR--VAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 986 EEIKALKDEKMQLQHlvEGEHVTSDGLKAEVArLSKQVKTISEFEKEIELLQAQKIDVE---KHVQSQKREMREKMSEIT 1062
Cdd:PRK02224 349 EDADDLEERAEELRE--EAAELESELEEAREA-VEDRREEIEELEEEIEELRERFGDAPvdlGNAEDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1063 KQLLE-SYDIEDVRSRlsVEDLEHLNEDG---ELWFAYEGLKKATRVLEShfQSQKDCYEKEIEALNFKVVHLSQEINHL 1138
Cdd:PRK02224 426 EREAElEATLRTARER--VEEAEALLEAGkcpECGQPVEGSPHVETIEED--RERVEELEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1139 QKLFREENDIN--ESIRHEVTRLTSENMMIPDFKQ-QISELEKQKQDLEirlNEQAEKmkgklEELSNQLHRSQEEEGTQ 1215
Cdd:PRK02224 502 EDLVEAEDRIErlEERREDLEELIAERRETIEEKReRAEELRERAAELE---AEAEEK-----REAAAEAEEEAEEAREE 573
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545112 1216 RKALEAQNEIHTKEKEKLiDKIQEMQEASDHLKKQFETESEVKCNF--RQEASRLTLEN-----RDLEEELD 1280
Cdd:PRK02224 574 VAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALaeLNDERRERLAEkrerkRELEAEFD 644
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1292 |
4.93e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKenhglVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKR---YRDAVEEKLAKLQKHNS 921
Cdd:PTZ00121 1379 KADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeaKKKAEEAKKADEAKKKA 1453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 922 ELETQKEQIQLKLQE--KTEELKEKMDNLTKQlfDDVQKEERQRMllEKSFELKTQDYEKQiqslKEEIKALKDEKMQLQ 999
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEakKADEAKKKAEEAKKA--DEAKKKAEEAK--KKADEAKKAAEAKK----KADEAKKAEEAKKAD 1525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1000 HLVEGEhvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDV--EKHVQSQKREMREKMSEITKQLlESYDIEDVRSR 1077
Cdd:PTZ00121 1526 EAKKAE----EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeEAKKAEEDKNMALRKAEEAKKA-EEARIEEVMKL 1600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1078 LSVEDL---EHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDinesirh 1154
Cdd:PTZ00121 1601 YEEEKKmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------- 1673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1155 evtrltsenmmipdfKQQISELEKQKQDLeiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLI 1234
Cdd:PTZ00121 1674 ---------------KKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545112 1235 DKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRD----LEEELDMKDRVIKKLQDQ 1292
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEkeavIEEELDEEDEKRRMEVDK 1798
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
849-1302 |
2.45e-13 |
|
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: 75.44 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 849 LQKKLEDQNKENHGLVEKLTSLAalragdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKE 928
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 929 QIQlKLQEKTEELK-EKMDNLTKQLFDDVQKEERQRMLLEKsfelKTQDYEKQIQSLKEEIKALKDEKMQLqhlvEGEHV 1007
Cdd:TIGR04523 289 QLN-QLKSEISDLNnQKEQDWNKELKSELKNQEKKLEEIQN----QISQNNKIISQLNEQISQLKKELTNS----ESENS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1008 TSDG-LKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVE----- 1081
Cdd:TIGR04523 360 EKQReLEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiiknn 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1082 ----DLEhlNEDGELWFAYEGLKKATRVLESHFQSQKDCY-----------------EKEIEALNFKVVHLSQEINHL-- 1138
Cdd:TIGR04523 440 seikDLT--NQDSVKELIIKNLDNTRESLETQLKVLSRSInkikqnleqkqkelkskEKELKKLNEEKKELEEKVKDLtk 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1139 ---------QKLFREEN-------DINESIRHEVTRLTSENM--MIPDFKQQISELeKQKQDLEIRLNEQAEKMKGKLEE 1200
Cdd:TIGR04523 518 kisslkekiEKLESEKKekeskisDLEDELNKDDFELKKENLekEIDEKNKEIEEL-KQTQKSLKKKQEEKQELIDQKEK 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1201 LSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELd 1280
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI- 675
|
490 500
....*....|....*....|..
gi 2462545112 1281 mkDRVIKKLQDQVKTLSKTIGK 1302
Cdd:TIGR04523 676 --DDIIELMKDWLKELSLHYKK 695
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
636-1333 |
4.46e-13 |
|
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: 74.77 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 636 ISAQSYPSRWTYIEFYSRYGILMT--KQELSFSDKKEVCKVV---------LHRLIQDSNQYQfGKTKIFFRAG------ 698
Cdd:pfam15921 39 IENTSSTGTFTQIPIFPKYEVELDspRKIIAYPGKEHIERVLeeyshqvkdLQRRLNESNELH-EKQKFYLRQSvidlqt 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 699 --QVAYLEKLRLDKLRQSCVMVQKHMRGWLQRKkfLRERRAALIIQQYFRGQ-----QTVRKAITAV--ALKEAWAAIII 769
Cdd:pfam15921 118 klQEMQMERDAMADIRRRESQSQEDLRNQLQNT--VHELEAAKCLKEDMLEDsntqiEQLRKMMLSHegVLQEIRSILVD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 770 QKHCRGylvRSLYQLIRMATITMQAYSRGFlarrryRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLN---IQLTYRV 846
Cdd:pfam15921 196 FEEASG---KKIYEHDSMSTMHFRSLGSAI------SKILRELDTEISYLKGRIFPVEDQLEALKSESQNkieLLLQQHQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 847 QRLQKKLEDQNKENHGLVEKLTSLAAlragdveKIQKLEAELEKAATHRRNYEEKGKRyrdaveeKLAKLQKHNSELETQ 926
Cdd:pfam15921 267 DRIEQLISEHEVEITGLTEKASSARS-------QANSIQSQLEIIQEQARNQNSMYMR-------QLSDLESTVSQLRSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 927 KEQIQLKLQEKTEELKEK------------------------MDNLTKQLFDDVQKEERQrMLLEKS------------- 969
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQlvlanseltearterdqfsqesgnLDDQLQKLLADLHKREKE-LSLEKEqnkrlwdrdtgns 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 970 -----FELKTQDYEKQIQSLKEEIKALKDE-KMQLQHLVEGEHVTSDGLKaEVARLSKQVKTISE-FEKEIELLQAQKI- 1041
Cdd:pfam15921 412 itidhLRRELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEmLRKVVEELTAKKMt 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1042 ---------DVEKHVQSQKREMREKMSEITKqllesydiedVRSR--LSVEDLEHLNEDGElwfayeglkkatrvlesHF 1110
Cdd:pfam15921 491 lessertvsDLTASLQEKERAIEATNAEITK----------LRSRvdLKLQELQHLKNEGD-----------------HL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1111 QS-QKDCYEKEIE-ALNFKVVH-LSQEINHLQKLFREENDINESIRHEVTRLTSE----NMMIPDFK-------QQISEL 1176
Cdd:pfam15921 544 RNvQTECEALKLQmAEKDKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEindrRLELQEFKilkdkkdAKIREL 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1177 EKQKQDLEIR----LNEQAEKMKGkLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFE 1252
Cdd:pfam15921 624 EARVSDLELEkvklVNAGSERLRA-VKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1253 T-ESEVkcnfrqEASRLTLENRD------------LEEELDMKDRVIKKLQDQVKTLSKTIGKANDvhsssgPKEYLgml 1319
Cdd:pfam15921 703 SaQSEL------EQTRNTLKSMEgsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANK------EKHFL--- 767
|
810
....*....|....
gi 2462545112 1320 qykREDEAKLIQNL 1333
Cdd:pfam15921 768 ---KEEKNKLSQEL 778
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
877-1307 |
6.32e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 73.99 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 877 DVEKIQKLEAELEKAAThrrNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTE-------ELKEKMDNLT 949
Cdd:pfam05483 220 DHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN-QLEEKTKlqdenlkELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 950 KQLfDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDE--KMQLQH-LVEGEHVTS-----DGLKAEVARLSK 1021
Cdd:pfam05483 296 KEL-EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEElnKAKAAHsFVVTEFEATtcsleELLRTEQQRLEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1022 ---QVKTIS-EFEKEI-ELLQAQKIDVEKHVQSQkrEMREKMSEITKQLLESYDIEDVRSRLSvedlehlNEDGELWFAY 1096
Cdd:pfam05483 375 nedQLKIITmELQKKSsELEEMTKFKNNKEVELE--ELKKILAEDEKLLDEKKQFEKIAEELK-------GKEQELIFLL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1097 EGLKK----------ATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHL----QKLFREENDINESIRHEVTRLTSE 1162
Cdd:pfam05483 446 QAREKeihdleiqltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLllenKELTQEASDMTLELKKHQEDIINC 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1163 NMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEeegtqrKALEAQNEIHTKEKEKLIdkiqeMQE 1242
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEE------NARSIEYEVLKKEKQMKI-----LEN 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545112 1243 ASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVH 1307
Cdd:pfam05483 595 KCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1239 |
7.81e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 7.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQKKLEDQNKEnhgLVEKLTSLAALRAgDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 920
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKA---LAELRKELEELEE-ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 SELETQKEQIQLKLQEKTEELKEKMDNLTKQlfddvqkeerqrmlleksfELKTQDYEKQIQSLKEEIKALKDEKMQLQh 1000
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEEL-------------------EAQIEQLKEELKALREALDELRAELTLLN- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 lvEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEkHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 1080
Cdd:TIGR02168 817 --EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-AEIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1081 EDLEHLNEDgelwfayeglkkaTRVLESHFQSQKDCYE---KEIEALNFKVVHLSQEINHLQKLFREENDIN--ESIRHE 1155
Cdd:TIGR02168 894 SELEELSEE-------------LRELESKRSELRRELEelrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTleEAEALE 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1156 VTRLTSENmmipDFKQQISELEKQKQDL-EIRLN--EQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEK 1232
Cdd:TIGR02168 961 NKIEDDEE----EARRRLKRLENKIKELgPVNLAaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
....*..
gi 2462545112 1233 LIDKIQE 1239
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 ... |
1351-1657 |
2.96e-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: 69.65 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1351 PAHILFMCVRYADSLND---------ANMLKSLMNSTINGIKQVVKEHLEDFEMLSFWLSNTCHFLNCLKQysgeeefmk 1421
Cdd:cd15471 25 PAYTLYLAARYRLSTHYrpeltpterAHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1422 hnspqqnknclnNFDLSEYR----QILSDVAIRIYHQFIIIMEKNIQPIIVPGMLEYESLQGISGlkptgfrkrsssIDD 1497
Cdd:cd15471 96 ------------DRDLSAFSvqaqDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPA------------IGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1498 tdgytmtsVLQQLSYFYTTMCQNGLDPELVRQAVKQLFFLIGAVTLNSLFLRKD--MCSCRKGMQIRCNISYLEEWLKDK 1575
Cdd:cd15471 152 --------VLHTLSSAMRLLRRCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWAERQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1576 NLQnsLAKET-LEPLSQAAWLLQVKKTTDSDAKEIYERCTSLSAVQIIKILNSYTPiDDFEKRVTPSFVRKVQALLNSRE 1654
Cdd:cd15471 224 GLE--LAADChLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP-PPGEPPIPPDLIERVVRLAESQA 300
|
...
gi 2462545112 1655 DSS 1657
Cdd:cd15471 301 DEL 303
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
846-1296 |
4.48e-12 |
|
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: 71.36 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 846 VQRLQKKLEdQNKENHGLVEKltSLAALRAGDVEkiqkLEAELEKAATHRRNYEEKGKRyrdaVEEKLAKLQKHNSELET 925
Cdd:pfam01576 358 LEELTEQLE-QAKRNKANLEK--AKQALESENAE----LQAELRTLQQAKQDSEHKRKK----LEGQLQELQARLSESER 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 926 QKEQiqlkLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEK---SFELKTQDYEKQIQ-------SLKEEIKALKDEK 995
Cdd:pfam01576 427 QRAE----LAEKLSKLQSELESVSSLL----NEAEGKNIKLSKdvsSLESQLQDTQELLQeetrqklNLSTRLRQLEDER 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 996 MQLQHLVEGEHVTSDGLKAEVARLSKQV----KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITK-------- 1063
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrl 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1064 -QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKAtRVLESHFQSQKDCYEKEIEALNfkvvhLSQEINHLQKLF 1142
Cdd:pfam01576 579 qQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISA-RYAEERDRAEAEAREKETRALS-----LARALEEALEAK 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1143 REENDINESIRHEVTRLTSENmmiPDFKQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSQE-----EEGTQrk 1217
Cdd:pfam01576 653 EELERTNKQLRAEMEDLVSSK---DDVGKNVHELERSKRALE----QQVEEMKTQLEELEDELQATEDaklrlEVNMQ-- 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1218 ALEAQNE--IHTKE------KEKLIDKIQEMQEASDHLKKQFETESEVKcnfrqeaSRLTLENRDLEEELDM----KDRV 1285
Cdd:pfam01576 724 ALKAQFErdLQARDeqgeekRRQLVKQVRELEAELEDERKQRAQAVAAK-------KKLELDLKELEAQIDAankgREEA 796
|
490
....*....|....
gi 2462545112 1286 IK---KLQDQVKTL 1296
Cdd:pfam01576 797 VKqlkKLQAQMKDL 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
869-1242 |
4.61e-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: 71.24 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 869 SLAALRAGDVEKI-----QKLEAELEKAA---THRRNYEEKGKRYRDAvEEKLAKLQKHNSELETQKEQIQL------KL 934
Cdd:TIGR02168 137 SYSIIEQGKISEIieakpEERRAIFEEAAgisKYKERRKETERKLERT-RENLDRLEDILNELERQLKSLERqaekaeRY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 935 QEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKA 1014
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1015 EVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE-SYDIEDVRSRLSVedlehlnedgelw 1093
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElKEELESLEAELEE------------- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1094 fayegLKKATRVLESHFQSQkdcyEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSEnmmIPDFKQQI 1173
Cdd:TIGR02168 363 -----LEAELEELESRLEEL----EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE---IEELLKKL 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 1174 SELEKQKQDLEI-RLNEQAEKMKGKLEELSNQLHRSQEE-EGTQRKALEAQNEIHTKEKEklIDKIQEMQE 1242
Cdd:TIGR02168 431 EEAELKELQAELeELEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQAR--LDSLERLQE 499
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
830-1243 |
5.93e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 830 FQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAV 909
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 910 EEKLAKLQKHNSELETQKEQIQLK-LQEKTEELKEKMDNLTKQLFDDVQKEERQRML---LEKSFELKTQDYEKQIQSLK 985
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAELAeLPERLEELEERLEELRELEEELEELEAELAELqeeLEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 986 EEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEK---------------------------------- 1031
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1032 ---EIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLES 1108
Cdd:COG4717 279 lflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1109 HF-QSQKDCYEKEIEAL-NFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENmmiPDFKQQISELEKQkqdleiR 1186
Cdd:COG4717 359 LEeELQLEELEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELL---GELEELLEALDEE------E 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545112 1187 LNEQAEKMKGKLEELSNQLHRSQEEEGT---QRKALEAQNEIHTK--EKEKLIDKIQEMQEA 1243
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAEleaELEQLEEDGELAELlqELEELKAELRELAEE 491
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
847-1333 |
2.45e-11 |
|
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: 68.84 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 847 QRLQKKLEDQNKENHGLVEKLTSLaalragdvEKIQKLEAELEKAaTHRRNYEEKGKRY---RDAVEEKLAKLQKHNSEL 923
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARI--------EELRAQEAVLEET-QERINRARKAAPLaahIKAVTQIEQQAQRIHTEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 924 ETQKEQIQLKLQEKTEELKEKMD-----NLTKQLF---------DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIK 989
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSieeqrRLLQTLHsqeihirdaHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 990 ALKDEKMQL---QHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLL 1066
Cdd:TIGR00618 397 SLCKELDILqreQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1067 ESYDIEDVRSRLSVEDLEHLNEDGELwfaYEGLKKATRVLESHFQ----SQKDC---------YEKEIEALNFKVVHLSQ 1133
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEE---PCPLCGSCIHPNPARQdidnPGPLTrrmqrgeqtYAQLETSEEDVYHQLTS 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1134 EINHLQKLFREEndinESIRHEVTRLTSenmMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEG 1213
Cdd:TIGR00618 554 ERKQRASLKEQM----QEIQQSFSILTQ---CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1214 TQRKALEAQNEIHTKEKEKL------IDKIQEMQEASDHLKKQFETES-EVKCNFRQEASRLTLENRDLEEELDMKDRVI 1286
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTalhalqLTLTQERVREHALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2462545112 1287 KKLQDQVKTLSKTIGKANDVHSSSGPKeylgmLQYKREDEAKLIQNL 1333
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSD-----LAAREDALNQSLKEL 748
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
917-1305 |
4.44e-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: 68.16 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 917 QKHNSELETQKEQiqLKLQEKTEELKEKMDNLTKQLfDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKM 996
Cdd:TIGR02168 667 KTNSSILERRREI--EELEEKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 997 QLQHLVEGEHVTSDGLKAEV----ARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITkqlLESYDIE 1072
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT---LLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1073 DVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLEShfqsqkdcYEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 1152
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIES--------LAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1153 RHEVTRLTSEnmmipdfkqqISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLhRSQEEEGTQRKALEAqnEIHTKE 1229
Cdd:TIGR02168 893 RSELEELSEE----------LRELESKRSELRrelEELREKLAQLELRLEGLEVRI-DNLQERLSEEYSLTL--EEAEAL 959
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545112 1230 KEKLIDKIQEMQEASDHLKKQFETESEVkcNFRQEAsrltlENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1305
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKELGPV--NLAAIE-----EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
828-1092 |
7.32e-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: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 828 RRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENhglvEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRD 907
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 908 AVEEKLAKLQKHNSELETQKEQIQ------LKLQEKTEELKEKMDNLTKQL---FDDVQKEERQRMLLEKSFELKTQDYE 978
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRReleerlEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 979 KQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKM 1058
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270
....*....|....*....|....*....|....
gi 2462545112 1059 SEITKQLLESYDIEDVRSRLSVEDLEHLNEDGEL 1092
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
727-1305 |
8.66e-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: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 727 QRKKFLRERRAALIIQQYFRG---QQTVRKAITAVALKEAWAAIIIQkhcrgylVRSLYQLIRMATITMQAYSRGFLARR 803
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEaqlEELESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 804 R-YRKMLEEHKAVILQKYARAWLARRRFQSIRRfvlniqltyRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGdvEKIQ 882
Cdd:TIGR02168 375 EeLEEQLETLRSKVAQLELQIASLNNEIERLEA---------RLERLEDRRERLQQEIEELLKKLEEAELKELQ--AELE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 883 KLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQK------EQIQLKLQEKTEELKEKMDN------LTK 950
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNqsglsgILG 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 951 QLFDDVQKEERQRMLLEKSFELKTQDYE-KQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAE-----------VAR 1018
Cdd:TIGR02168 524 VLSELISVDEGYEAAIEAALGGRLQAVVvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNdreilkniegfLGV 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1019 LSKQVKTISEFEKEIELLQAQKIDVE--KHVQSQKREMREKMSEITKqllesyDIEDVRSRLSV------EDLEHLNEDG 1090
Cdd:TIGR02168 604 AKDLVKFDPKLRKALSYLLGGVLVVDdlDNALELAKKLRPGYRIVTL------DGDLVRPGGVItggsakTNSSILERRR 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1091 ELwfayEGLKKATRVLESHFQSQK---DCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSenmMIP 1167
Cdd:TIGR02168 678 EI----EELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE---RIA 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1168 DFKQQISELEKQKQDLEIRLNEQAEKMK---GKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLID---KIQEMQ 1241
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLESLE 830
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 1242 EASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAND 1305
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
802-1300 |
1.57e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 802 RRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLtyRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKI 881
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELEL--ELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 882 QKLEAELEKAATHRRNYEEKgkryRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLtkqlfDDVQKEER 961
Cdd:COG1196 319 EELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 962 QRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKI 1041
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1042 DVEKHVQSQKREMREKMSE------ITKQLLESYD--IEDVRSRLSVEDLEHLNEDGELW----FAYEGL---------- 1099
Cdd:COG1196 470 EEAALLEAALAELLEELAEaaarllLLLEAEADYEgfLEGVKAALLLAGLRGLAGAVAVLigveAAYEAAleaalaaalq 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1100 -------------------KKATRV----LESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEV 1156
Cdd:COG1196 550 nivveddevaaaaieylkaAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1157 TRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEiHTKEKEKLIDK 1236
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE-ALLAEEEEERE 708
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545112 1237 IQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDR----VIKKLQDQVKTLSKTI 1300
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELpeppDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
804-1140 |
2.40e-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: 65.86 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 804 RYRKMLEEhkaviLQKYaRAWLARRRFQSIRRfvlniqltyRVQRLQKKLEDQNKEnhglVEKLTslaalragdvEKIQK 883
Cdd:TIGR02169 212 RYQALLKE-----KREY-EGYELLKEKEALER---------QKEAIERQLASLEEE----LEKLT----------EEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 884 LEAELEKAathRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELkEKMDNLTKQLFddvqkEERQR 963
Cdd:TIGR02169 263 LEKRLEEI---EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL-EDAEERLAKLE-----AEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 964 MLLEK-SFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKID 1042
Cdd:TIGR02169 334 LLAEIeELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1043 VEKHVQSQKREMREKMSEITKQLLEsydiedVRSRLSVEDLEhlnedgelwfayegLKKATRVLEShFQSQKDCYEKEIE 1122
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINE------LEEEKEDKALE--------------IKKQEWKLEQ-LAADLSKYEQELY 472
|
330
....*....|....*...
gi 2462545112 1123 ALNFKVVHLSQEINHLQK 1140
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQR 490
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
921-1300 |
3.18e-10 |
|
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: 65.38 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 SELETQKEQIQLKLQEKTEELKEKMDNLTkqlfddvqKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEkmQLQH 1000
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLE--------ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD--YLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsYDIEDVRSRLSV 1080
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-LLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1081 EDLEHLNEDGELwfaYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQ--------EINHLQKLFREENDINESI 1152
Cdd:pfam02463 314 EKLKESEKEKKK---AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKlqekleqlEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1153 rhevtRLTSENMMIPDFKQQISELEKQ--KQDLEIRLNEQAEKMKGKLEELSnqlhrsqEEEGTQRKALEAQNEIHTKEK 1230
Cdd:pfam02463 391 -----KLKEEELELKSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEE-------SIELKQGKLTEEKEELEKQEL 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1231 EKLIDKIQEMQEASDHLKKQfETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1300
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQ-LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
843-1208 |
3.76e-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: 64.49 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 843 TYRVQRLQKKLEDqnkenhglVEKLTSLAAlraGDVEKIQK-LEAELEKAATHRRNYEEKGKRYR--------------- 906
Cdd:pfam06160 78 KYRFKKAKKALDE--------IEELLDDIE---EDIKQILEeLDELLESEEKNREEVEELKDKYRelrktllanrfsygp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 907 --DAVEEKLAKLQKHNSELETQKEQ--------IQLKLQEKTEELKEKMDNLtKQLFDDVQKE---------ERQRMLLE 967
Cdd:pfam06160 147 aiDELEKQLAEIEEEFSQFEELTESgdyleareVLEKLEEETDALEELMEDI-PPLYEELKTElpdqleelkEGYREMEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 968 KSFELKTQDYEKQIQSLKEEIKALkdekmqLQHLVEGEhvtSDGLKAEVARLSKQVKTISE-FEKEIEllqaQKIDVEKH 1046
Cdd:pfam06160 226 EGYALEHLNVDKEIQQLEEQLEEN------LALLENLE---LDEAEEALEEIEERIDQLYDlLEKEVD----AKKYVEKN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1047 vQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHlnedgelwfayeglkkaTRVLESHFQSQKDCYEKEIEALNF 1126
Cdd:pfam06160 293 -LPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELER-----------------VRGLEKQLEELEKRYDEIVERLEE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1127 KVVHLSQEINHLQKLFREENDINEsiRHEvtrltsenmmipDFKQQISELEKQkqdlEIRLNEQAEKMKGKLEELSNQLH 1206
Cdd:pfam06160 355 KEVAYSELQEELEEILEQLEEIEE--EQE------------EFKESLQSLRKD----ELEAREKLDEFKLELREIKRLVE 416
|
..
gi 2462545112 1207 RS 1208
Cdd:pfam06160 417 KS 418
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
910-1249 |
6.00e-10 |
|
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: 64.58 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 910 EEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvqkeeRQRML-LEKS---FELKTQDYEKQIQSLK 985
Cdd:pfam15818 27 EEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQL--------QMKMCaLEEEkgkYQLATEIKEKEIEGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 986 EEIKALKDEKMQLQhlvegehvtsdglkaevarlskqvKTISEFEKEIELLQAQKIDVEKhvqsQKREMREKMSEITKQL 1065
Cdd:pfam15818 99 ETLKALQVSKYSLQ------------------------KKVSEMEQKLQLHLLAKEDHHK----QLNEIEKYYATITGQF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1066 ---------LESYDIEDVR--SRLSVedlehLNE--DGELWFAYEGLKKATRVL-ESHFQSQkdcYEKEIEALNFKVVHl 1131
Cdd:pfam15818 151 glvkenhgkLEQNVQEAIQlnKRLSA-----LNKkqESEICSLKKELKKVTSDLiKSKVTCQ---YKMGEENINLTIKE- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1132 sQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQ--AEKMKGKLEELSNQLHRSQ 1209
Cdd:pfam15818 222 -QKFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAElkALKENNQTLERDNELQREK 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2462545112 1210 EEEgTQRKALEAQNEiHTK-------EKEKLIDKIQEMQEASDHLKK 1249
Cdd:pfam15818 301 VKE-NEEKFLNLQNE-HEKalgtwkkHVEELNGEINEIKNELSSLKE 345
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
943-1302 |
6.58e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 943 EKMDNLTKQL--FDDVQKEERQRMLLEKSFELKTQDYEKQIQS---LKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVA 1017
Cdd:PRK03918 145 ESREKVVRQIlgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1018 RLSKQVKTISEFEKEIELLQAQKIDVEKHvqsqKREMREKMSEITKQLLES-YDIEDVRSRlsVEDLEHLNEDGELWFAY 1096
Cdd:PRK03918 225 KLEKEVKELEELKEEIEELEKELESLEGS----KRKLEEKIRELEERIEELkKEIEELEEK--VKELKELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1097 EGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEndinESIRHEVTRLTSENMMIPDFKQQISEL 1176
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL----KELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1177 EKQKQDLEirlNEQAEKMKGKLEELSNqlhrsqeeegtqrkaleAQNEIhTKEKEKLIDKIQEMQEASDHLKKQFE--TE 1254
Cdd:PRK03918 375 ERLKKRLT---GLTPEKLEKELEELEK-----------------AKEEI-EEEISKITARIGELKKEIKELKKAIEelKK 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545112 1255 SEVKC---------NFRQE-ASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1302
Cdd:PRK03918 434 AKGKCpvcgrelteEHRKElLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
846-1220 |
7.21e-10 |
|
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: 64.22 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 846 VQRLQKKLEDQNKEnhgLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELET 925
Cdd:pfam02463 164 GSRLKRKKKEALKK---LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 926 QKEQIQLKLQEKTEELKEKMDNlTKQLFDDVQKEERQrmlleksfelktqdyEKQIQSLKEEIKALKD-----EKMQLQH 1000
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEK-EEEKLAQVLKENKE---------------EEKEKKLQEEELKLLAkeeeeLKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSv 1080
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1081 edlehlnedgelwfayeglkkatrvleSHFQSQKDCYEKEIEALNFKVvhlsQEINHLQKLFREENDINESIRHEVTRLT 1160
Cdd:pfam02463 384 ---------------------------ERLSSAAKLKEEELELKSEEE----KEAQLLLELARQLEDLLKEEKKEELEIL 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 1161 SENMMIPDFKQQISELEKQKQDL----EIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALE 1220
Cdd:pfam02463 433 EEEEESIELKQGKLTEEKEELEKqelkLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
883-1338 |
1.01e-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: 63.60 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 883 KLEAELEkaaTHRRNYEEKGKRYRDAVEEKLA--------KLQKHNSELETQK---EQIQLKLQEKTEELKEKMDNLTkq 951
Cdd:pfam15921 56 KYEVELD---SPRKIIAYPGKEHIERVLEEYShqvkdlqrRLNESNELHEKQKfylRQSVIDLQTKLQEMQMERDAMA-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 952 lfdDVQKEERQrmlleksfelKTQDYEKQIQSLKEEIKA---LKDE-------------KMQLQH---LVEGEHVTSDGL 1012
Cdd:pfam15921 131 ---DIRRRESQ----------SQEDLRNQLQNTVHELEAakcLKEDmledsntqieqlrKMMLSHegvLQEIRSILVDFE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1013 KAEVARLSKQ---------------VKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQ-------LLESYD 1070
Cdd:pfam15921 198 EASGKKIYEHdsmstmhfrslgsaiSKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhqdrieqLISEHE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1071 IE----------------DVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVV----- 1129
Cdd:pfam15921 278 VEitgltekassarsqanSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVlanse 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1130 ---------HLSQEI----NHLQKLF-------------REEN------DINESIR--HEVTRLTSENMMIP-------- 1167
Cdd:pfam15921 358 ltearterdQFSQESgnldDQLQKLLadlhkrekelsleKEQNkrlwdrDTGNSITidHLRRELDDRNMEVQrleallka 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1168 -------DFKQQISELEKQKQDLE------IRLNEQAEKMKGKLEELSNQLHRSQEEEGT----------QRKALEAQNE 1224
Cdd:pfam15921 438 mksecqgQMERQMAAIQGKNESLEkvssltAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltaslqeKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1225 IHTKEKEKLIDKIQEMQeasdHLKkqfeTESEVKCNFRQEASRLTLenrdleeELDMKDRVIKKLQDQVKTLSKTIGKan 1304
Cdd:pfam15921 518 EITKLRSRVDLKLQELQ----HLK----NEGDHLRNVQTECEALKL-------QMAEKDKVIEILRQQIENMTQLVGQ-- 580
|
570 580 590
....*....|....*....|....*....|....
gi 2462545112 1305 dvHSSSGpkeylGMLQYKREDEAKLIQNLILDLK 1338
Cdd:pfam15921 581 --HGRTA-----GAMQVEKAQLEKEINDRRLELQ 607
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
879-1300 |
1.11e-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: 63.66 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 879 EKIQKLEAEL--EKAATHRRNYEE-----KGKRyrdaVEEKLAKLQKHNSELETQKEQIQLKLQEKTEEL---KEKMDNL 948
Cdd:pfam01576 103 QHIQDLEEQLdeEEAARQKLQLEKvtteaKIKK----LEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeeEEKAKSL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 949 TK----------QLFDDVQKEERQRMLLEKS---FELKTQDYEKQIQSLKEEIKALKdekMQLQHlvegehvTSDGLKAE 1015
Cdd:pfam01576 179 SKlknkheamisDLEERLKKEEKGRQELEKAkrkLEGESTDLQEQIAELQAQIAELR---AQLAK-------KEEELQAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1016 VARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQkREMREKMSEITKQLLEsyDIEDVRSRLsvED-LEHLNEDGELWF 1094
Cdd:pfam01576 249 LARLEEETAQKNNALKKIRELEAQISELQEDLESE-RAARNKAEKQRRDLGE--ELEALKTEL--EDtLDTTAAQQELRS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1095 AYEG----LKKA----TRVLESHFQSQKDCYEKEIEALN--------FKVV------HLSQEINHLQKLFREENDINESI 1152
Cdd:pfam01576 324 KREQevteLKKAleeeTRSHEAQLQEMRQKHTQALEELTeqleqakrNKANlekakqALESENAELQAELRTLQQAKQDS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1153 RHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEI---H 1226
Cdd:pfam01576 404 EHKRKKLEGQ---LQELQARLSESERQRAELAEKLSKlqsELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELlqeE 480
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 1227 TKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1300
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
967-1305 |
1.79e-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: 62.78 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 967 EKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQvktISEFEKEIELLQAQkidvekh 1046
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK---IGEIEKEIEQLEQE------- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1047 vqsqkremREKMSEItkqllesydIEDVRSRLSVEDLEHLNEDGELwfayeglkkatrvleshfqsqkDCYEKEIEALNF 1126
Cdd:TIGR02169 732 --------EEKLKER---------LEELEEDLSSLEQEIENVKSEL----------------------KELEARIEELEE 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1127 KVVHLSQEINHLqklfreENDINESIRHEVTRLTSEnmmipdFKQQISELEKQKQDLEIRLNEQaEKMKGKLEELSNQLH 1206
Cdd:TIGR02169 773 DLHKLEEALNDL------EARLSHSRIPEIQAELSK------LEEEVSRIEARLREIEQKLNRL-TLEKEYLEKEIQELQ 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1207 RSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFEtesevkcNFRQEASRLTLENRDLEEELDMKDRVI 1286
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG-------DLKKERDELEAQLRELERKIEELEAQI 912
|
330
....*....|....*....
gi 2462545112 1287 KKLQDQVKTLSKTIGKAND 1305
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEE 931
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
908-1277 |
2.24e-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: 62.68 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 908 AVEEKLAKLQKHNSE------LETQKEQIQLkLQEKTEELKEKMDNLTK---------QLFDDVQKEERQRMLLEKSFEL 972
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKtftrvvLLPQGEFAQF-LKAKSKEKKELLMNLFPldqytqlalMEFAKKKSLHGKAELLTLRSQL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 973 KTQDYEKQIQSLKEEIKALKDEKMQL----QHLVEGEHVTSDGLKAEVARLSKQvKTISEFEKEIELLQAQKIDVEKhvQ 1048
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLrealQQTQQSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEELRAQEAVLEE--T 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1049 SQKREMREKMSEITkqllesydiedvrsrLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKV 1128
Cdd:TIGR00618 283 QERINRARKAAPLA---------------AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1129 VHLSQEINHlqklFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQ----KQDLEIRLNEQAEKMKGKLEE--LS 1202
Cdd:TIGR00618 348 QTLHSQEIH----IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKlqslCKELDILQREQATIDTRTSAFrdLQ 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545112 1203 NQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEE 1277
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
921-1303 |
3.39e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 SELETQKEQIQLKLqEKTEElkekmdNLTKqlFDDVQKE--------ERQRMLLEKSFELKTQDYEKQIQSLKEEIKALK 992
Cdd:COG1196 168 SKYKERKEEAERKL-EATEE------NLER--LEDILGElerqleplERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 993 DEKMQLQHLVEGEHVTSDGLKAEVARLskqvktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQllesydie 1072
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAEL----------EAELEELRLELEELELELEEAQAEEYELLAELARL-------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1073 dvrsrlsVEDLEHLNEDgelwfayeglkkatrvlESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 1152
Cdd:COG1196 301 -------EQDIARLEER-----------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1153 RhevtrltsenmmipdfkQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEgTQRKALEAQNEIHTKEKEK 1232
Cdd:COG1196 357 E-----------------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLER 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 1233 LIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKA 1303
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
847-1269 |
3.81e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.66 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 847 QRLQKKlEDQNK-------ENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKH 919
Cdd:pfam05483 370 QRLEKN-EDQLKiitmelqKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 920 NSE---LETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELkTQDYEKQIQSLKEEIKALKDEKM 996
Cdd:pfam05483 449 EKEihdLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL-TQEASDMTLELKKHQEDIINCKK 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 997 QLQHLVegehvtsdglkaevarlskqvktisefeKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESydiEDVRS 1076
Cdd:pfam05483 528 QEERML----------------------------KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS---EENAR 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1077 RLSVEDLEHLNEDGELWFAYEGLKK----ATRVLESHFQSQK------DCYEKEIEALNFKVVHLSQEINHLQKLFREEN 1146
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKqienKNKNIEELHQENKalkkkgSAENKQLNAYEIKVNKLELELASAKQKFEEII 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1147 DiNESIRHEVTRLTSENMM--IPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNE 1224
Cdd:pfam05483 657 D-NYQKEIEDKKISEEKLLeeVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2462545112 1225 IHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLT 1269
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
828-1284 |
4.59e-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: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 828 RRFQSIRRFVLNIQL-----TYRVQRLQKKLEDQNKENHGLVEKLTS--------LAAL--RAGDVEKIQKLEaELE--- 889
Cdd:COG4913 496 EHYAAALRWVNRLHLrgrlvYERVRTGLPDPERPRLDPDSLAGKLDFkphpfrawLEAElgRRFDYVCVDSPE-ELRrhp 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 890 KAAT------HRRNYEEKGKRYRDA--------VEEKLAKLQKhnsELETQKEQIQlKLQEKTEELKEKMDNLTKQLfdd 955
Cdd:COG4913 575 RAITragqvkGNGTRHEKDDRRRIRsryvlgfdNRAKLAALEA---ELAELEEELA-EAEERLEALEAELDALQERR--- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 956 vqkeERQRMLLEKSF-ELKTQDYEKQIQSLKEEIKALKDEKMQLQHLvegehvtsdglkaevarlskqvktisefEKEIE 1034
Cdd:COG4913 648 ----EALQRLAEYSWdEIDVASAEREIAELEAELERLDASSDDLAAL----------------------------EEQLE 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1035 LLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQK 1114
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1115 DCYEKEIEALNFKVVHLSQEINHLQKLFREENDI----NESIRHEVTRLTSENmmIPDFKQQISELEKQ-----KQDLEI 1185
Cdd:COG4913 776 DALRARLNRAEEELERAMRAFNREWPAETADLDAdlesLPEYLALLDRLEEDG--LPEYEERFKELLNEnsiefVADLLS 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1186 RLNEQAEKMKGKLEELSNQLHRSQEEEGTqRKALEAQNEIHTKEKEKLidkiQEMQEASDHLKKQFETESEVKCNFRQEA 1265
Cdd:COG4913 854 KLRRAIREIKERIDPLNDSLKRIPFGPGR-YLRLEARPRPDPEVREFR----QELRAVTSGASLFDEELSEARFAALKRL 928
|
490 500
....*....|....*....|
gi 2462545112 1266 -SRLtlenRDLEEELDMKDR 1284
Cdd:COG4913 929 iERL----RSEEEESDRRWR 944
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
866-1298 |
4.77e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 866 KLTSLAALRAGDVEKIQKLEAELEKAA--THRRNYEEkgkryRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKE 943
Cdd:COG4717 36 KSTLLAFIRAMLLERLEKEADELFKPQgrKPELNLKE-----LKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 944 KMDNLTKQLfDDVQKEERQRMLLEKSFELKTQ--DYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSK 1021
Cdd:COG4717 110 ELEELREEL-EKLEKLLQLLPLYQELEALEAElaELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1022 QV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEI--TKQLLESYDIEDVRSRLSV----------------ED 1082
Cdd:COG4717 189 ATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELeqLENELEAAALEERLKEARLllliaaallallglggSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1083 LEHLNEDGELWFAYEGLkkaTRVLESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIrhEVTRLTSE 1162
Cdd:COG4717 269 LSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQ-ALPALEELEEEELEELLAALGLPPDL--SPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1163 NMMIPDFKQQISELEKQKQDLEIRLNEQaekmkgKLEELSNQLHRSQEEEGTQR-KALEAQNEIhTKEKEKLIDKIQEMQ 1241
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLEELEQ------EIAALLAEAGVEDEEELRAAlEQAEEYQEL-KEELEELEEQLEELL 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545112 1242 EASDHLKKQFETEsevkcNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSK 1298
Cdd:COG4717 416 GELEELLEALDEE-----ELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
934-1292 |
8.99e-09 |
|
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: 59.91 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 934 LQEKTEE-LKEKMDNLTKQLFDDVQKE-ERQRMLLEK-SFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSD 1010
Cdd:pfam07888 32 LQNRLEEcLQERAELLQAQEAANRQREkEKERYKRDReQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1011 GLKAEVARLSKQ----VKTISEFEKEIELLQAQKIDVEkhvqSQKREMREKMSEITKQLLESY-DIEDVRSRL--SVEDL 1083
Cdd:pfam07888 112 ELSEEKDALLAQraahEARIRELEEDIKTLTQRVLERE----TELERMKERAKKAGAQRKEEEaERKQLQAKLqqTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1084 EHLNEDgelwfaYEGLKKATRVLESHFQSQKDcyekeiealnfKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSEN 1163
Cdd:pfam07888 188 RSLSKE------FQELRNSLAQRDTQVLQLQD-----------TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1164 MMIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEM 1240
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRL 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545112 1241 QEA-----SDHLKKQFETESEVKCNFRQEAsrltlENRDLEEELDMKDRVIKKLQDQ 1292
Cdd:pfam07888 331 EERlqeerMEREKLEVELGREKDCNRVQLS-----ESRRELQELKASLRVAQKEKEQ 382
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
806-1241 |
1.08e-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: 60.15 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 806 RKMLEEHKavilqkyarawlaRRRFQSIRRFVLNiQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVE------ 879
Cdd:pfam07111 131 RKNLEEGS-------------QRELEEIQRLHQE-QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKqlaeaq 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 880 --------KIQKLEAELEKAAT-----------------HRRNYEEKGKRYRDAVEEklakLQKHNSELETQKEQIQLKL 934
Cdd:pfam07111 197 keaellrkQLSKTQEELEAQVTlveslrkyvgeqvppevHSQTWELERQELLDTMQH----LQEDRADLQATVELLQVRV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 935 QEKTEELKEKMDNLTK--QLFDDVQKE--ERQRMLL----EKSF----ELKTQDYEK---------QIQSLKEEIKALKD 993
Cdd:pfam07111 273 QSLTHMLALQEEELTRkiQPSDSLEPEfpKKCRSLLnrwrEKVFalmvQLKAQDLEHrdsvkqlrgQVAELQEQVTSQSQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 994 EKMQLQHL-------VEGEHVTSDGLKAEVARLS----KQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEI- 1061
Cdd:pfam07111 353 EQAILQRAlqdkaaeVEVERMSAKGLQMELSRAQearrRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIp 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1062 --TKQLleSYDIEDVRS------------RLSVE-----------------DLEHLNEDGELWFAYegLKKATRVLESHF 1110
Cdd:pfam07111 433 slSNRL--SYAVRKVHTikglmarkvalaQLRQEscpppppappvdadlslELEQLREERNRLDAE--LQLSAHLIQQEV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1111 QSQKDCYEKEIEALNFKVVHLSQEINHLQKLF--------------REENDINESIRHEVTRltSENMMIPDFKQQISEL 1176
Cdd:pfam07111 509 GRAREQGEAERQQLSEVAQQLEQELQRAQESLasvgqqlevarqgqQESTEEAASLRQELTQ--QQEIYGQALQEKVAEV 586
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545112 1177 E----KQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQ 1241
Cdd:pfam07111 587 EtrlrEQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRVQELE 655
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
938-1343 |
1.08e-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: 60.24 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 938 TEELKEKMDNLTKQLFDDVQKEERQrmllEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHL-VEGEHVTSDGLKAEV 1016
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAA----EEQLVQANGELEKASREETFARTALKNARLDLRRLfDEKQSEKDKKNKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1017 ARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSrlsvedlehlneDGELWFAY 1096
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL------------KAAIAARR 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1097 EGLKKATRVLESHfqsqkdcYEKEIEALNF---KVVHLSQEINHL-QKLFREENDinesiRHEVTRLTsenmmipDFKQQ 1172
Cdd:pfam12128 743 SGAKAELKALETW-------YKRDLASLGVdpdVIAKLKREIRTLeRKIERIAVR-----RQEVLRYF-------DWYQE 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1173 ISELEKQkqdleiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQneihTKEKEKLIDKIQEMQEASDHLKKQFE 1252
Cdd:pfam12128 804 TWLQRRP------RLATQLSNIERAISELQQQLARLIADTKLRRAKLEME----RKASEKQQVRLSENLRGLRCEMSKLA 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1253 TESEvKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKandvHSSSGPKEYlgmLQYKREDEAKLIQN 1332
Cdd:pfam12128 874 TLKE-DANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD----HSGSGLAET---WESLREEDHYQNDK 945
|
410
....*....|.
gi 2462545112 1333 LILDLKPRGVV 1343
Cdd:pfam12128 946 GIRLLDYRKLV 956
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
972-1305 |
1.78e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 972 LKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQK 1051
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1052 rEMREKMSEITKQLlesydiedvrsrLSVE-DLEHLNED-GELWFAYEGLKKATRVLESHfqsqkdcyEKEIEALNFKVv 1129
Cdd:PRK03918 235 -ELKEEIEELEKEL------------ESLEgSKRKLEEKiRELEERIEELKKEIEELEEK--------VKELKELKEKA- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1130 hlsQEINHLQKLFREENDINESIRHEVTRLTsenmmipdfkQQISELEKQKQDLEiRLNEQAEKMKGKLEELSNQLHRSQ 1209
Cdd:PRK03918 293 ---EEYIKLSEFYEEYLDELREIEKRLSRLE----------EEINGIEERIKELE-EKEERLEELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1210 EEEGTQRKALEAQNEIHT-------KEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLE----------- 1271
Cdd:PRK03918 359 ERHELYEEAKAKKEELERlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieelkkakgkc 438
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462545112 1272 ---NRDLEEEldMKDRVIKKLQDQVKTLSKTIGKAND 1305
Cdd:PRK03918 439 pvcGRELTEE--HRKELLEEYTAELKRIEKELKEIEE 473
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
834-1203 |
1.80e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 834 RRFVLNIQLTYRvQRLQKKLEDQNKENHGLVEKLTSLAALragdVEKIQKLEAELEKAATHR------RNYEEKGKRYRD 907
Cdd:PRK04863 281 RRVHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAEL----NEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 908 AVEEKLAKLQKHNSELETQKEQiQLKLQEKTEELKEKMDNLTKQLFDDVQK-EERQRMLLEksfelktqdYEKQIQSLkE 986
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQ-QEENEARAEAAEEEVDELKSQLADYQQAlDVQQTRAIQ---------YQQAVQAL-E 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 987 EIKALKD---------EKMQLQHLVEGEHVTSDGLKAEvARLSKQVKTISEFEKEIELLQAQKIDVE------------- 1044
Cdd:PRK04863 425 RAKQLCGlpdltadnaEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSQFEQAYQLVRKIAGEVSrseawdvarellr 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1045 -----KHVQSQKREMREKMSEITKQLLESYDIEDVRSRL---------SVEDLEHLNEDGElwfayeglkkatRVLESHF 1110
Cdd:PRK04863 504 rlreqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFckrlgknldDEDELEQLQEELE------------ARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1111 QSQKDCYEKEIEaLNFKVVHLSQEINHLQKL---FREENDINESIRHEV--TRLTSENMMipDFKQQISELEKQKQDLEI 1185
Cdd:PRK04863 572 ESVSEARERRMA-LRQQLEQLQARIQRLAARapaWLAAQDALARLREQSgeEFEDSQDVT--EYMQQLLERERELTVERD 648
|
410
....*....|....*...
gi 2462545112 1186 RLNEQAEKMKGKLEELSN 1203
Cdd:PRK04863 649 ELAARKQALDEEIERLSQ 666
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
876-1302 |
4.62e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.37 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 876 GDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLqekteelkekmdnltkqlfdd 955
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKL--------------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 956 vqkeerqrmlleksfelktQDYEKQIQSLKEEIKALKDEKMQLQHLVE-----------GEHVTSDGLKAEVARLSKQVK 1024
Cdd:PRK01156 419 -------------------QDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKS 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1025 TISEFEKEIElLQAQKIDvEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSvEDLEHLNEDGELWFAYEGLKKATR 1104
Cdd:PRK01156 480 RLEEKIREIE-IEVKDID-EKIVDLKKRKEYLESEEINKSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1105 VLEshfqsQKDCYEKEIEALNFKVVHLSQEINHLQKLFreeNDINESIRHEVTRLTSENMMIPDFK----QQISELEKQK 1180
Cdd:PRK01156 557 SLK-----LEDLDSKRTSWLNALAVISLIDIETNRSRS---NEIKKQLNDLESRLQEIEIGFPDDKsyidKSIREIENEA 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1181 QDLEIRLNE------QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT--KEKEKLIDKIqemqeasdhLKKQFE 1252
Cdd:PRK01156 629 NNLNNKYNEiqenkiLIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDnlKKSRKALDDA---------KANRAR 699
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1253 TESEVKCNfRQEASRLTLENRDLEEELDMKDRVIKKLQDqVKTLSKTIGK 1302
Cdd:PRK01156 700 LESTIEIL-RTRINELSDRINDINETLESMKKIKKAIGD-LKRLREAFDK 747
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
801-1328 |
6.72e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 801 ARR--RYRKMLEEHKAVILQKY--ARAWLARRRFQSIRRF--VLNIQLTYRVQRLQKKLEDQNKenhglvekltslaALR 874
Cdd:PTZ00121 1181 ARKaeEVRKAEELRKAEDARKAeaARKAEEERKAEEARKAedAKKAEAVKKAEEAKKDAEEAKK-------------AEE 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 875 AGDVEKIQKLEaELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFD 954
Cdd:PTZ00121 1248 ERNNEEIRKFE-EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 955 DVQKEERQRmllEKSFELKTQDYEKQIQSLKEEIKALKDEKmqlqhlvegehvtsdglKAEVARLSKqvktiSEFEKEIE 1034
Cdd:PTZ00121 1327 AKKKADAAK---KKAEEAKKAAEAAKAEAEAAADEAEAAEE-----------------KAEAAEKKK-----EEAKKKAD 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1035 LLQAQKIDVEKHVQSQKR--EMREKMSEITKQLLESYDIEDVRSRLSvedlehlnedgELWFAYEGLKKATRVLESHFQS 1112
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKKADEAKKKAE-----------EKKKADEAKKKAEEAKKADEAK 1450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1113 QKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIR--HEVTRLTSENMMIPDFKQQISEL----EKQKQDlEIR 1186
Cdd:PTZ00121 1451 KKAEEAKKAEEAK-KKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEAKKAAEAKKKADEAkkaeEAKKAD-EAK 1528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1187 LNEQAEKM--------KGKLEELSNQLHRSQEEEgtQRKALEAQNEihTKEKEKLIDKIQEMQEASDHLKKQFETESEVK 1258
Cdd:PTZ00121 1529 KAEEAKKAdeakkaeeKKKADELKKAEELKKAEE--KKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1259 CNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPKEYLGMLQYKREDEAK 1328
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
841-1185 |
7.59e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.44 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQKKLEDQNKENHGLVEKltslaalragdvEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHN 920
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQ------------ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 S-ELETQKEQIQLKLQEKTEELK-----------EKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQ--IQSLKE 986
Cdd:pfam17380 341 RmAMERERELERIRQEERKRELErirqeeiameiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQrkIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 987 EIKALKDEKmqlqhlvegehvtSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVekhVQSQKREMREKMSEITKQLL 1066
Cdd:pfam17380 421 EMEQIRAEQ-------------EEARQREVRRLEEERAREMERVRLEEQERQQQVER---LRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1067 ESYDIEDVRSRLSVEDLEHLNEdgelwfAYEGLKKATRVLESHFQS-QKDCYEKEIEalnfkvvHLSQEINHLQKLFREE 1145
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQ------AMIEEERKRKLLEKEMEErQKAIYEEERR-------REAEEERRKQQEMEER 551
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2462545112 1146 NDINESIR---HEVTRLTS---ENMMIpdfkQQISELEKQKQDLEI 1185
Cdd:pfam17380 552 RRIQEQMRkatEERSRLEAmerEREMM----RQIVESEKARAEYEA 593
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
845-1314 |
1.01e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLTSLAALragdVEKIQKLEAELEKAATHRRNYEEKGKRYRDaVEEKLAKLQkhNSELE 924
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSALNELSSL----EDMKNRYESEIKTAESDLSMELEKNNYYKE-LEERHMKII--NDPVY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 925 TQKEQIQ--LKLQEKTEELKEKMDNLTKQL--FDDVQKEERQrmlLEKSFElktqDYEKQiQSLKEEIKALKDEkmqlqh 1000
Cdd:PRK01156 292 KNRNYINdyFKYKNDIENKKQILSNIDAEInkYHAIIKKLSV---LQKDYN----DYIKK-KSRYDDLNNQILE------ 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 lVEGEHVTSDGLKAEVARLSKQvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLE-SYDIE--DVRSR 1077
Cdd:PRK01156 358 -LEGYEMDYNSYLKSIESLKKK---IEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDiSSKVSslNQRIR 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1078 LSVEDLEHLNEDGELWFAYE---------GLKKATRVLEsHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKL--FREEN 1146
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQSvcpvcgttlGEEKSNHIIN-HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRkeYLESE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1147 DINESIrhevtrlTSENmmipdfkqQISELEKQKQDLEIRLNEQAEKmKGKLEELSNQlHRSQEEEGTQRKALEAQNEIH 1226
Cdd:PRK01156 513 EINKSI-------NEYN--------KIESARADLEDIKIKINELKDK-HDKYEEIKNR-YKSLKLEDLDSKRTSWLNALA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1227 TKEkekLIDkIQEMQEASDHLKKQF-ETES---EVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1302
Cdd:PRK01156 576 VIS---LID-IETNRSRSNEIKKQLnDLESrlqEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGK 651
|
490
....*....|..
gi 2462545112 1303 ANDVHSSSGPKE 1314
Cdd:PRK01156 652 IDNYKKQIAEID 663
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
778-1193 |
1.15e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 778 VRSLYQLIRMATITMQAYSRGFLARRRYRKMLEEHKAVILQkyarawlARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQN 857
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-------LREELEKLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 858 KENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATHRRNYEEK-GKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQE 936
Cdd:COG4717 146 ERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELE-EAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 937 KTEELKEKMDNLTKQLFDDVQKEERQRMLLEK-------SFELKTQDYEKQIQSLKEEIKA---------LKDEKMQLQH 1000
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLliaaallALLGLGGSLLSLILTIAGVLFLvlgllallfLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 LVEGEHVTSDGLKAEVARLS-KQVKTISEFEKEIELLQAQK-IDVEKHVQSQKREMREKMSEITKQLLESyDIEDVRSRL 1078
Cdd:COG4717 301 GKEAEELQALPALEELEEEElEELLAALGLPPDLSPEELLElLDRIEELQELLREAEELEEELQLEELEQ-EIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1079 SVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKvvHLSQEINHLQ-KLFREENDINEsIRHEVT 1157
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEeELEELEEELEE-LREELA 456
|
410 420 430
....*....|....*....|....*....|....*.
gi 2462545112 1158 RLTSENMMIPDfKQQISELEKQKQDLEIRLNEQAEK 1193
Cdd:COG4717 457 ELEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1026-1308 |
1.22e-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: 57.00 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1026 ISEFEKEIELLQA------QKIDVEKHVQSQKREMREKMsEITKQLLESYDieDVRSRL-SVEDLEHLNEdgelwfayeg 1098
Cdd:TIGR02169 165 VAEFDRKKEKALEeleeveENIERLDLIIDEKRQQLERL-RREREKAERYQ--ALLKEKrEYEGYELLKE---------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1099 lKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREEN-DINE-------SIRHEVTRLTSE----NMMI 1166
Cdd:TIGR02169 232 -KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkKIKDlgeeeqlRVKEKIGELEAEiaslERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1167 PDFKQQISELEKQKQDLEIRLNEQAEKM----------KGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT--------- 1227
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIeelereieeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelkdy 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1228 -KEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDV 1306
Cdd:TIGR02169 391 rEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
..
gi 2462545112 1307 HS 1308
Cdd:TIGR02169 471 LY 472
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1225 |
1.83e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAElEKAATHRRNYEEKGKRYRDAVEEKLaKLQKHNSELE 924
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKI-KAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 925 TQKEQIQLKLQE-----KTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEkmQLQ 999
Cdd:PTZ00121 1631 EKKKVEQLKKKEaeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE--ELK 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1000 HLVEGEHVTSDGL-KAEVARLSKQVKTISEFEKEIELLQAQKIDVE--KHVQSQKREMREKMSEITKQ----LLESYDIE 1072
Cdd:PTZ00121 1709 KKEAEEKKKAEELkKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekKKIAHLKKEEEKKAEEIRKEkeavIEEELDEE 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1073 DVRSRLSVE-DLEHLNEDGELwfAYEGLKKATRVLeshfQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINES 1151
Cdd:PTZ00121 1789 DEKRRMEVDkKIKDIFDNFAN--IIEGGKEGNLVI----NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545112 1152 IRHEVTRLTSENMMIPDFKQQISELEKQKQ----DLEIRLNEQaeKMKGKLEELSNQlhRSQEEEGTQRKALEAQNEI 1225
Cdd:PTZ00121 1863 DGNKEADFNKEKDLKEDDEEEIEEADEIEKidkdDIEREIPNN--NMAGKNNDIIDD--KLDKDEYIKRDAEETREEI 1936
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
845-998 |
2.09e-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: 53.78 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKEnhgLVEKLTSLAALRAgdveKIQKLEAELEKAATHRRNYEEKGKRYRDAVEekLAKLQKhnsELE 924
Cdd:COG1579 32 ELAELEDELAALEAR---LEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRNNKE--YEALQK---EIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 925 TQKEQIQlKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQL 998
Cdd:COG1579 100 SLKRRIS-DLEDEILELMERIEELEEEL----AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
863-1309 |
2.34e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 863 LVEKLTSLAALRAgDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEK-LAKLQKHNSELETQKEQIQlKLQEKTEEL 941
Cdd:COG4913 230 LVEHFDDLERAHE-ALEDAREQIELLEPIRELAERYAAARERLAELEYLRaALRLWFAQRRLELLEAELE-ELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 942 KEKMDNLTKQLfDDVQKEERQrmlLEKsfELKTQDYEkQIQSLKEEIKALKDEK-------MQLQHLVEGEHVTSDGLKA 1014
Cdd:COG4913 308 EAELERLEARL-DALREELDE---LEA--QIRGNGGD-RLEQLEREIERLERELeererrrARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1015 EVARLSKQVKTISEFEKEI-ELLQAQKIDVEKHVQSQKREMREKMSEItkQLLES------YDIEDVRSRLSvedlEHLN 1087
Cdd:COG4913 381 EFAALRAEAAALLEALEEElEALEEALAEAEAALRDLRRELRELEAEI--ASLERrksnipARLLALRDALA----EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1088 ED-GELWF----------------AYEGL---------------KKATRVLESHFQSQKDCYEKeIEALNFKVVHLSQEI 1135
Cdd:COG4913 455 LDeAELPFvgelievrpeeerwrgAIERVlggfaltllvppehyAAALRWVNRLHLRGRLVYER-VRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1136 NHL-QKLFREENDINESIRHEVTR-------------------LTSENMM--------------IP-------DFKQQIS 1174
Cdd:COG4913 534 DSLaGKLDFKPHPFRAWLEAELGRrfdyvcvdspeelrrhpraITRAGQVkgngtrhekddrrrIRsryvlgfDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1175 ELEKQKQDLEIRLNE---QAEKMKGKLEELSNQ---LHRSQEEEGTQRKALEAQNEIHTKEKEklidkIQEMQEASDHLK 1248
Cdd:COG4913 614 ALEAELAELEEELAEaeeRLEALEAELDALQERreaLQRLAEYSWDEIDVASAEREIAELEAE-----LERLDASSDDLA 688
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 1249 KQfetesevkcnfRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSS 1309
Cdd:COG4913 689 AL-----------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
921-1300 |
2.48e-07 |
|
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: 55.80 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 SELETQKEQIQLKLQEKTEELKekmdNLTKQLFDDVQKeerqrmllEKSFELKTQDYEKQIQSLKeeiKALKDEKMQLqh 1000
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELK----NLDKNLNKDEEK--------INNSNNKIKILEQQIKDLN---DKLKKNKDKI-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 lvegehvtsDGLKAEVARLSKQVKT----ISEFEKEIELLQAQKIDVEKHV----------QSQKREMREKMSEITKQLL 1066
Cdd:TIGR04523 99 ---------NKLNSDLSKINSEIKNdkeqKNKLEVELNKLEKQKKENKKNIdkflteikkkEKELEKLNNKYNDLKKQKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1067 E--------SYDIEDVRSRLSVEDLEHLNEDGELwFAYEGLKKATRVLES---HFQSQKDCYEKEIEALNFKVVHLSQEI 1135
Cdd:TIGR04523 170 ElenelnllEKEKLNIQKNIDKIKNKLLKLELLL-SNLKKKIQKNKSLESqisELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1136 N----HLQKLFREENDINESIRHEVTRLTSENMMIPD-------FKQQISELEKQK-QDLEIRLNEQAEKMKGKLEELSN 1203
Cdd:TIGR04523 249 SntqtQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKElekqlnqLKSEISDLNNQKeQDWNKELKSELKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1204 QLHRSQE---EEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELD 1280
Cdd:TIGR04523 329 QISQNNKiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
410 420
....*....|....*....|
gi 2462545112 1281 MKDRVIKKLQDQVKTLSKTI 1300
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEI 428
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
846-1297 |
4.58e-07 |
|
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: 55.18 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 846 VQRLQKKLEDQNKEnhgLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR---DAVEEKLAKLQKHNSE 922
Cdd:pfam01576 403 SEHKRKKLEGQLQE---LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSkdvSSLESQLQDTQELLQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 923 LETQK----------EQIQLKLQEKTEELKEKMDNLTK-------QLFDDVQKEERQRMLLEKSFELK---TQDYEKQIQ 982
Cdd:pfam01576 480 ETRQKlnlstrlrqlEDERNSLQEQLEEEEEAKRNVERqlstlqaQLSDMKKKLEEDAGTLEALEEGKkrlQRELEALTQ 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 983 SLKEEIKA---LKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMS 1059
Cdd:pfam01576 560 QLEEKAAAydkLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAL 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1060 EITKQLLESYD----IEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQS---QKDCYEKEIEA-----LNFK 1127
Cdd:pfam01576 640 SLARALEEALEakeeLERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEmktQLEELEDELQAtedakLRLE 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1128 VVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNE-----------------Q 1190
Cdd:pfam01576 720 VNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqidaankgreeavkQ 799
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1191 AEKMKGKLEELSNQL---HRSQEEEGTQRKaleaQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETE-----SEVKCN-- 1260
Cdd:pfam01576 800 LKKLQAQMKDLQRELeeaRASRDEILAQSK----ESEKKLKNLEAELLQLQEDLAASERARRQAQQErdelaDEIASGas 875
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462545112 1261 ----FRQEASRLTLENRDLEEELD--------MKDRViKKLQDQVKTLS 1297
Cdd:pfam01576 876 gksaLQDEKRRLEARIAQLEEELEeeqsntelLNDRL-RKSTLQVEQLT 923
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
850-1140 |
4.94e-07 |
|
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: 53.66 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 850 QKKLEDQNKenHGLVEKLTSLAALRAGDVEK-IQKLEAELEK------AAThrrnyeekgkRYRDAVEEKLAKLQKHNSE 922
Cdd:pfam15905 66 QKNLKESKD--QKELEKEIRALVQERGEQDKrLQALEEELEKveaklnAAV----------REKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 923 LETQKEQIQLKLQEKTEelKEKMDNLTKQLF---DDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQ 999
Cdd:pfam15905 134 LTRVNELLKAKFSEDGT--QKKMSSLSMELMklrNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1000 HLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQllesydIEDVRSRLS 1079
Cdd:pfam15905 212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ------IKDLNEKCK 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 1080 VedLEHLNEDgelwfayeglkkatrvLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQK 1140
Cdd:pfam15905 286 L--LESEKEE----------------LLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
910-1328 |
7.23e-07 |
|
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: 54.28 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 910 EEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNL------------TKQLFDDVQKEERQRMLLEKsfelKTQDY 977
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqdeesdLERLKEEIEKSSKQRAMLAG----ATAVY 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 978 EKQIQSLKEEI--------------KALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEF----EKEIELLQAQ 1039
Cdd:TIGR00606 666 SQFITQLTDENqsccpvcqrvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrQSIIDLKEKE 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1040 KIDVEKHVQSQKREMREKMSEITKQ--LLESYDIEDVRSRLSVED------LEHLNEDGELWFAYEGLKKATRVLESHFQ 1111
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQetLLGTIMPEEESAKVCLTDvtimerFQMELKDVERKIAQQAAKLQGSDLDRTVQ 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1112 SQKdcyeKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQA 1191
Cdd:TIGR00606 826 QVN----QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1192 EKMKGKLEE---LSNQLHRSQEEEGTQRKALEAQNEIHTKE----KEKLIDKIQEM-------QEASDHLKKQFETE--- 1254
Cdd:TIGR00606 902 REIKDAKEQdspLETFLEKDQQEKEELISSKETSNKKAQDKvndiKEKVKNIHGYMkdienkiQDGKDDYLKQKETElnt 981
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545112 1255 ---SEVKCNFRQEasRLTLENRDLEEELDMKDRVIKKLQDQVkTLSKTIGKANDVHSSsgPKEYLGMLQYKREDEAK 1328
Cdd:TIGR00606 982 vnaQLEECEKHQE--KINEDMRLMRQDIDTQKIQERWLQDNL-TLRKRENELKEVEEE--LKQHLKEMGQMQVLQMK 1053
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
849-1279 |
8.48e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 849 LQKKLEDQNKENHGLVEKLTSLAALRAGDVEkiqkLEAELEKAATHRR------NYEEKGKRYRDAVEEKLAKLQKHNSE 922
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARELEELSARESD----LEQDYQAASDHLNlvqtalRQQEKIERYQEDLEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 923 LETQKEQiQLKLQEKTEELKEKMDNLTKQLfDDVQK--EERQRMLLEksfelktqdYEKQIQSLKEEikalkdekmqlQH 1000
Cdd:COG3096 370 VEEAAEQ-LAEAEARLEAAEEEVDSLKSQL-ADYQQalDVQQTRAIQ---------YQQAVQALEKA-----------RA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 LVEGEHVTSDGLKAEVARLSKQVKTISEfekeiELLQA-QKIDVEkhvQSQKREMREKMseitkQLLESYDIEDVRSRls 1079
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATE-----EVLELeQKLSVA---DAARRQFEKAY-----ELVCKIAGEVERSQ-- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1080 vedlehlnedgelwfAYEglkKATRVLESHfQSQKDCYEKEiEALNFKVVHLSQEINHLQKLFREENDINESIRHEVtrl 1159
Cdd:COG3096 493 ---------------AWQ---TARELLRRY-RSQQALAQRL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL--- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1160 tSENMMIPDFKqqiSELEKQKQDLEIRLNEQAEKmkgkleelSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLiDKIQE 1239
Cdd:COG3096 550 -DAAEELEELL---AELEAQLEELEEQAAEAVEQ--------RSELRQQLEQLRARIKELAARAPAWLAAQDAL-ERLRE 616
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462545112 1240 M--------QEASDHLKKQFETESEVKcnfrQEASRLTLENRDLEEEL 1279
Cdd:COG3096 617 QsgealadsQEVTAAMQQLLEREREAT----VERDELAARKQALESQI 660
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
879-1279 |
8.92e-07 |
|
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: 54.03 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 879 EKIQKLEAELEKAathrrnyeekgKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKT------EELKEKMDNlTKQL 952
Cdd:pfam01576 5 EEMQAKEEELQKV-----------KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcaeaEEMRARLAA-RKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 953 FDDV---------QKEER-QRMLLEKsfelktQDYEKQIQSLKEEIKALKDEKMQLQHlvegEHVTSDGlkaevarlskq 1022
Cdd:pfam01576 73 LEEIlhelesrleEEEERsQQLQNEK------KKMQQHIQDLEEQLDEEEAARQKLQL----EKVTTEA----------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1023 vkTISEFEKEIELLQAQKIDVEKhvqsQKREMREKMSEITKQLLESYDIEDVRSRLS------VEDLE-HLNEDGELWFA 1095
Cdd:pfam01576 132 --KIKKLEEDILLLEDQNSKLSK----ERKLLEERISEFTSNLAEEEEKAKSLSKLKnkheamISDLEeRLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1096 YEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREE----NDINESIRHEVTRLTSENMMIPDFKQ 1171
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEEtaqkNNALKKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1172 QISELEKQKQDLEirlnEQAEKMKGKLEEL-----SNQLHRSQ-EEEGTQ-RKALEAQNEIHtkeKEKLIDKIQEMQEAS 1244
Cdd:pfam01576 286 ARNKAEKQRRDLG----EELEALKTELEDTldttaAQQELRSKrEQEVTElKKALEEETRSH---EAQLQEMRQKHTQAL 358
|
410 420 430
....*....|....*....|....*....|....*
gi 2462545112 1245 DHLKKQFETESEVKCNFRQEASRLTLENRDLEEEL 1279
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
878-1220 |
1.05e-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: 53.42 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 878 VEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQ 957
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 958 KEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKdekmqlqhlvegehvtsDGLKAEVARLSKQVKTISEfEKEIELLQ 1037
Cdd:COG5185 315 EEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQ-----------------ESLTENLEAIKEEIENIVG-EVELSKSS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1038 AQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDgelwfayegLKKATRVLEShFQSQKDCY 1117
Cdd:COG5185 377 EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQ---------IEQATSSNEE-VSKLLNEL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1118 EKEIEalnfKVVHLSQEiNHLQKLFREENDINESIRHEVTRLTSENMMIpdfKQQISELEKQKQDLEIRLNEQAEKMKGK 1197
Cdd:COG5185 447 ISELN----KVMREADE-ESQSRLEEAYDEINRSVRSKKEDLNEELTQI---ESRVSTLKATLEKLRAKLERQLEGVRSK 518
|
330 340
....*....|....*....|...
gi 2462545112 1198 LEELSNQLHRSQEEEGTQRKALE 1220
Cdd:COG5185 519 LDQVAESLKDFMRARGYAHILAL 541
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
928-1275 |
1.08e-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: 53.61 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 928 EQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERqrmlleKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHV 1007
Cdd:pfam09731 44 EEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTG------ESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1008 TSDglKAEVARLSKQVKTISEFEKEIELLQAQ--------KIDVEKHVQSQKREM------REKMSEITKQLLESYDIED 1073
Cdd:pfam09731 118 QLP--KSEQEKEKALEEVLKEAISKAESATAVakeakddaIQAVKAHTDSLKEASdtaeisREKATDSALQKAEALAEKL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1074 VRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIR 1153
Cdd:pfam09731 196 KEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1154 HEVTRLTSE-NMMIPDFKQQISELEKQKQDL----EIRLNEQAEKMKGKLEELSNQL------HRSQEEEGTQRKALEAQ 1222
Cdd:pfam09731 276 EDNLLSNDDlNSLIAHAHREIDQLSKKLAELkkreEKHIERALEKQKEELDKLAEELsarleeVRAADEAQLRLEFERER 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462545112 1223 NEIHTKEKEKLIDKIQEMQEA-SDHLKKQFET-ESEVKCNFRQEASRLTLENRDL 1275
Cdd:pfam09731 356 EEIRESYEEKLRTELERQAEAhEEHLKDVLVEqEIELQREFLQDIKEKVEEERAG 410
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
847-1212 |
1.19e-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: 53.90 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 847 QRLQKKLEDQNKENHGLVEKLTSLAALRagDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVE--EKLAKLQKHNSELE 924
Cdd:TIGR01612 1325 KELQKNLLDAQKHNSDINLYLNEIANIY--NILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDksEKLIKKIKDDINLE 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 925 TQKEQIQLKLQE-------------KTEELKEKMDNLTkqLFDDVQKEERQRMLLEKSFEL---KTQ------------D 976
Cdd:TIGR01612 1403 ECKSKIESTLDDkdidecikkikelKNHILSEESNIDT--YFKNADENNENVLLLFKNIEMadnKSQhilkikkdnatnD 1480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 977 YEKQIQSLKEEI---KALKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQV------KTISEFEKEIELLQAQKIDVEKHV 1047
Cdd:TIGR01612 1481 HDFNINELKEHIdksKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYsalaikNKFAKTKKDSEIIIKEIKDAHKKF 1560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1048 QSQKREMREKMSEITKqllESYDIEDvrsrlsveDLEHLNEDGElwfAYEGLKKATRVLESHF-------QSQKDCYeKE 1120
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKK---EKFRIED--------DAAKNDKSNK---AAIDIQLSLENFENKFlkisdikKKINDCL-KE 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1121 IEALNFKVVHLSqeINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEE 1200
Cdd:TIGR01612 1626 TESIEKKISSFS--IDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIE 1703
|
410
....*....|..
gi 2462545112 1201 LSNQLHRSQEEE 1212
Cdd:TIGR01612 1704 KIKEIAIANKEE 1715
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
851-1328 |
1.21e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 851 KKLEDQNKENHGLVEKLTSL--AALRAGDVEKIQKLE--AELEKAATHRRNYEEK----GKRYRDAVEEKLAKLQKHNSE 922
Cdd:PTZ00121 1098 GKAEEAKKTETGKAEEARKAeeAKKKAEDARKAEEARkaEDARKAEEARKAEDAKrveiARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 923 LETQKEQIQLKlqeKTEELKEKmdnltkqlfDDVQKEERQRMLLE--KSFELKTQDYEKQIQSLKEEIKALKDE----KM 996
Cdd:PTZ00121 1178 AEAARKAEEVR---KAEELRKA---------EDARKAEAARKAEEerKAEEARKAEDAKKAEAVKKAEEAKKDAeeakKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 997 QLQHLVEGEHVTSDGLKAEVARLSKQVKTiSEFEKEIELLQAQkiDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRS 1076
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKA-EEARKADELKKAE--EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1077 RLSvedlEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKeiealnfkvvhlSQEINHLQKLFREEndinESIRHEV 1156
Cdd:PTZ00121 1323 KAE----EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA------------AEEKAEAAEKKKEE----AKKKADA 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1157 TRLTSEnmmipdfkqqiselEKQKQDleiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDK 1236
Cdd:PTZ00121 1383 AKKKAE--------------EKKKAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1237 IQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPK--- 1313
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkad 1525
|
490
....*....|....*
gi 2462545112 1314 EYLGMLQYKREDEAK 1328
Cdd:PTZ00121 1526 EAKKAEEAKKADEAK 1540
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
659-1228 |
1.30e-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: 53.43 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 659 TKQELSFSDKKEVCKVVLHRLIQDSNQYQFGKTKIffragQVAYLEKLRLDKLrQSCVMVQKHMRGWLQRKkfLRERRAA 738
Cdd:TIGR00618 361 HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL-----QSLCKELDILQRE-QATIDTRTSAFRDLQGQ--LAHAKKQ 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 739 LIIQQYFRGQQtvRKAITAVAlKEAWAAIIIQKHCRGYLVRSLYQLIRMATITMQaYSRgflarrryRKMLEEHKAVILQ 818
Cdd:TIGR00618 433 QELQQRYAELC--AAAITCTA-QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ-ETR--------KKAVVLARLLELQ 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 819 KYARAWLARRRFQSIRRFVLNIQ--LTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRR 896
Cdd:TIGR00618 501 EEPCPLCGSCIHPNPARQDIDNPgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDN 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 897 NYEEKGKRYRDAVEEklakLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQD 976
Cdd:TIGR00618 581 RSKEDIPNLQNITVR----LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLT 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 977 YEKQIQSLK--EEIKALKDEKMQ-----LQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQ----AQKIDVEK 1045
Cdd:TIGR00618 657 QERVREHALsiRVLPKELLASRQlalqkMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEnassSLGSDLAA 736
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1046 HVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNE----DGELWF---AYEGLKKATRVLESHFQSQKDCYE 1118
Cdd:TIGR00618 737 REDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAElshlAAEIQFfnrLREEDTHLLKTLEAEIGQEIPSDE 816
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1119 keiEALNFKVVHLSQEINHLQKLFREendiNESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLeIRLNEQAEKMKGKL 1198
Cdd:TIGR00618 817 ---DILNLQCETLVQEEEQFLSRLEE----KSATLGEITHQLLK---YEECSKQLAQLTQEQAKI-IQLSDKLNGINQIK 885
|
570 580 590
....*....|....*....|....*....|
gi 2462545112 1199 EELSNQLHRSQEEEGTQRKALEAQNEIHTK 1228
Cdd:TIGR00618 886 IQFDGDALIKFLHEITLYANVRLANQSEGR 915
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
867-1064 |
1.39e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 867 LTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMD 946
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-KLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 947 NLTKQLFD---DVQKEERQRMLLE-----KSFE--LKTQDYEKQI----QSLKEEIKALKDEKMQLQHLVEGEHVTSDGL 1012
Cdd:COG3883 83 ERREELGErarALYRSGGSVSYLDvllgsESFSdfLDRLSALSKIadadADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 1013 KAEVARLSKQV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQ 1064
Cdd:COG3883 163 KAELEAAKAELeAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
914-1124 |
2.23e-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: 52.45 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 914 AKLQKHNSELETQKEQIQLKLQEKTEELKEKmdnltkqlFDDVQKEERQRMLLEKSFELKtqDYEKQIQSLKEEIKALKD 993
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEE--------LDKLAEELSARLEEVRAADEA--QLRLEFEREREEIRESYE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 994 EKMQLQhLVEGEHVTSDGLKAEVArlskqvktisefEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsydIED 1073
Cdd:pfam09731 364 EKLRTE-LERQAEAHEEHLKDVLV------------EQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKG---LEK 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 1074 VRSRLSVEDLEHLNEDgELWFAYEGLKKATRvlESHFQSQKDCYEKEIEAL 1124
Cdd:pfam09731 428 ATSSHSEVEDENRKAQ-QLWLAVEALRSTLE--DGSADSRPRPLVRELKAL 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1088 |
2.66e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLTSL----AALRAGDVEKIQKLEAELEKAatHRRNYEEKGKRYRdaVEEKLAKLQKHN 920
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELlkelEELGFESVEELEERLKELEPF--YNEYLELKDAEKE--LEREEKELKKLE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 SELETQKEQIQLKLQEkTEELKEKMDNLtKQLFDDVQKEERQRMLLEKSFELKtqdyekqiqSLKEEIKALKDEKmqlqh 1000
Cdd:PRK03918 626 EELDKAFEELAETEKR-LEELRKELEEL-EKKYSEEEYEELREEYLELSRELA---------GLRAELEELEKRR----- 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 lvegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEkhvqsqkrEMREKMSEItKQLLESYDIEDVrSRLSV 1080
Cdd:PRK03918 690 ---------EEIKKTLEKLKEELEEREKAKKELEKLEKALERVE--------ELREKVKKY-KALLKERALSKV-GEIAS 750
|
....*...
gi 2462545112 1081 EDLEHLNE 1088
Cdd:PRK03918 751 EIFEELTE 758
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
910-1257 |
2.95e-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: 52.00 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 910 EEKLAKLQKHNSELETQKEqiqlKLQEKTEELKE----------KMDNLTKQLfdDVQKEERQRmlLEKS---FELKTQD 976
Cdd:pfam05622 20 DQQVSLLQEEKNSLQQENK----KLQERLDQLESgddsgtpggkKYLLLQKQL--EQLQEENFR--LETArddYRIKCEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 977 YEKQI----------QSLKEEIKALKDEKMQLQHlvegehvTSDGLK---AEVARLSKQVKTISEFEKEIELLQ------ 1037
Cdd:pfam05622 92 LEKEVlelqhrneelTSLAEEAQALKDEMDILRE-------SSDKVKkleATVETYKKKLEDLGDLRRQVKLLEernaey 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1038 -AQKIDVEK----------HVQSQKREMRE---KMSEIT----------KQLLESYD-IEDVRSRLSVE--DLEHLNEDG 1090
Cdd:pfam05622 165 mQRTLQLEEelkkanalrgQLETYKRQVQElhgKLSEESkkadklefeyKKLEEKLEaLQKEKERLIIErdTLRETNEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1091 ELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNF-----------KVVHLSQEINHLQKLFREENDINESIRhEVTRL 1159
Cdd:pfam05622 245 RCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIreklirlqhenKMLRLGQEGSYRERLTELQQLLEDANR-RKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1160 TSENMMIpdfKQQISELEKQKQDLEIRLNEQAEK------MKGKLEELSNQLHRSQEEEGTQRKALE-----AQNEIHTK 1228
Cdd:pfam05622 324 ETQNRLA---NQRILELQQQVEELQKALQEQGSKaedsslLKQKLEEHLEKLHEAQSELQKKKEQIEelepkQDSNLAQK 400
|
410 420 430
....*....|....*....|....*....|..
gi 2462545112 1229 E---KEKLIDKIQEMQEASDHLKKQFETESEV 1257
Cdd:pfam05622 401 IdelQEALRKKDEDMKAMEERYKKYVEKAKSV 432
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
845-1006 |
3.41e-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: 51.61 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLtSLAALRAGDVEkiQKLEaELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 924
Cdd:pfam05622 305 RLTELQQLLEDANRRKNELETQN-RLANQRILELQ--QQVE-ELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 925 TQKEQI-------QLKLQEKTEELKEkmdNLTKQLFDDVQKEERQRMLLEKSFE-LKTQDyEKQIQSLKEEIKALKD--- 993
Cdd:pfam05622 381 KKKEQIeelepkqDSNLAQKIDELQE---ALRKKDEDMKAMEERYKKYVEKAKSvIKTLD-PKQNPASPPEIQALKNqll 456
|
170
....*....|...
gi 2462545112 994 EKMQLQHLVEGEH 1006
Cdd:pfam05622 457 EKDKKIEHLERDF 469
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
898-1233 |
3.54e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.68 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 898 YEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfddvqKEERQRMLleksfelktqdy 977
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRD-ELNAQVKELREEAQEL---------REKRDELN------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 978 eKQIQSLKEEIKALKDEKMQLQHLVegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQaQKIDVEKHVQSQKREMREK 1057
Cdd:COG1340 71 -EKVKELKEERDELNEKLNELREEL-------DELRKELAELNKAGGSIDKLRKEIERLE-WRQQTEVLSPEEEKELVEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1058 MSEITKQLlesydiedvrsrlsvEDLEHLNEdgelwfayegLKKATRVLESHFQSQKdcyeKEIEALNFKVVHLSQEINH 1137
Cdd:COG1340 142 IKELEKEL---------------EKAKKALE----------KNEKLKELRAELKELR----KEAEEIHKKIKELAEEAQE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1138 L----QKLFREEndinESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNqLHRSQEEEG 1213
Cdd:COG1340 193 LheemIELYKEA----DELRKEADELHKE---IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRA-LKREKEKEE 264
|
330 340
....*....|....*....|
gi 2462545112 1214 TQRKALEAQNEIhtKEKEKL 1233
Cdd:COG1340 265 LEEKAEEIFEKL--KKGEKL 282
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
826-991 |
4.60e-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: 51.60 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 826 ARRRFQSIRRFVLNiqLTYRVQRLQKKLEDQNKENHGLV-------EKLTSLAALRAGDVEKIQKLEAELEKA------- 891
Cdd:TIGR02168 808 LRAELTLLNEEAAN--LRERLESLERRIAATERRLEDLEeqieelsEDIESLAAEIEELEELIEELESELEALlnerasl 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 892 ----ATHRRNYEEKGKRYRDaVEEKLAKLQKHNSELETQKEQIQLKLQekteELKEKMDNLTKQLFDDVQKEERQRMLLE 967
Cdd:TIGR02168 886 eealALLRSELEELSEELRE-LESKRSELRRELEELREKLAQLELRLE----GLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
170 180
....*....|....*....|....
gi 2462545112 968 KSFELKTQDYEKQIQSLKEEIKAL 991
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
976-1244 |
5.25e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 976 DYEKQIQSLKEEIKALKDEKMQLQHLVEgehvtsdGLKAEVARLSKQVKTISEfekeiellQAQKIdvekhvQSQKREMR 1055
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELK-------ELAEKRDELNAQVKELRE--------EAQEL------REKRDELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1056 EKMSEITKQLLESYD-IEDVRSRLSV--EDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYEKEIEALNfKVVHLS 1132
Cdd:COG1340 71 EKVKELKEERDELNEkLNELREELDElrKELAELNKAGG---SIDKLRKEIERLEWRQQTEVLSPEEEKELVE-KIKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1133 QEINHLQKlfreENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQ---DLEIRLNEQAEKMKGKLEELSNQLHRSQ 1209
Cdd:COG1340 147 KELEKAKK----ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQelhEEMIELYKEADELRKEADELHKEIVEAQ 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462545112 1210 EEEGTQRKAL-EAQNEIHtkEKEKLIDKIQEMQEAS 1244
Cdd:COG1340 223 EKADELHEEIiELQKELR--ELRKELKKLRKKQRAL 256
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
570-607 |
6.76e-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: 48.11 E-value: 6.76e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2462545112 570 VYDMLVEILRASKFRSSLYLLMETLNATTPHYVRCIKP 607
Cdd:cd01363 133 FIEILLDIAGFEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
870-1065 |
6.79e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 870 LAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQL------KLQEKTEELKE 943
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelaALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 944 KMDNLTKQLfdDVQKEERQRMLLeKSFELKTQDYEKQIQSLKEEIKALKDEKMqLQHLVEGEHVTSDGLKAEVARLSKQV 1023
Cdd:COG4942 91 EIAELRAEL--EAQKEELAELLR-ALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462545112 1024 KTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQL 1065
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1329 |
6.82e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLTSL------AALRAGDV-EKIQKLEAELEKAATH----------------------- 894
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELlveqgrLQLQADRHqEHIRARDSLIQSLATRleldgfergpfserqiknfhtlv 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 895 RRNYEEKGK---RYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFE 971
Cdd:TIGR00606 400 IERQEDEAKtaaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 972 LKTQDYE-------KQIQSLKEEIKALKDEKMQLqhlvegehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVE 1044
Cdd:TIGR00606 480 LRKAERElskaeknSLTETLKKEVKSLQNEKADL-----------DRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1045 KHVQSQKREMREKMSEI------TKQLLESYDIEDVRSRLSVEDLEHLNEDGElwfAYEGLKKATRVLESHFQSQKDCYE 1118
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA---SLEQNKNHINNELESKEEQLSSYE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1119 KEI------EALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAE 1192
Cdd:TIGR00606 626 DKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLR 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1193 KMKGKLEELSNQLHRSQEE-EGTQRKALEAQNEIHTKEKEklidkIQEMQEASDHLKKQFEtesEVKCNFRQEASRLTLE 1271
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRrDEMLGLAPGRQSIIDLKEKE-----IPELRNKLQKVNRDIQ---RLKNDIEEQETLLGTI 777
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 1272 NRDLE--EELDMKDRVIKKLQDQVKTLSKTIGK-ANDVHSSSGPKEYLGMLQYKREDEAKL 1329
Cdd:TIGR00606 778 MPEEEsaKVCLTDVTIMERFQMELKDVERKIAQqAAKLQGSDLDRTVQQVNQEKQEKQHEL 838
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
880-1290 |
9.90e-06 |
|
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: 50.59 E-value: 9.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 880 KIQKLEAELEKAATHR----------RNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLT 949
Cdd:pfam10174 290 KIDQLKQELSKKESELlalqtkletlTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 950 -------------KQLFDDVQKEERQRMLLEKSFE-LKTQ--DYEKQIQSLKEEIKALkdekmqlqhlvEGEHVTSDglk 1013
Cdd:pfam10174 370 dlteekstlageiRDLKDMLDVKERKINVLQKKIEnLQEQlrDKDKQLAGLKERVKSL-----------QTDSSNTD--- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1014 aevARLSKQVKTISEFEKEIELLQAQKidvekhvqsqKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELW 1093
Cdd:pfam10174 436 ---TALTTLEEALSEKERIIERLKEQR----------EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLK 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1094 -----FAYEGLKKatrvlESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDINESIRH---EVTRLTSENMm 1165
Cdd:pfam10174 503 ehassLASSGLKK-----DSKLKSLEIAVEQKKEECS-KLENQLKKAHNAEEAVRTNPEINDRIRLleqEVARYKEESG- 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1166 ipdfKQQiSELEKQKQDLEIRLNEQAEKMK--GKLEELSNQLHRSQEEEGTQRKALeaQNEIHTKEKEKLID-KIQEMQE 1242
Cdd:pfam10174 576 ----KAQ-AEVERLLGILREVENEKNDKDKkiAELESLTLRQMKEQNKKVANIKHG--QQEMKKKGAQLLEEaRRREDNL 648
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2462545112 1243 ASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQ 1290
Cdd:pfam10174 649 ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR 696
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1118-1252 |
9.94e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1118 EKEIEALNFKVVHLSQEINHLQKLFRE-ENDInESIRHEVTRLTSENMMIPDFKQ------QISELEKQKQDLE---IRL 1187
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRlELEI-EEVEARIKKYEEQLGNVRNNKEyealqkEIESLKRRISDLEdeiLEL 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545112 1188 NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEA-SDHLKKQFE 1252
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKiPPELLALYE 181
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1133-1300 |
1.04e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1133 QEINHLQKLFREENDINEsIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQ 1209
Cdd:COG1579 4 EDLRALLDLQELDSELDR-LEHRLKELPAE---LAELEDELAALEARLEAAKTELEDlekEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1210 EEEGTQR-----KALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQF-ETESEVKcnfrQEASRLTLENRDLEEELDMKD 1283
Cdd:COG1579 80 EQLGNVRnnkeyEALQKEIESLKRRISDLEDEILELMERIEELEEELaELEAELA----ELEAELEEKKAELDEELAELE 155
|
170
....*....|....*..
gi 2462545112 1284 RVIKKLQDQVKTLSKTI 1300
Cdd:COG1579 156 AELEELEAEREELAAKI 172
|
|
| Myo5p-like_CBD_Rasip1 |
cd15472 |
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ... |
1351-1630 |
1.15e-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: 49.58 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1351 PAHILFMCVRYADS-----------LNDANMLKSLMNSTINGIKQVVKEHLE--------------DFEMLSFWLSNT-- 1403
Cdd:cd15472 25 PAFLLCLCIQHSAThfepghfgkllLKIAKRIQEIVWEKTKELAEKQPEHQDpaslsllsiaelapDLQPLLFWMSNSie 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1404 --CHFLNCLKQYSGE-EEFMKHNSPQQNKNCLNNfDLSEYRQILSDVAIRIYHQFIIIMEKNIQPIIvPGMLE------- 1473
Cdd:cd15472 105 llYFIQQKVPLYEQSmEEELDVGSKESLLSSTLT-ASEEAMTVLEEVIMYTFQQCVYYLTKTLYVAL-PALLDsnpftae 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1474 -YESLQGISGLkPTGFRKrsssiddtdgytMTSVLQ---QLsyfyTTMCQngLDPELVRQAVKQLFFLIGAVTLNSLFLR 1549
Cdd:cd15472 183 eRESWSGGSRL-PEGVRR------------VLEIYQatlDL----LRQYQ--VHPEIASQMFAYLFFFSNASLFNQLMEK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1550 KDMCSC---RKGMQIRCNISYLEEWLKDKNLqNSLAKETLEPLSQAAWLLQVKKTT--DSDAKEIYERCTSLSAVQIIKI 1624
Cdd:cd15472 244 GSGGGFfqwSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQllQMSWSSLRAEFPALNPAQLHHL 322
|
....*.
gi 2462545112 1625 LNSYTP 1630
Cdd:cd15472 323 LRQYQL 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
843-1057 |
1.17e-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: 49.76 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 843 TYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSE 922
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 923 LETQKEQI--QLKLQEKTEELKEKMDNLTKQLFDDVQKeeRQRMLLEKSFELKTQDYE-----KQIQSLKEEIKALKDEK 995
Cdd:COG4942 99 LEAQKEELaeLLRALYRLGRQPPLALLLSPEDFLDAVR--RLQYLKYLAPARREQAEElradlAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 996 MQLQHLVEGEHVTSDGLKAEVARLSKQV-KTISEFEKEIELLQAQKIDVEKHVQSQKREMREK 1057
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
836-999 |
1.18e-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: 49.42 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 836 FVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYeEKGKRYRDAVEEKLAK 915
Cdd:pfam15905 176 MAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQV-EKYKLDIAQLEELLKE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 916 LQKHNSELetqkeqiQLKLQEKTEELKEKMDNLTKQLfdDVQKEERQRMLLEksFELKTQDYEKQIQSLKEEIKALKDEK 995
Cdd:pfam15905 255 KNDEIESL-------KQSLEEKEQELSKQIKDLNEKC--KLLESEKEELLRE--YEEKEQTLNAELEELKEKLTLEEQEH 323
|
....
gi 2462545112 996 MQLQ 999
Cdd:pfam15905 324 QKLQ 327
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1064 |
1.38e-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: 50.07 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLTSLAAlragDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE 924
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 925 TQKEQIQLK---LQEKTEELKEKMDNLTKQLfddVQKEERQRMLLEKSFELKTQDYE--KQIQSLKEEIKALKDEKMQLQ 999
Cdd:TIGR02169 868 EELEELEAAlrdLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKRKRLSElkAKLEALEEELSEIEDPKGEDE 944
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545112 1000 HLVEGEHVTSDgLKAEVARLSKQV--------KTISEFEkeiELLQAQKIDVEKH--VQSQKREMREKMSEITKQ 1064
Cdd:TIGR02169 945 EIPEEELSLED-VQAELQRVEEEIralepvnmLAIQEYE---EVLKRLDELKEKRakLEEERKAILERIEEYEKK 1015
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
973-1244 |
1.64e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 973 KTQDYEKQIQSLKEEIKALKDEKMQLQhlvEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKR 1052
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALK---KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1053 EMREKMSEITKQLLESYDIEDvRSRLsvedlehlnedgELWFAYEGLKKATRVLEshfqsqkdcYEKEIEAlnfkvvHLS 1132
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGR-QPPL------------ALLLSPEDFLDAVRRLQ---------YLKYLAP------ARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1133 QEINHLQKLFREENDINESIRHEVTRLtsenmmipdfKQQISELEKQKQDLEIRLNEQaekmkgklEELSNQLHRSQEEE 1212
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAEL----------EALLAELEEERAALEALKAER--------QKLLARLEKELAEL 211
|
250 260 270
....*....|....*....|....*....|..
gi 2462545112 1213 GTQRKALEAQNEIHTKEKEKLIDKIQEMQEAS 1244
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
833-1152 |
1.66e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 833 IRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEK 912
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 913 LAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKSFELKtqdyEKQIQSLKEEIKALK 992
Cdd:COG4372 93 QAELAQAQEELESLQEEAE-ELQEELEELQKERQDLEQQR----KQLEAQIAELQSEIAER----EEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 993 DEKMQLQhlVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQaQKIDVEKHVQSQKREMREKMSEITKQLLESYDIE 1072
Cdd:COG4372 164 EELAALE--QELQALSEAEAEQALDELLKEANRNAEKEEELAEAE-KLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1073 DVRsrlSVEDLEHLNEDGELWFAYEGLKKATRVLESHfqsqkdcyEKEIEALNFKVVHLSQEINHLQKLFREENDINESI 1152
Cdd:COG4372 241 ALE---LEEDKEELLEEVILKEIEELELAILVEKDTE--------EEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
871-1032 |
2.17e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 871 AALRAGDVEKIQKLEAELEKAATH-RRNYEEKGKRYRDaVEEKLAKLQKHNSELEtqkeqiqlklqEKTEELKEKMDNLT 949
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHeERELTEEEEEIRR-LEEQVERLEAEVEELE-----------AELEEKDERIERLE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 950 KQLfDDVQKEERQRMLLEKsfELKTQDYE-----KQIQSLKEEIKALKDEKMQLQHLVEGEHvtSDGLKAevarlskqVK 1024
Cdd:COG2433 448 REL-SEARSEERREIRKDR--EISRLDREierleRELEEERERIEELKRKLERLKELWKLEH--SGELVP--------VK 514
|
....*...
gi 2462545112 1025 TISEFEKE 1032
Cdd:COG2433 515 VVEKFTKE 522
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
912-1102 |
2.22e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 912 KLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKqLFDDVQKEERQRmlleKSFELKTQDYEKQIQSLKEEIKAL 991
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEA-AKTELEDLEKEI----KRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 992 KDEK--MQLQHLVEgehvtsdGLKAEVARLSKQvktISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLEsy 1069
Cdd:COG1579 86 RNNKeyEALQKEIE-------SLKRRISDLEDE---ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE-- 153
|
170 180 190
....*....|....*....|....*....|....
gi 2462545112 1070 dIEDVRSRLSVEDLEHLNE-DGELWFAYEGLKKA 1102
Cdd:COG1579 154 -LEAELEELEAEREELAAKiPPELLALYERIRKR 186
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
956-1297 |
2.67e-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: 49.05 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 956 VQKEERQRMLLEKSFELKTQDYEKQ----IQSLKEEIKALKDekmqLQHLVEGEHVTSDGLKAE---VARLSKQ--VKTI 1026
Cdd:pfam10174 47 LRKEEAARISVLKEQYRVTQEENQHlqltIQALQDELRAQRD----LNQLLQQDFTTSPVDGEDkfsTPELTEEnfRRLQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1027 SEFE---KEIELLQAQKIDVEKHVQSQKREMrEKMSEITKQLLE----------SYDIEDVRSRLSVEDLEHLNE-DGEL 1092
Cdd:pfam10174 123 SEHErqaKELFLLRKTLEEMELRIETQKQTL-GARDESIKKLLEmlqskglpkkSGEEDWERTRRIAEAEMQLGHlEVLL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1093 WFAYEGLKKATRVLESHFQSQKD-----CYEKEIEALNFKVVHLSQEINHLQ---KLFREENDINESIRH------EVTR 1158
Cdd:pfam10174 202 DQKEKENIHLREELHRRNQLQPDpaktkALQTVIEMKDTKISSLERNIRDLEdevQMLKTNGLLHTEDREeeikqmEVYK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1159 LTSENMmipdfKQQISELekqKQDLEiRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNE---IHTKEKEKLID 1235
Cdd:pfam10174 282 SHSKFM-----KNKIDQL---KQELS-KKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQraaILQTEVDALRL 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545112 1236 KIQEMQEASDHLKKQFETESEvkcnfrqEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLS 1297
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
810-1279 |
3.37e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 810 EEHKAVILQKYARAWLARRRFQSIRRFvlniqltYRVQRlQKKLEDQNKENHGLVEKLTSLAAlragDVEKIQKLEAELE 889
Cdd:PRK04863 753 EELEKAVVVKIADRQWRYSRFPEVPLF-------GRAAR-EKRIEQLRAEREELAERYATLSF----DVQKLQRLHQAFS 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 890 K-AATHRrnyeekgkryrdAV------EEKLAKLQKHNSELETQKEQiqlkLQEKTEELKEKMDNLtKQLFDDVQKEERQ 962
Cdd:PRK04863 821 RfIGSHL------------AVafeadpEAELRQLNRRRVELERALAD----HESQEQQQRSQLEQA-KEGLSALNRLLPR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 963 RMLLEKsfelktQDYEKQIQSLKEEIKALKDEKMQL-QHlvegehvtsdglKAEVARLSKQVKTISEFEKEIELLQAQki 1041
Cdd:PRK04863 884 LNLLAD------ETLADRVEEIREQLDEAEEAKRFVqQH------------GNALAQLEPIVSVLQSDPEQFEQLKQD-- 943
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1042 dvekHVQSQKREMREKMseitkqllESYDIEDVRSRlsvedLEHlnedgelwFAYEglkkatrvleshfQSQKDCYEKei 1121
Cdd:PRK04863 944 ----YQQAQQTQRDAKQ--------QAFALTEVVQR-----RAH--------FSYE-------------DAAEMLAKN-- 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1122 EALNFKvvhLSQEINHLQklfREENDINESIRHEVTRLTSENMMIPDFK-------QQISELEKQKQDLEIRLNEQAE-K 1193
Cdd:PRK04863 984 SDLNEK---LRQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKssydakrQMLQELKQELQDLGVPADSGAEeR 1057
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1194 MKGKLEELSNQLHRSQeeegTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENR 1273
Cdd:PRK04863 1058 ARARRDELHARLSANR----SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERR 1133
|
....*.
gi 2462545112 1274 DLEEEL 1279
Cdd:PRK04863 1134 LHRREL 1139
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
833-990 |
3.41e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 833 IRRFVLNIQLTYRVQRLQKKLEDQNKEnhglVEKLTSLAALRAGdvEKIQKLEAELEKAATHRRNY----EEKGKRYRDA 908
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKE----AEAIKKEALLEAK--EEIHKLRNEFEKELRERRNElqklEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 909 VEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLtkqlfddvQKEERQRmlLEKSFELkTQDYEKQI--QSLKE 986
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELE-QKQQELEKKEEELEEL--------IEEQLQE--LERISGL-TAEEAKEIllEKVEE 165
|
....
gi 2462545112 987 EIKA 990
Cdd:PRK12704 166 EARH 169
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
915-1231 |
3.59e-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: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 915 KLQKHNSELETQKEQIQLKLQE-KTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKD 993
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKvQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 994 EKMQLqHLVEGEHVTSDGLKAEVARLSKQVKTIseFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLlESYDIEd 1073
Cdd:TIGR00606 260 NLSKI-MKLDNEIKALKSRKKQMEKDNSELELK--MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQREL-EKLNKE- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1074 vRSRLSVEDLEHLNEDGELWFAYE-----GLKKATRVLESHFQSQKDCYEKEIEAlnfkvvhlSQEINHLQKLFRE-END 1147
Cdd:TIGR00606 335 -RRLLNQEKTELLVEQGRLQLQADrhqehIRARDSLIQSLATRLELDGFERGPFS--------ERQIKNFHTLVIErQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1148 INESIRHEVTRLTSENMMIpdfKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHT 1227
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482
|
....
gi 2462545112 1228 KEKE 1231
Cdd:TIGR00606 483 AERE 486
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
980-1296 |
3.78e-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: 48.68 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 980 QIQSLKEEIKALKDEKMQLQHLvegeHVtsdGLKAEVARLSKQVKTISEFEKEIELLQAQKIDvekhvqsqkrEMREKMS 1059
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHL----HF---GYKSDETLIASRQEERQETSAELNQLLRTLDD----------QWKEKRD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1060 EITKQL-LESYDIEDVRSRLSVEDLEHLNedgelwFAYEGLKKATRVLES--HFQSQKDCYEKEIEALNFKVVHLSQEIN 1136
Cdd:pfam12128 305 ELNGELsAADAAVAKDRSELEALEDQHGA------FLDADIETAAADQEQlpSWQSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1137 HLQKLFREEN-----DINE---SIRHEVTRLTSENMmiPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRS 1208
Cdd:pfam12128 379 RRRSKIKEQNnrdiaGIKDklaKIREARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQA 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1209 Q--EEEGTQRKAleaqneihtkeKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEAS-RLTLENRDLEEELDMKDRV 1285
Cdd:pfam12128 457 TatPELLLQLEN-----------FDERIERAREEQEAANAEVERLQSELRQARKRRDQASeALRQASRRLEERQSALDEL 525
|
330
....*....|.
gi 2462545112 1286 IKKLQDQVKTL 1296
Cdd:pfam12128 526 ELQLFPQAGTL 536
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
942-1211 |
4.18e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 942 KEKMDNLTKQL---FDDVQKEERQRMLLEKSFELKTQD-----------YEKQIQSLKEEIKALKDEKMQLQhlvegehV 1007
Cdd:pfam00038 3 KEQLQELNDRLasyIDKVRFLEQQNKLLETKISELRQKkgaepsrlyslYEKEIEDLRRQLDTLTVERARLQ-------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1008 TSDGLKAEVARLSKQVKT-----------ISEFEKEIELLQAQKIDVEKHVQS-------QKREMREKMSEITKQLLESY 1069
Cdd:pfam00038 76 ELDNLRLAAEDFRQKYEDelnlrtsaendLVGLRKDLDEATLARVDLEAKIESlkeelafLKKNHEEEVRELQAQVSDTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1070 DIEDVRSRLSVEdlehlnedgelwfayegLKKATRVLESHFQSQKDCYEKEIEAL-NFKVVHLSQEIN-HLQKLFREEND 1147
Cdd:pfam00038 156 VNVEMDAARKLD-----------------LTSALAEIRAQYEEIAAKNREEAEEWyQSKLEELQQAAArNGDALRSAKEE 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 1148 INESiRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEE 1211
Cdd:pfam00038 219 ITEL-RRTIQSLEIE---LQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQE 278
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1009-1250 |
4.22e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1009 SDGLKAEVARLSKQVKTISEFEKEIELLQAQKidveKHVQSQKREMREKMSEITKQL--LESyDIEDVRSRLSVedlehl 1086
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEE----KALLKQLAALERRIAALARRIraLEQ-ELAALEAELAE------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1087 nedgelwfayegLKKATRVLESHFQSQKDCYEKEIEALnfkvvHLSQEINHLQKLFREEnDINESIRhevtRLTSENMMI 1166
Cdd:COG4942 88 ------------LEKEIAELRAELEAQKEELAELLRAL-----YRLGRQPPLALLLSPE-DFLDAVR----RLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1167 PDFKQQISELEKQKQDLEiRLNEQAEKMKGKLEELsnqlhrsQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDH 1246
Cdd:COG4942 146 PARREQAEELRADLAELA-ALRAELEAERAELEAL-------LAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
....
gi 2462545112 1247 LKKQ 1250
Cdd:COG4942 218 LQQE 221
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1175-1294 |
4.32e-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: 44.52 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1175 ELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEaqneihtkEKEKLIDKIQEMQEASDHLKKQFETE 1254
Cdd:pfam20492 3 EAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEE--------EAERLEQKRQEAEEEKERLEESAEME 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2462545112 1255 SEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVK 1294
Cdd:pfam20492 75 AEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELE 114
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
841-1040 |
5.33e-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: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKH- 919
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 920 ---------NSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvQKEERQRMLLEKsfelKTQDYEKQIQSLKEEIKA 990
Cdd:COG4942 118 rqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEA----ERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462545112 991 LKDEKMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQK 1040
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1150-1325 |
5.83e-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: 48.14 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1150 ESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKE 1229
Cdd:TIGR02169 240 EAIERQLASLEEE---LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1230 KEKLIDKIQEMQEASDHLKKQFEtesevkcNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSS 1309
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIE-------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170
....*....|....*.
gi 2462545112 1310 SgpKEYLGMLQYKRED 1325
Cdd:TIGR02169 390 Y--REKLEKLKREINE 403
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
839-1065 |
6.26e-05 |
|
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: 46.27 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 839 NIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLaalragdvekiqKLEAELEKAATHRrnyeeKGKRYRDaVEEKLAKLQK 918
Cdd:pfam17078 19 NLQLTVQSQNLLSKLEIAQQKESKFLENLASL------------KHENDNLSSMLNR-----KERRLKD-LEDQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 919 HNSELETQKEQIQLKLQEKTE---ELKEKMDNLTKQLFDDVQKEERQRmlleksfelktQDYEKQIQSLKEEIKALK-DE 994
Cdd:pfam17078 81 SYEELTESNKQLKKRLENSSAsetTLEAELERLQIQYDALVDSQNEYK-----------DHYQQEINTLQESLEDLKlEN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545112 995 KMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKE--IELLQ-----AQKIDVEKHVQSQKrEMREKMSEITKQL 1065
Cdd:pfam17078 150 EKQLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNknNKLLTkldslAQLLDLPSWLNLYP-ESRNKILEYAEKM 226
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
878-1055 |
6.56e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 878 VEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKhnsELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvq 957
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQAIKEAKKEADEIIKEL----- 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 958 keerQRMLLEKSFELKTQDYEKQIQSLKEEIKAL---KDEKMQLQH-LVEGEHV--TSDGLKAEVARLSKQVKTISEF-- 1029
Cdd:PRK00409 594 ----RQLQKGGYASVKAHELIEARKRLNKANEKKekkKKKQKEKQEeLKVGDEVkyLSLGQKGEVLSIPDDKEAIVQAgi 669
|
170 180 190
....*....|....*....|....*....|..
gi 2462545112 1030 ------EKEIELLQAQKIDVEKHVQSQKREMR 1055
Cdd:PRK00409 670 mkmkvpLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
915-1298 |
7.23e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.52 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 915 KLQKHNSELETQKEQI-------------QLKL----QEKTEELKEKMDNLTKQLFDDVQKE--------ERQRML---- 965
Cdd:PRK04778 26 RNYKRIDELEERKQELenlpvndelekvkKLNLtgqsEEKFEEWRQKWDEIVTNSLPDIEEQlfeaeelnDKFRFRkakh 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 966 LEKSFELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKAEVarLSKQVK---TISEFEKEIELLQAQ--- 1039
Cdd:PRK04778 106 EINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL--LANRFSfgpALDELEKQLENLEEEfsq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1040 ---------KIDVEKHVQSQKREM---REKMSEItKQLLESY---------DIEDVRSRLSVE--DLEHLNEDGELwfay 1096
Cdd:PRK04778 184 fveltesgdYVEAREILDQLEEELaalEQIMEEI-PELLKELqtelpdqlqELKAGYRELVEEgyHLDHLDIEKEI---- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1097 EGLKKATRvleshfQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDinesIRHEVTRLtsenmmIPDFKQQISEL 1176
Cdd:PRK04778 259 QDLKEQID------ENLALLEELDLDEAEEKNEEIQERIDQLYDILEREVK----ARKYVEKN------SDTLPDFLEHA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1177 EKQKQDLEI---------RLN----EQAEKMKGKLEELSNQLHRSQEEEGTQRKAL-EAQNEIhtKEKEKLIDKIQEMQ- 1241
Cdd:PRK04778 323 KEQNKELKEeidrvkqsyTLNeselESVRQLEKQLESLEKQYDEITERIAEQEIAYsELQEEL--EEILKQLEEIEKEQe 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545112 1242 EASDHLKKQFETESEVKCN---FRQEAS--RLTLENRDL----EEELDMKDRVIKKLQDQVKTLSK 1298
Cdd:PRK04778 401 KLSEMLQGLRKDELEAREKlerYRNKLHeiKRYLEKSNLpglpEDYLEMFFEVSDEIEALAEELEE 466
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
800-1333 |
7.52e-05 |
|
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: 47.66 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 800 LARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAalragdvE 879
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS-------K 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 880 KIQKLEAE-----------------------------LEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQI 930
Cdd:pfam02463 258 QEIEKEEEklaqvlkenkeeekekklqeeelkllakeEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 931 QLKLQEKTE--ELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQdYEKQIQSLKEEIKALKDEKMQ----LQHLVEG 1004
Cdd:pfam02463 338 EELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE-RLSSAAKLKEEELELKSEEEKeaqlLLELARQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1005 EHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKmseITKQLLESYDIEDVRSRLSVEDLE 1084
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK---SEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1085 HLNEDGELWFAYEGLKKATRVLESHFQSQKDCYE------KEIEALNFKVVHLS----------QEINHLQKLFREENDI 1148
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGGRIISAhgrlgdLGVAVENYKVAISTavivevsataDEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1149 NESIRHEVTRLTSENM-----MIPDFKQQISELEKQKQDLEIRLNEQAEK---MKGKLEELSNQLHRSQEEEGTQRKALE 1220
Cdd:pfam02463 574 PLGARKLRLLIPKLKLplksiAVLEIDPILNLAQLDKATLEADEDDKRAKvveGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1221 AQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL---- 1296
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEaqdk 733
|
570 580 590
....*....|....*....|....*....|....*..
gi 2462545112 1297 SKTIGKANDVHSSSGPKEYLGMLQYKREDEAKLIQNL 1333
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1047-1291 |
9.82e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1047 VQSQKREMREKMSEITKQL--LESYDIEDV----RSRLS--VEDLEHLNEDGElwFAYEGLKKATRVLESHFQSQK--DC 1116
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIeeKEEKDLHERlnglESELAelDEEIERYEEQRE--QARETRDEADEVLEEHEERREelET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1117 YEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSE----NMMIPDFKQQISELEKQKQDLEIRL----- 1187
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagldDADAEAVEARREELEDRDEELRDRLeecrv 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1188 -----NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKL--IDK-IQEMQEASDHLKKQFETESEVKC 1259
Cdd:PRK02224 336 aaqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIeeLEEeIEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270
....*....|....*....|....*....|..
gi 2462545112 1260 NFRQEASRLTLENRDLEEELDMKDRVIKKLQD 1291
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
933-1307 |
1.36e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 933 KLQEKTEELKEKMDNLTKQLFD-DVQKEERQRMLLE--------KSFELKTQDYEKQIQSLKEEIKALKDEKmqlqhlve 1003
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNiDYLEEKLKSSNLElenikkqiADDEKSHSITLKEIERLSIEYNNAMDDY-------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1004 gehvtsDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV----QSQKREMR-------EKMSEITKQLLESYDIE 1072
Cdd:PRK01156 235 ------NNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNnyykELEERHMKiindpvyKNRNYINDYFKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1073 DVRSRLSvedlehlNEDGELWFAYEGLKKATrVLESHF------QSQKDCYEKEIEAL---NFKVVHLSQEINHLQKLFR 1143
Cdd:PRK01156 309 NKKQILS-------NIDAEINKYHAIIKKLS-VLQKDYndyikkKSRYDDLNNQILELegyEMDYNSYLKSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1144 EENDINESIRHEVTRLTSENMMIPD-FKQQISELEKQKQDLEIR---LNEQAEKMKGKLEELSnqlhRSQEEEGTQRKAL 1219
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDaIKKELNEINVKLQDISSKvssLNQRIRALRENLDELS----RNMEMLNGQSVCP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1220 EAQNEIHTKEKEKLIDKIQEmqEASDHLKKQFETESEVKC---NFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL 1296
Cdd:PRK01156 457 VCGTTLGEEKSNHIINHYNE--KKSRLEEKIREIEIEVKDideKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDI 534
|
410
....*....|.
gi 2462545112 1297 SKTIGKANDVH 1307
Cdd:PRK01156 535 KIKINELKDKH 545
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1284 |
1.53e-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: 46.71 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 848 RLQKKLEDqnkenhgLVEKLTSLAALrAGDVEKIQK----LEAElEKAATHRrNYEEKGKRYRDAvEEKLAKLQKHNSEL 923
Cdd:pfam01576 577 RLQQELDD-------LLVDLDHQRQL-VSNLEKKQKkfdqMLAE-EKAISAR-YAEERDRAEAEA-REKETRALSLARAL 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 924 ETQKEQIQlKLQEKTEELKEKMDNLTKQLfDDVQKE----ERQRMLLEKSF-ELKTQdyekqIQSLKEEIKALKDEKMQL 998
Cdd:pfam01576 646 EEALEAKE-ELERTNKQLRAEMEDLVSSK-DDVGKNvhelERSKRALEQQVeEMKTQ-----LEELEDELQATEDAKLRL 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 999 QhlvegehVTSDGLKAEvarlskqvktiseFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQL---------LESy 1069
Cdd:pfam01576 719 E-------VNMQALKAQ-------------FERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRaqavaakkkLEL- 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1070 DIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCY------EKEIEALNFKVVHLSQEINHLQKLFR 1143
Cdd:pfam01576 778 DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILaqskesEKKLKNLEAELLQLQEDLAASERARR 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1144 EENDINESIRHEVTRLTSENMMIPDFKQQI--------SELEKQKQDLEIrLNEQAEKMKGKLEELSNQL----HRSQEE 1211
Cdd:pfam01576 858 QAQQERDELADEIASGASGKSALQDEKRRLeariaqleEELEEEQSNTEL-LNDRLRKSTLQVEQLTTELaaerSTSQKS 936
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 1212 EGTqRKALEAQNeihtkeKEkLIDKIQEMqeasdhlkkqfetESEVKCNFRQEASRLTLENRDLEEELDMKDR 1284
Cdd:pfam01576 937 ESA-RQQLERQN------KE-LKAKLQEM-------------EGTVKSKFKSSIAALEAKIAQLEEQLEQESR 988
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
911-1040 |
2.13e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 911 EKLAK--LQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK--------- 979
Cdd:PRK12704 37 EEEAKriLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKreeelekke 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545112 980 -QIQSLKEEIKALKDE--KMQLQHLVEGEHVTsdGLKAEVAR--LSKQVK---------TISEFEKEIElLQAQK 1040
Cdd:PRK12704 117 kELEQKQQELEKKEEEleELIEEQLQELERIS--GLTAEEAKeiLLEKVEeearheaavLIKEIEEEAK-EEADK 188
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
879-1070 |
2.21e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 879 EKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQlKLQEKTEELKEKMDNLTKQL----FD 954
Cdd:COG1340 29 EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD-ELNEKLNELREELDELRKELaelnKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 955 DVQKEERQRML--LEKSFELKTQDYEK------QIQSLKEEIKALKDEKMQLQHLVEgehvtsdgLKAEVARLSKQVkti 1026
Cdd:COG1340 108 GGSIDKLRKEIerLEWRQQTEVLSPEEekelveKIKELEKELEKAKKALEKNEKLKE--------LRAELKELRKEA--- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462545112 1027 SEFEKEIELL--QAQKIDVEKHVQSQKR-EMREKMSEITKQLLESYD 1070
Cdd:COG1340 177 EEIHKKIKELaeEAQELHEEMIELYKEAdELRKEADELHKEIVEAQE 223
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
858-1067 |
2.41e-04 |
|
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: 45.44 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 858 KENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAatHRRNYEEKGKRYRDAVEEKLAKLQKHNSELET--QKEQIQLKLQ 935
Cdd:pfam15742 107 KSQNSLQEKLAQEKSRVADAEEKILELQQKLEHA--HKVCLTDTCILEKKQLEERIKEASENEAKLKQqyQEEQQKRKLL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 936 EKT-EELKEKMDNL----------TKQLFDDVQKEERQRMLLEKsfELKTQD-YEKQIQSLKEEIKALKDEK----MQLQ 999
Cdd:pfam15742 185 DQNvNELQQQVRSLqdkeaqlemtNSQQQLRIQQQEAQLKQLEN--EKRKSDeHLKSNQELSEKLSSLQQEKealqEELQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1000 HLVE--GEHVTS-----DGLKAEVAR----LSKQV----KTISEFEKEIELLQaQKIDVEKHVQSQKREMREKMSEITKQ 1064
Cdd:pfam15742 263 QVLKqlDVHVRKynekhHHHKAKLRRakdrLVHEVeqrdERIKQLENEIGILQ-QQSEKEKAFQKQVTAQNEILLLEKRK 341
|
...
gi 2462545112 1065 LLE 1067
Cdd:pfam15742 342 LLE 344
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
887-1280 |
2.72e-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: 45.94 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 887 ELEKAathRRNYEEKGKRYRDAVEEKLAKLQ-----KHNSELETQ--KEQIQLKLQEKTEELKEKMDNLTKQLFD---DV 956
Cdd:pfam01576 682 ELERS---KRALEQQVEEMKTQLEELEDELQatedaKLRLEVNMQalKAQFERDLQARDEQGEEKRRQLVKQVREleaEL 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 957 QKEERQRMLL---EKSFELKTQDYEKQIQSL----KEEIKALKDEKMQLQHL---VEGEHVTSDGLKAEVARLSKQVKTI 1026
Cdd:pfam01576 759 EDERKQRAQAvaaKKKLELDLKELEAQIDAAnkgrEEAVKQLKKLQAQMKDLqreLEEARASRDEILAQSKESEKKLKNL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1027 sefekEIELLQAQKI-----DVEKHVQSQKREMREkmsEITKQLLESYDIEDVRSRLS--VEDLEHLNEDgelwfayegl 1099
Cdd:pfam01576 839 -----EAELLQLQEDlaaseRARRQAQQERDELAD---EIASGASGKSALQDEKRRLEarIAQLEEELEE---------- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1100 kkatrvLESHFQSQKDCYEK---EIEALNfkvVHLSQEINHLQKlfreendiNESIRhevtrltsenmmipdfkqqiSEL 1176
Cdd:pfam01576 901 ------EQSNTELLNDRLRKstlQVEQLT---TELAAERSTSQK--------SESAR--------------------QQL 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1177 EKQKQDLEIRLNEQAEKMKGK-------LEELSNQLHRSQEEEGTQRKAleAQNEIHTKEK--EKLIDKIQEMQEASDHL 1247
Cdd:pfam01576 944 ERQNKELKAKLQEMEGTVKSKfkssiaaLEAKIAQLEEQLEQESRERQA--ANKLVRRTEKklKEVLLQVEDERRHADQY 1021
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2462545112 1248 KKQFE-TESEVKCNFRQ------EASRLTLENRDLEEELD 1280
Cdd:pfam01576 1022 KDQAEkGNSRMKQLKRQleeaeeEASRANAARRKLQRELD 1061
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1166-1244 |
2.79e-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: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1166 IPDFKQQISELEKQKQDLE---IRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1242
Cdd:COG3883 18 IQAKQKELSELQAELEAAQaelDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
..
gi 2462545112 1243 AS 1244
Cdd:COG3883 98 SG 99
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
882-985 |
2.98e-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: 44.88 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 882 QKLEAELEKAATHRRnyEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEer 961
Cdd:cd16269 192 ALTEKEKEIEAERAK--AEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKE-- 267
|
90 100
....*....|....*....|....
gi 2462545112 962 QRMLLEKSFELKTQDYEKQIQSLK 985
Cdd:cd16269 268 QEALLEEGFKEQAELLQEEIRSLK 291
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
841-1084 |
3.53e-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: 45.42 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEE------KLA 914
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLE 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 915 KLQKHNSELETQKEQIQLKLQEKTEELKEKMDNL---TKQLFDDVQ---------KE-------------ERQRMLLEKS 969
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQdgkddylkqKEtelntvnaqleecEKHQEKINED 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 970 FELKTQDYEKQIQS------------LKEEIKALKDEKMQLQHLVEGEHVTSdgLKAEVARLSKQVKTIsefEKEIELLQ 1037
Cdd:TIGR00606 1000 MRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQMQVLQ--MKQEHQKLEENIDLI---KRNHVLAL 1074
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462545112 1038 AQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLE 1084
Cdd:TIGR00606 1075 GRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
852-1073 |
3.66e-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: 44.33 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 852 KLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELE-TQKEQI 930
Cdd:pfam06008 41 QIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGENDFaLPSSDL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 931 QLKLQEKTEELKE-KMDNLTKQLFDDVQKEERQRMLLEKSfelktqdyEKQIQSLKEEIKALKDekmQLQHLVeGEHvtS 1009
Cdd:pfam06008 121 SRMLAEAQRMLGEiRSRDFGTQLQNAEAELKAAQDLLSRI--------QTWFQSPQEENKALAN---ALRDSL-AEY--E 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 1010 DGLKAEVARLSKQVKTISEFEkeiELLQAQKIDVEKHvQSQKREMREKMSEITKQLLESYDIED 1073
Cdd:pfam06008 187 AKLSDLRELLREAAAKTRDAN---RLNLANQANLREF-QRKKEEVSEQKNQLEETLKTARDSLD 246
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1105-1302 |
4.01e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1105 VLESHFQSQKDCYEKEIEALNFKVvhlSQEINHLQKLFREENDINESIRHEVTRLTSEnmmipdfkqqISELEKQKQDLE 1184
Cdd:PHA02562 188 MKIDHIQQQIKTYNKNIEEQRKKN---GENIARKQNKYDELVEEAKTIKAEIEELTDE----------LLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1185 I---RLNEQAEKMKGKLEELSNQLHR----------SQEEEGTQRKALEAQNEIH--TKEKEKLIDKIQEMQEASDHLKK 1249
Cdd:PHA02562 255 AalnKLNTAAAKIKSKIEQFQKVIKMyekggvcptcTQQISEGPDRITKIKDKLKelQHSLEKLDTAIDELEEIMDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 1250 QFETESEVKC---NFRQEASRLTLENRDLEEELD--MKDRV-----IKKLQDQVKTLSKTIGK 1302
Cdd:PHA02562 335 QSKKLLELKNkisTNKQSLITLVDKAKKVKAAIEelQAEFVdnaeeLAKLQDELDKIVKTKSE 397
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
800-1298 |
5.16e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.73 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 800 LARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRfvlNIQLTYRVQRLQKKLEDQNKENHGLVE----KLTSLAALRA 875
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDR---NQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 876 GDVEKIQKLE----------------------AELEKAATH------RRNYEEKGKRYRDAvEEKLAKLQKHNSELETQK 927
Cdd:pfam05557 91 KLNEKESQLAdarevisclknelselrrqiqrAELELQSTNseleelQERLDLLKAKASEA-EQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 928 EQIQ-----LKLQEK-TEELKE---------KMDNLTKQLFDDV---------------QKEERQRML------------ 965
Cdd:pfam05557 170 QRIKelefeIQSQEQdSEIVKNskselaripELEKELERLREHNkhlnenienklllkeEVEDLKRKLereekyreeaat 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 966 --LEKS-FELKTQDYEKQIQSLKEEIKALKDEKMQLQHLVEGEHVtsdgLKAEVARLSKQVK----TISEFEKEIELLQA 1038
Cdd:pfam05557 250 leLEKEkLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIV----LKEENSSLTSSARqlekARRELEQELAQYLK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1039 QKIDVE---KHVQSQKREMREKMSEITK------QLLESYDIEDVRSRLSVEDLEHLNEDGELWFAYEGLKKATRVlesh 1109
Cdd:pfam05557 326 KIEDLNkklKRHKALVRRLQRRVLLLTKerdgyrAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEA---- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1110 fqsQKDCYEKEIEALNFKVVHLSQEInhlqKLFREENDINE--SIRHEVTRLTSENmmiPDFKQQISELEKQKQDLEIRL 1187
Cdd:pfam05557 402 ---QLSVAEEELGGYKQQAQTLEREL----QALRQQESLADpsYSKEEVDSLRRKL---ETLELERQRLREQKNELEMEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1188 neqaekMKGKLEELSNQ-----LHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQFETESEVkcNFR 1262
Cdd:pfam05557 472 ------ERRCLQGDYDPkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTM--NFK 543
|
570 580 590
....*....|....*....|....*....|....*.
gi 2462545112 1263 qeasrltlENRDLEEELDMKDRVIKKLQDQVKTLSK 1298
Cdd:pfam05557 544 --------EVLDLRKELESAELKNQRLKEVFQAKIQ 571
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
842-1280 |
5.71e-04 |
|
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: 44.51 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 842 LTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRA--------GDVEKIQKLEAELEKAAT--HRRNYEEKGKRyRDAVEE 911
Cdd:pfam15964 236 LESQVKSLRKDLAESQKTCEDLKERLKHKESLVAastssrvgGLCLKCAQHEAVLAQTHTnvHMQTIERLTKE-RDDLMS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 912 KLAKLQKHNSELETQK----EQIQLKLQEKTEELKEKMDNLTKqlFDDVQKE-ERQRMLLEKSFELKTQDYEKQIQSLKE 986
Cdd:pfam15964 315 ALVSVRSSLAEAQQREssayEQVKQAVQMTEEANFEKTKALIQ--CEQLKSElERQKERLEKELASQQEKRAQEKEALRK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 987 EIKALKDEKMQLQhLVEGEHVTSdgLKAEVARLSKQ-VKTISEFEKEIELLQAQKIDVEK----------HVQSQK---- 1051
Cdd:pfam15964 393 EMKKEREELGATM-LALSQNVAQ--LEAQVEKVTREkNSLVSQLEEAQKQLASQEMDVTKvcgemryqlnQTKMKKdeae 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1052 REMREKMSEITKQL-LESYDIEDVRSRL--SVEDLEHLNEDG-----ELWFAYEGLKKATRVLESHFQ---SQKDCYEKE 1120
Cdd:pfam15964 470 KEHREYRTKTGRQLeIKDQEIEKLGLELseSKQRLEQAQQDAarareECLKLTELLGESEHQLHLTRLekeSIQQSFSNE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1121 IEALNFKVVHLSQEINhlQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKqkqdleiRLNEQAEKMKGKLEE 1200
Cdd:pfam15964 550 AKAQALQAQQREQELT--QKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAK-------KLEEITQKSRSEVEQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1201 LSNQ---LHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEmqeasdhLKKQFETESEVKCNFRQEASRLTLENRDLEE 1277
Cdd:pfam15964 621 LSQEkeyLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQ-------LDKHCQATAQQLVQLLSKQNQLFKERQNLTE 693
|
...
gi 2462545112 1278 ELD 1280
Cdd:pfam15964 694 EVQ 696
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
907-1092 |
5.84e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 907 DAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLfddvqkEERQRMLLEksFELKTQDYEKQIQSLKE 986
Cdd:PHA02562 191 DHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEI------EELTDELLN--LVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 987 EIKALKDEKMQLQ---HLVEGEHV---TSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHV------QSQKREM 1054
Cdd:PHA02562 263 AAAKIKSKIEQFQkviKMYEKGGVcptCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdefneqSKKLLEL 342
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462545112 1055 REKMSEItKQLLESY-----DIEDVRSRLSVedlEHLNEDGEL 1092
Cdd:PHA02562 343 KNKISTN-KQSLITLvdkakKVKAAIEELQA---EFVDNAEEL 381
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
859-991 |
6.91e-04 |
|
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: 42.50 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 859 ENHGLVEKLTSLAALRAgdvEKIQKLEAELEKaathRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKT 938
Cdd:pfam06785 66 EKSFLEEKEAKLTELDA---EGFKILEETLEE----LQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFR 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 939 EELKEKMDNLTKQLFDDVQKEERQRMLLEKSFElKTQDYEKQIQSLKEEIKAL 991
Cdd:pfam06785 139 LESEEQLAEKQLLINEYQQTIEEQRSVLEKRQD-QIENLESKVRDLNYEIKTL 190
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
847-996 |
7.90e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 847 QRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQ 926
Cdd:smart00787 147 EGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKK 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 927 KEQIQLKLQEKTEELkEKMDNLTKQLFDDVQKEERQRmlleksfeLKTQDYE-KQIQSLKEEIKALKDEKM 996
Cdd:smart00787 227 LEELEEELQELESKI-EDLTNKKSELNTEIAEAEKKL--------EQCRGFTfKEIEKLKEQLKLLQSLTG 288
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
797-991 |
8.39e-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: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 797 RGFLARRRYRKMLEEHKAVILQKYARAWLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAG 876
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 877 DVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQI--QLKLQEKTEELKEKMDNLTKQLFD 954
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERleEELEEEALEEQLEAEREELLEELL 742
|
170 180 190
....*....|....*....|....*....|....*..
gi 2462545112 955 DVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKAL 991
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
907-1017 |
8.41e-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: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 907 DAVEEKLAKLQKHNSELETQKEQI----QLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK--Q 980
Cdd:COG0542 407 DSKPEELDELERRLEQLEIEKEALkkeqDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRygK 486
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462545112 981 IQSLKEEIKALKDEKMQLQHLVEgEHVTSDglkaEVA 1017
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLR-EEVTEE----DIA 518
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1026-1243 |
8.44e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1026 ISEFEKEIELLQAQKidveKHVQSQKREMREKMSEITKQLLE-SYDIEDVRSRLSV--EDLEHLNEDgelwfayegLKKA 1102
Cdd:COG3883 18 IQAKQKELSELQAEL----EAAQAELDALQAELEELNEEYNElQAELEALQAEIDKlqAEIAEAEAE---------IEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1103 TRVLESHFQSQkdcYEKeiealnfkvvhlSQEINHLQKLFrEENDINESIR--HEVTRLTS-ENMMIPDFKQQISELEKQ 1179
Cdd:COG3883 85 REELGERARAL---YRS------------GGSVSYLDVLL-GSESFSDFLDrlSALSKIADaDADLLEELKADKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 1180 KQDLEIRLNEqAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEA 1243
Cdd:COG3883 149 KAELEAKLAE-LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1150-1300 |
8.50e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1150 ESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLHRSqEEEGTQRKALEAQNEIHTKE 1229
Cdd:PRK02224 247 EERREELETLEAE---IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREELEDR 322
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 1230 KEKLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTI 1300
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
840-1084 |
8.52e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 840 IQLTYRVQRLQKKLEDQNKENHGLVEKLTSlaalragdvEKIQKLEAELEKAATHRrnYEEKGkryrdaVEEKLAKLQKH 919
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALN---------EMIEKLKKEIDLEYTEA--VIAMG------LQERLENLREE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 920 NSELETQKEQIQLKLQEKTEELKEKMD-NLT--------KQLFDDVQKEERQRMLLE---KSFELKtQDYEKQIQS---- 983
Cdd:PLN03229 495 FSKANSQDQLMHPVLMEKIEKLKDEFNkRLSrapnylslKYKLDMLNEFSRAKALSEkksKAEKLK-AEINKKFKEvmdr 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 984 --LKEEIKALKDEKMQLQHLVEGEhvTSDGLKAEVARLSKQV-----KTISEFEKEIELLQAQKIDVEKHVQSQkrEMRE 1056
Cdd:PLN03229 574 peIKEKMEALKAEVASSGASSGDE--LDDDLKEKVEKMKKEIelelaGVLKSMGLEVIGVTKKNKDTAEQTPPP--NLQE 649
|
250 260 270
....*....|....*....|....*....|..
gi 2462545112 1057 KMS----EITKQLLESYDIEDVRSRLSVEDLE 1084
Cdd:PLN03229 650 KIEslneEINKKIERVIRSSDLKSKIELLKLE 681
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1170-1300 |
1.05e-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: 43.86 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1170 KQQISELEKQKQDLEirlnEQAEKMKGKLEELSNQLHRSqEEEGTQRKALEAQNEIHTKEKEKLID----------KIQE 1239
Cdd:pfam05667 334 EEELEELQEQLEDLE----SSIQELEKEIKKLESSIKQV-EEELEELKEQNEELEKQYKVKKKTLDllpdaeeniaKLQA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1240 MQEASD----HLKKQFET----------ESEVKCNFRQEASRLTLEN--------RDLEEELDMKDRVIKKLQDQVKTLS 1297
Cdd:pfam05667 409 LVDASAqrlvELAGQWEKhrvplieeyrALKEAKSNKEDESQRKLEEikelrekiKEVAEEAKQKEELYKQLVAEYERLP 488
|
...
gi 2462545112 1298 KTI 1300
Cdd:pfam05667 489 KDV 491
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
845-1093 |
1.05e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLTSLAALRA------GDVEKIQKLEAELEKA---ATHRRNYEEKgkryrdaVEEKLAK 915
Cdd:COG1340 72 KVKELKEERDELNEKLNELREELDELRKELAelnkagGSIDKLRKEIERLEWRqqtEVLSPEEEKE-------LVEKIKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 916 LQKhnsELETQKEQIQLKlqEKTEELKEKMDNLTKQLfddvqKEERQRMlleksfelktQDYEKQIQSLKEEIKALKDEK 995
Cdd:COG1340 145 LEK---ELEKAKKALEKN--EKLKELRAELKELRKEA-----EEIHKKI----------KELAEEAQELHEEMIELYKEA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 996 MQLQHLVEGEHVTSDGLKAEVARLSKQ----VKTISEFEKEIELLQAQKIDVEKhvQSQKREMREKMSEITKQLLESydi 1071
Cdd:COG1340 205 DELRKEADELHKEIVEAQEKADELHEEiielQKELRELRKELKKLRKKQRALKR--EKEKEELEEKAEEIFEKLKKG--- 279
|
250 260
....*....|....*....|..
gi 2462545112 1072 edvrSRLSVEDLEHLNEDGELW 1093
Cdd:COG1340 280 ----EKLTTEELKLLQKSGLLE 297
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
845-1084 |
1.13e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.52 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENhglvEKLTSLAA-----------LRAGdVEKIQKLEAELEkaaTHRRNYEEKG--KRYRDAVEE 911
Cdd:pfam05622 88 KCEELEKEVLELQHRN----EELTSLAEeaqalkdemdiLRES-SDKVKKLEATVE---TYKKKLEDLGdlRRQVKLLEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 912 KLA-----------KLQKHN---SELETQKEQIQ---LKLQE---KTEELKEKMDNLTKQLfDDVQKeERQRMLLEK--- 968
Cdd:pfam05622 160 RNAeymqrtlqleeELKKANalrGQLETYKRQVQelhGKLSEeskKADKLEFEYKKLEEKL-EALQK-EKERLIIERdtl 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 969 ----------------------------------SFELKTQDYEKQIQSLKEEIKALK--------DEKMQLQHLVEGEH 1006
Cdd:pfam05622 238 retneelrcaqlqqaelsqadallspssdpgdnlAAEIMPAEIREKLIRLQHENKMLRlgqegsyrERLTELQQLLEDAN 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1007 VTSDGLKAEvARLSKQvktisefekEIELLQAQKIDVEKHVQSQ--KRE----MREKMSEITKQLLESYDiEDVRSRLSV 1080
Cdd:pfam05622 318 RRKNELETQ-NRLANQ---------RILELQQQVEELQKALQEQgsKAEdsslLKQKLEEHLEKLHEAQS-ELQKKKEQI 386
|
....
gi 2462545112 1081 EDLE 1084
Cdd:pfam05622 387 EELE 390
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
906-1218 |
1.14e-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: 43.15 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 906 RDAVEEKLAKLQKHNSELE-------TQKEQIQLKLQEKTEELKEKMDNL--TKQLFDDVQKEERQRMLLeksfelktqD 976
Cdd:pfam04108 37 RRGLSVQLANLEKVREGLEkvlnelkKDFKQLLKDLDAALERLEETLDKLrnTPVEPALPPGEEKQKTLL---------D 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 977 Y--EKQIQSLKEEIKALKDEkmqlqhlvegehvtsdgLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKH---VQSQK 1051
Cdd:pfam04108 108 FidEDSVEILRDALKELIDE-----------------LQAAQESLDSDLKRFDDDLRDLQKELESLSSPSESislIPTLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1052 REMREKMSEItKQLLES----YDiedvrsrLSVEDLEHLNEDGELWFAYegLKKATRVLESHFQSQKDCYE--------- 1118
Cdd:pfam04108 171 KELESLEEEM-ASLLESltnhYD-------QCVTAVKLTEGGRAEMLEV--LENDARELDDVVPELQDRLDemennyerl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1119 -KEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLE----------IRL 1187
Cdd:pfam04108 241 qKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEGFPsaygslllevERR 320
|
330 340 350
....*....|....*....|....*....|.
gi 2462545112 1188 NEQAEKMKGKLEELSNQLHRSQEEEGTQRKA 1218
Cdd:pfam04108 321 REWAEKMKKILRKLAEELDRLQEEERKRREK 351
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
915-1086 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 915 KLQKHNSELETQK----------EQIQLKLQEKTEELKEKMDNLTKQlfddvqkeerqrMLLEKSFELKTQDYEkqiQSL 984
Cdd:smart00787 120 QLVKTFARLEAKKmwyewrmkllEGLKEGLDENLEGLKEDYKLLMKE------------LELLNSIKPKLRDRK---DAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 985 KEEIKALKdekmqlQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQS---QKREMREKMSEI 1061
Cdd:smart00787 185 EEELRQLK------QLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDltnKKSELNTEIAEA 258
|
170 180
....*....|....*....|....*...
gi 2462545112 1062 TKQLLES--YDIEDVRS-RLSVEDLEHL 1086
Cdd:smart00787 259 EKKLEQCrgFTFKEIEKlKEQLKLLQSL 286
|
|
| YkyA |
pfam10368 |
Putative cell-wall binding lipoprotein; YkyA is a family of proteins containing a lipoprotein ... |
850-998 |
1.32e-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: 41.81 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 850 QKKLEDQNKENHGLVEKLTSLAAlraGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKeq 929
Cdd:pfam10368 24 QEPLVELEKKEQELYEEIIELGM---DEFDEIKKLSDEALENVEEREELLEKEKESIEEAKEEFKKIKEIIEEIEDEE-- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545112 930 iqlkLQEKTEELKEKMDNLTK---QLFDDVQK---EERQ--RMLLEKSFELKtqDYEKQIQSLKEEIKALKDEKMQL 998
Cdd:pfam10368 99 ----LKKEAEELIDAMEERYEaydELYDAYKKaleLDKElyEMLKDEDLTLE--ELQEQIEKINESYEEVKEANEQF 169
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
727-1263 |
1.49e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 727 QRKKFLRERRAALIIQQyfrgQQTVRKAITAVALKEAWAAIIIQKHcrgylvrslyQLIRMATITMQAYSRGFLARRRYR 806
Cdd:COG1196 309 ERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEEAE----------EELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 807 KMLEEHKAVILQKYARAwLARRRFQSIRRFVLNIQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEA 886
Cdd:COG1196 375 AEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 887 ELEKAATHRRNYEEKGKRY---RDAVEEKLAKLQKHNSELETQKEQIQLKLQE----KTEELKEKMDNLTKQLFDDVQKE 959
Cdd:COG1196 454 LEEEEEALLELLAELLEEAallEAALAELLEELAEAAARLLLLLEAEADYEGFlegvKAALLLAGLRGLAGAVAVLIGVE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 960 ERQRMLLEKSFELKTQDY--------EKQIQSLKEE------------IKALKDEKMQLQHLVEGEHVtsDGLKAEVARL 1019
Cdd:COG1196 534 AAYEAALEAALAAALQNIvveddevaAAAIEYLKAAkagratflpldkIRARAALAAALARGAIGAAV--DLVASDLREA 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1020 SKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGElwfAYEGL 1099
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE---LAERL 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1100 KKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQ 1179
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1180 KQDLEIRL------NEQAekmkgkLEELsnqlhrsqEEEGTQRKALEAQNEIHTKEKEKLIDKIQEM-QEASDHLKKQFE 1252
Cdd:COG1196 769 LERLEREIealgpvNLLA------IEEY--------EELEERYDFLSEQREDLEEARETLEEAIEEIdRETRERFLETFD 834
|
570
....*....|.
gi 2462545112 1253 tesEVKCNFRQ 1263
Cdd:COG1196 835 ---AVNENFQE 842
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
765-783 |
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
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
845-979 |
1.98e-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: 40.37 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 845 RVQRLQKKLEDQNKENHGLVEKLTSLAAlragdveKIQKLEAELEKAathrrnyEEKGKRYRDAVEEKLAK------LQK 918
Cdd:pfam12718 15 RAEELEEKVKELEQENLEKEQEIKSLTH-------KNQQLEEEVEKL-------EEQLKEAKEKAEESEKLktnnenLTR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545112 919 HNSELETQKEQIQLKLQEKTEELKEkMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEK 979
Cdd:pfam12718 81 KIQLLEEELEESDKRLKETTEKLRE-TDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
903-1300 |
2.10e-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: 43.12 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 903 KRYRDAVEEKLA--KLQKHNSELETQKEQIQLKLQeKTEELKEKMDNLtkQLFDDVQKEERQRMLLEKSFELKTQDYEKQ 980
Cdd:TIGR01612 466 KRFFEIFEEEWGsyDIKKDIDENSKQDNTVKLILM-RMKDFKDIIDFM--ELYKPDEVPSKNIIGFDIDQNIKAKLYKEI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 981 IQSLKEEIKALKD-EKMQLQHLVEGEHVTSDGLKaevarLSKQVKTIseFEKEIELlqaqkIDVEKHVQSQKREMREKMS 1059
Cdd:TIGR01612 543 EAGLKESYELAKNwKKLIHEIKKELEEENEDSIH-----LEKEIKDL--FDKYLEI-----DDEIIYINKLKLELKEKIK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1060 EITKQ---LLESYDIEDV--RSRLSVEDLEHLNEdgelWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQE 1134
Cdd:TIGR01612 611 NISDKneyIKKAIDLKKIieNNNAYIDELAKISP----YQVPEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKE 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1135 --INHLQKLFREEnDINESIRHEVTRLtsENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGkleELSNQLHRSQEEe 1212
Cdd:TIGR01612 687 naIDNTEDKAKLD-DLKSKIDKEYDKI--QNMETATVELHLSNIENKKNELLDIIVEIKKHIHG---EINKDLNKILED- 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1213 gtqrkaleaqneIHTKEKEkLIDKIQEMQEASDHLKKQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQ 1292
Cdd:TIGR01612 760 ------------FKNKEKE-LSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIK 826
|
....*...
gi 2462545112 1293 VKTLSKTI 1300
Cdd:TIGR01612 827 EDEIFKII 834
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
841-1031 |
2.39e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQK----------KLEDQNKENHGLVEKLT----SLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR 906
Cdd:pfam07888 77 ELESRVAELKEelrqsrekheELEEKYKELSASSEELSeekdALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 907 DAVEEKLAKLQkhnsELETQKEQIQLKLQEKTEELKEKMDNLtkQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKE 986
Cdd:pfam07888 157 ERAKKAGAQRK----EEEAERKQLQAKLQQTEEELRSLSKEF--QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462545112 987 EIKALKDEKMQLQHLVEGEHVTSDGLKAEVARL-SKQVKTISEFEK 1031
Cdd:pfam07888 231 ENEALLEELRSLQERLNASERKVEGLGEELSSMaAQRDRTQAELHQ 276
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1138-1296 |
2.40e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1138 LQKLFREENDINE---SIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNQLhRSQEEEGT 1214
Cdd:COG3883 25 LSELQAELEAAQAeldALQAELEELNEE---YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA-RALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1215 QRKALE----------------AQNEIHTKEKEkLIDKIQEMQEASDHLKKQFETESEvkcNFRQEASRLTLENRDLEEE 1278
Cdd:COG3883 101 SVSYLDvllgsesfsdfldrlsALSKIADADAD-LLEELKADKAELEAKKAELEAKLA---ELEALKAELEAAKAELEAQ 176
|
170
....*....|....*...
gi 2462545112 1279 LDMKDRVIKKLQDQVKTL 1296
Cdd:COG3883 177 QAEQEALLAQLSAEEAAA 194
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
765-783 |
2.55e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 36.53 E-value: 2.55e-03
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1175-1302 |
2.58e-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: 42.11 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1175 ELEKQKQDLEIRLNE---QAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEK---EKLIDKIQEMQEASDHLK 1248
Cdd:pfam15905 160 ELMKLRNKLEAKMKEvmaKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKsetEKLLEYITELSCVSEQVE 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 1249 KQFETESEVKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGK 1302
Cdd:pfam15905 240 KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEE 293
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
958-1255 |
2.65e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 958 KEERQRML-LEKSFELKTQDYEKQIQSLKEEIKALKDEKmqlQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELL 1036
Cdd:pfam02029 16 REERRRQKeEEEPSGQVTESVEPNEHNSYEEDSELKPSG---QGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1037 QAqkiDVEKHVQSQKREMREKMSEITKQ------LLESYDIEDVRSRlSVEDLEHLNEDGELWFAYEGLKKATRVLESHF 1110
Cdd:pfam02029 93 IA---DEKESVAERKENNEEEENSSWEKeekrdsRLGRYKEEETEIR-EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1111 QSQKDCYEKEIEALNFK---------VVHLSQEINHL-QKLFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQK 1180
Cdd:pfam02029 169 VPTENFAKEEVKDEKIKkekkvkyesKVFLDQKRGHPeVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1181 QDLEIRL------NEQAEKMKGK-------LEEL---SNQLHRSQEEEGTQRKALEAQNEIHTKE-KEKLIDKIqEMQEA 1243
Cdd:pfam02029 249 KLEELRRrrqekeSEEFEKLRQKqqeaeleLEELkkkREERRKLLEEEEQRRKQEEAERKLREEEeKRRMKEEI-ERRRA 327
|
330
....*....|..
gi 2462545112 1244 SDHLKKQFETES 1255
Cdd:pfam02029 328 EAAEKRQKLPED 339
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
978-1193 |
2.86e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 978 EKQIQSLKEEIKALKDEKMQLQHLVegehvtsDGLKAEVARLSKQVKTIsefEKEIELLQAQKIDVEKHVQSQKREMREK 1057
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAEL-------DALQAELEELNEEYNEL---QAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1058 MSEITKQ----------------LLESYDIEDVRSRLSVedLEHLNE-DGELwfaYEGLKKATRVLEshfqSQKDCYEKE 1120
Cdd:COG3883 85 REELGERaralyrsggsvsyldvLLGSESFSDFLDRLSA--LSKIADaDADL---LEELKADKAELE----AKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 1121 IEALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLtsenmmipdfKQQISELEKQKQDLEIRLNEQAEK 1193
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA----------EAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
839-1329 |
2.93e-03 |
|
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: 42.50 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 839 NIQLTYRVQRLQKKLEDQNKENHGLVEKLTSlAALRAGDVEKIQKLEAE--LEKAATHRRNYEEKgKRYRDAVEEKLAKL 916
Cdd:pfam10174 69 NQHLQLTIQALQDELRAQRDLNQLLQQDFTT-SPVDGEDKFSTPELTEEnfRRLQSEHERQAKEL-FLLRKTLEEMELRI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 917 QKHNSELETQKEQIQlKLQEKTEelkekMDNLTKQLFDDVQkeERQRMLLEksFELKTQDYEKQIQSLKEEIKALKDE-- 994
Cdd:pfam10174 147 ETQKQTLGARDESIK-KLLEMLQ-----SKGLPKKSGEEDW--ERTRRIAE--AEMQLGHLEVLLDQKEKENIHLREElh 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 995 -KMQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQ-KIDVEKH---------VQSQKREMREKMSEItK 1063
Cdd:pfam10174 217 rRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNgLLHTEDReeeikqmevYKSHSKFMKNKIDQL-K 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1064 QLLESYDIEDVRSRLSVEDLEHLNEDGELWFayEGLKKATRVLE---SHFQSQKDCYEKEIEAlnfKVVHLSQEINHLQK 1140
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHI--EVLKESLTAKEqraAILQTEVDALRLRLEE---KESFLNKKTKQLQD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1141 LFREENDINESIRHEVTRLTSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELSNqlhrSQEEEGTQRKALe 1220
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN----TDTALTTLEEAL- 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1221 aqneihtKEKEKLIDKIQEMQEASDHlkkqfetesevkcNFRQEASRLTLENRDLEEELDM-------KDRVIKKLQDQV 1293
Cdd:pfam10174 446 -------SEKERIIERLKEQREREDR-------------ERLEELESLKKENKDLKEKVSAlqpelteKESSLIDLKEHA 505
|
490 500 510
....*....|....*....|....*....|....*.
gi 2462545112 1294 KTLSKTIGKANdvhssSGPKEYLGMLQYKREDEAKL 1329
Cdd:pfam10174 506 SSLASSGLKKD-----SKLKSLEIAVEQKKEECSKL 536
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
870-1067 |
2.98e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 870 LAALRAgDVEKIQKLEAELEK---------AATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLK-LQEKTE 939
Cdd:PRK04778 207 LAALEQ-IMEEIPELLKELQTelpdqlqelKAGYRELVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELDLDeAEEKNE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 940 ELKEKMDNL-----------------TKQLFDDVQKEERQ-RMLLE------KSFELKTQDYEKQiQSLKEEIKALKDEK 995
Cdd:PRK04778 286 EIQERIDQLydilerevkarkyveknSDTLPDFLEHAKEQnKELKEeidrvkQSYTLNESELESV-RQLEKQLESLEKQY 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462545112 996 MQLQHLVEGEHVTSDGLKAEVARLSKQVKTISEFEKEI-ELLQAQKIDvEKHVQSQKREMREKMSEItKQLLE 1067
Cdd:PRK04778 365 DEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLsEMLQGLRKD-ELEAREKLERYRNKLHEI-KRYLE 435
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1007-1290 |
3.15e-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: 41.72 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1007 VTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDvrsrlSVEDLEHL 1086
Cdd:pfam15905 56 VKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSA-----SVASLEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1087 NEDgelwfayegLKKATRVLESHFQSqkDCYEKEIEALNFKVVHLSQEINHLQK-LFREENDINESIRHEVTRLTSENMM 1165
Cdd:pfam15905 131 LLE---------LTRVNELLKAKFSE--DGTQKKMSSLSMELMKLRNKLEAKMKeVMAKQEGMEGKLQVTQKNLEHSKGK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1166 IPDFKQQISELEKQKQDLEirlnEQAEKMKGKLEELSN---QLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQE 1242
Cdd:pfam15905 200 VAQLEEKLVSTEKEKIEEK----SETEKLLEYITELSCvseQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSK 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462545112 1243 ASDHLK---KQFETESEVKCN-FRQEASRLTLENRDLEEELDMKDRVIKKLQ 1290
Cdd:pfam15905 276 QIKDLNekcKLLESEKEELLReYEEKEQTLNAELEELKEKLTLEEQEHQKLQ 327
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1157-1307 |
3.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1157 TRLTSENMMIPDFKQQISELEKQKQDLEIR---LNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKL 1233
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKrdeLNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545112 1234 IDKIQEMQEASDHLKKQFEtESEVKCNFRQEASRLTLENRDLEEELDMKD---RVIKKLQDQVKTLSKTIGKANDVH 1307
Cdd:COG1340 81 DELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVlspEEEKELVEKIKELEKELEKAKKAL 156
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1043-1276 |
3.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1043 VEKHVQSQKREMREKMSEITKQLlesydiEDVRSRLsvEDLEHlnedgelwfAYEGLKKATRVLEShfQSQKDCYEKEIE 1122
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQL------PELRKEL--EEAEA---------ALEEFRQKNGLVDL--SEEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1123 ALNFKVVHLSQEINHLQKLFREENDINESIRHEVTRLtSENMMIPDFKQQISELEKQKQDLEIRLNEQAEKMKGKLEELS 1202
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 1203 NQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDHLKKQfetesevkcnfRQEASRLtleNRDLE 1276
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL-----------EAELRRL---EREVE 361
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
841-1109 |
3.84e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQkhn 920
Cdd:COG4372 77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 sELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQDYEKQIQSLKEEIKALKDEKmqLQH 1000
Cdd:COG4372 154 -ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL--EAK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSV 1080
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
250 260
....*....|....*....|....*....
gi 2462545112 1081 EDLEHLNEDGELWFAYEGLKKATRVLESH 1109
Cdd:COG4372 311 GALEDALLAALLELAKKLELALAILLAEL 339
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
881-1246 |
3.90e-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: 42.35 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 881 IQKLEAELEKAATHRRNYEEKGKRYRDAVEEKLAKLQK---------HNSELETQKEQIQLKLQEKteelKEKMDNLtKQ 951
Cdd:TIGR01612 1120 IKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvadkaisndDPEEIEKKIENIVTKIDKK----KNIYDEI-KK 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 952 LFDDVQKEERQRMLLEKSFELKTQdYEKQIQSLKEEikALKDEKMQLQHLV---EGEHVTSDGLKAEVARLSKQVKTISE 1028
Cdd:TIGR01612 1195 LLNEIAEIEKDKTSLEEVKGINLS-YGKNLGKLFLE--KIDEEKKKSEHMIkamEAYIEDLDEIKEKSPEIENEMGIEMD 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1029 FEKEIELLQAQKIDVEKH-VQSQKR-----EMREKMSEITKQLLESYDIEDVRSRLSvedlehlnedgelwfayeglkka 1102
Cdd:TIGR01612 1272 IKAEMETFNISHDDDKDHhIISKKHdenisDIREKSLKIIEDFSEESDINDIKKELQ----------------------- 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1103 TRVLESH-FQSQKDCYEKEIEALnFKVVHLSQEINHLQKLFREENDINESIRHEVTRLTSENMMIPDFKQQISeLEKQKQ 1181
Cdd:TIGR01612 1329 KNLLDAQkHNSDINLYLNEIANI-YNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDIN-LEECKS 1406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462545112 1182 DLEIRL-----NEQAEKMKGK-----LEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEKLIDKIQEMQEASDH 1246
Cdd:TIGR01612 1407 KIESTLddkdiDECIKKIKELknhilSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDH 1481
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1168-1331 |
4.03e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 40.52 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1168 DFKQQISELEKQKQDLEIRLNEQaekmkgkLEELSNQLHRSQEEEGTQRKALEAQNEIhTKEKEKLIDKIQEMQEASDHL 1247
Cdd:pfam14988 26 QYVQECEEIERRRQELASRYTQQ-------TAELQTQLLQKEKEQASLKKELQALRPF-AKLKESQEREIQDLEEEKEKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1248 KKQF-ETESEVKCNFRQEASRLTLENRDLeEELDMKDRVIKKLQDQVKTLSKTIGKANDVHSSSGPKEYlgmlQYKREDE 1326
Cdd:pfam14988 98 RAETaEKDREAHLQFLKEKALLEKQLQEL-RILELGERATRELKRKAQALKLAAKQALSEFCRSIKREN----RQLQKEL 172
|
....*
gi 2462545112 1327 AKLIQ 1331
Cdd:pfam14988 173 LQLIQ 177
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1256 |
4.08e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 850 QKKLEDQNKENHGLVEKLTSLAALRagdvEKIQKLEAELEKAATH---------RRNYEEKGKRYRDAvEEKLAKLQKhn 920
Cdd:TIGR00606 254 LKEIEHNLSKIMKLDNEIKALKSRK----KQMEKDNSELELKMEKvfqgtdeqlNDLYHNHQRTVREK-ERELVDCQR-- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 921 sELETQKEQIQLKLQEKTEELKEKMdnlTKQLFDDVQKEErqrmlleksfelkTQDYEKQIQSLkeeikALKDEKMQLQH 1000
Cdd:TIGR00606 327 -ELEKLNKERRLLNQEKTELLVEQG---RLQLQADRHQEH-------------IRARDSLIQSL-----ATRLELDGFER 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1001 LVEGEHVTSDGLKAEVARLSKQVKTISEFEKEIEllqaqkiDVEKHVQSQKREMREKMSEITKQLlesyDIEDVRSRLSV 1080
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ-------SKERLKQEQADEIRDEKKGLGRTI----ELKKEILEKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1081 EDLEHLNEDGELwfAYEGLKKATRVLESHFQSQKDCYEKE----IEALNFKVVHLSQEINHLQKLFREENDINESIRHEV 1156
Cdd:TIGR00606 454 EELKFVIKELQQ--LEGSSDRILELDQELRKAERELSKAEknslTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1157 TRLTSENMMIPD---FKQQISELEKQKQDLEI-----------------RLNEQAEKMKGKLEELSNQLHRSQEEEGTQR 1216
Cdd:TIGR00606 532 TTRTQMEMLTKDkmdKDEQIRKIKSRHSDELTsllgyfpnkkqledwlhSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2462545112 1217 KALEAQNEIHTKEKEKLIDKIQEMQEASD--HLKKQFETESE 1256
Cdd:TIGR00606 612 NELESKEEQLSSYEDKLFDVCGSQDEESDleRLKEEIEKSSK 653
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
941-1209 |
4.15e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 941 LKEKMDNLTKQL-------FDDVQKEErQRMLLEKSFELKTQDYEK--QIQSLKEEIKALKDEKMQLQHLVegehvTSDG 1011
Cdd:PRK05771 14 LKSYKDEVLEALhelgvvhIEDLKEEL-SNERLRKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVKS-----LEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1012 LKAEVARLSKQVKTISEFEKEIELLQaqkidvekhvqSQKREMREKMSEITKqlLESYDIedvrsrlsveDLEHLNeDGE 1091
Cdd:PRK05771 88 IKDVEEELEKIEKEIKELEEEISELE-----------NEIKELEQEIERLEP--WGNFDL----------DLSLLL-GFK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1092 LWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHLSQEINHLQKLFRE-------ENDINESIrhEVTRLtsenm 1164
Cdd:PRK05771 144 YVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEElkklgfeRLELEEEG--TPSEL----- 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462545112 1165 mIPDFKQQISELEKQKQDLEIRLNEQAEK----MKGKLEELSNQLHRSQ 1209
Cdd:PRK05771 217 -IREIKEELEEIEKERESLLEELKELAKKyleeLLALYEYLEIELERAE 264
|
|
| TBCA |
pfam02970 |
Tubulin binding cofactor A; |
1099-1203 |
4.18e-03 |
|
Tubulin binding cofactor A;
Pssm-ID: 460769 [Multi-domain] Cd Length: 99 Bit Score: 38.26 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1099 LKKATRVLEsHFQSQKDCYEKEIEalnfkvvhlsQEINHLQKLFREENDINEsIRHEVTRLTSENMMIPDFKQQIselEK 1178
Cdd:pfam02970 6 LKIKTGVVK-RLVKEEASYEKELE----------EQEARLEKLKADGADEYD-LKKQEEVLEETKAMIPDLKKRL---EE 70
|
90 100
....*....|....*....|....*
gi 2462545112 1179 QKQDLEIRLNEQAEKMKGkLEELSN 1203
Cdd:pfam02970 71 AVEDLEEFLEEEEDLGAD-TEELTA 94
|
|
| DUF6262 |
pfam19776 |
Family of unknown function (DUF6262); This family of proteins, functionally uncharacterized, ... |
897-998 |
4.51e-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: 38.37 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 897 NYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQL-KLQEKT----------EELKEKMDNLTKQlfddvQKE--ERQR 963
Cdd:pfam19776 1 KYDKMVELNRKESEEKIELAKKAIQEMLEEGEKITVpELVKRTglsrgffyknPEVRRELDEAIEQ-----QGGmvNPKR 75
|
90 100 110
....*....|....*....|....*....|....*
gi 2462545112 964 MLLEKSFELKTQDYEKQIQSLKEEIKALKDEKMQL 998
Cdd:pfam19776 76 EILDMALEKRIELLKKEIKELKRENEELKKENEKL 110
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
980-1241 |
4.63e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 980 QIQSLKEEIKALKDEKMQLQHLVEGEHVTSDGLKA---EVARLSKQV----KTISEFEKEIELLQAQKIDVEKHVQSQKR 1052
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSsnlELENIKKQIaddeKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1053 EMREKMS-EITKQLLESyDIEDVRSRLSVEdLEHLNEDGELWFAYEGLKKATRVLESHFQSQKDCYEKEIEALNFKVVHL 1131
Cdd:PRK01156 240 ALNELSSlEDMKNRYES-EIKTAESDLSME-LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1132 SQEINHLQKLFREENDInESIRHEVTRLTSEnmmIPDFKQQISELEKQKQDLEIRLNEqAEKMKGKLEELSNQLHRSQEE 1211
Cdd:PRK01156 318 DAEINKYHAIIKKLSVL-QKDYNDYIKKKSR---YDDLNNQILELEGYEMDYNSYLKS-IESLKKKIEEYSKNIERMSAF 392
|
250 260 270
....*....|....*....|....*....|
gi 2462545112 1212 EGTQRKALEAQNEIHTKEKEKLIDKIQEMQ 1241
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
878-1024 |
5.89e-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: 40.73 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 878 VEKIQKLEAELEKAATHRRNYEEKGKRY---RDAVEEKLAKLQKHNSELETQKEqiqlKLQEKTEELKEKmdnltKQLFD 954
Cdd:pfam02841 154 LEERDKLEAKYNQVPRKGVKAEEVLQEFlqsKEAVEEAILQTDQALTAKEKAIE----AERAKAEAAEAE-----QELLR 224
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545112 955 DVQKEERQRMlleksfELKTQDYEKQIQSLKEEIKALKD------EKMQLQHLVEGEHVTSDGLKAEVARLSKQVK 1024
Cdd:pfam02841 225 EKQKEEEQMM------EAQERSYQEHVKQLIEKMEAEREqllaeqERMLEHKLQEQEELLKEGFKTEAESLQKEIQ 294
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
879-1094 |
6.56e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 40.58 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 879 EKIQKLEAELEKAAthrRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQK 958
Cdd:pfam09755 85 KKIQALKKEKETLA---MNYEQEEEFLTNDLSRKLTQLRQEKVELEQTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 959 EERQRMLLEKSFElktQDYEKQIQSLKEEIKALKDEKMQLQHLVE-------------GEHVTSDGLKAEVARLSKQVkt 1025
Cdd:pfam09755 162 LRREKVELENTLE---QEQEALVNRLWKRMDKLEAEKRLLQEKLDqpvsappsprdstSEGDTAQNLTAHIQYLRKEV-- 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545112 1026 iSEFEKEIELLQAQKIDVEKHVQSQKREMREKMSEITKQLLESYDIEDVRSRLSVEDLEHLNEDGELWF 1094
Cdd:pfam09755 237 -ERLRRQLATAQQEHTEKMAQYAQEERHIREENLRLQRKLQLEMERREALCRHLSESESSLEMDEERYF 304
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1170-1296 |
6.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1170 KQQISELEKQKQDLEIRL---NEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEihtkEKEKLIDKIQEMQEASDH 1246
Cdd:COG4372 51 REELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE----EAEELQEELEELQKERQD 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1247 LKkqfetesevkcnfrQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTL 1296
Cdd:COG4372 127 LE--------------QQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
841-1065 |
6.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 841 QLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKRYR--DAVEEKLAKLQK 918
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIAALLAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 919 HNSELETQKEQIQLKLQEKtEELKEKMDNLTKQLfDDVQKEERQRMLLEKSFELKT--QDYEKQIQSLKEEIKALKDEKM 996
Cdd:COG4717 379 AGVEDEEELRAALEQAEEY-QELKEELEELEEQL-EELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545112 997 QLQHLVE--GEHVTSDGLKAEVARLSKQVKTISEFEKEIELLQAQKIDVEKHVQSQKR-EMREKMSEITKQL 1065
Cdd:COG4717 457 ELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
914-997 |
6.91e-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: 38.72 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 914 AKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQlfddvQKEERqrmllEKSFELKTQDYEKQIQSLKEEIKALKD 993
Cdd:smart00935 21 KQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLSEA-----AREKK-----EKELQKKVQEFQRKQQKLQQDLQKRQQ 90
|
....
gi 2462545112 994 EKMQ 997
Cdd:smart00935 91 EELQ 94
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
909-1123 |
6.98e-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: 41.17 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 909 VEEKLAKLQKH---NSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQKEER-----QRMLLEKSFELktQDYEKQ 980
Cdd:pfam05701 231 AEEELQRLNQQllsAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKtstsiQAALASAKKEL--EEVKAN 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 981 IQSLKEEIKALKDEKMQLQHLVEGEhvtsdglKAEVARLSKQ----VKTISEFEKEIELLQaQKIDVekhVQSQKREMRE 1056
Cdd:pfam05701 309 IEKAKDEVNCLRVAAASLRSELEKE-------KAELASLRQRegmaSIAVSSLEAELNRTK-SEIAL---VQAKEKEARE 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1057 KMSEITKQLLE-SYDIEDVRS--RLSVEDLEHLNEDGELwfayegLKKATRVLESHFQSQKdcyeKEIEA 1123
Cdd:pfam05701 378 KMVELPKQLQQaAQEAEEAKSlaQAAREELRKAKEEAEQ------AKAAASTVESRLEAVL----KEIEA 437
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1097-1304 |
7.03e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1097 EGLKKATRVLESHFQSQKDCYEKEIEALNfKVVHLSQEINHLQKLFREENDI-NESIRHEVTRLTSENMMIPDFKQQISE 1175
Cdd:COG5185 186 LGLLKGISELKKAEPSGTVNSIKESETGN-LGSESTLLEKAKEIINIEEALKgFQDPESELEDLAQTSDKLEKLVEQNTD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 1176 LEK----QKQDLEIRLNEQAEKMKGKLEELSNQLHRSQEEEGTQRKALEAQNEIHTKEKEK-LIDKIQEMQEASDHLKKQ 1250
Cdd:COG5185 265 LRLeklgENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQeLEESKRETETGIQNLTAE 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462545112 1251 FETESEvKCNFRQEASRLTLENRDLEEELDMKDRVIKKLQDQVKTLSKTIGKAN 1304
Cdd:COG5185 345 IEQGQE-SLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIP 397
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
907-988 |
7.82e-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: 39.05 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 907 DAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQ--LFDDVQKEERQRML--LEKSFELKTQDYEKQIQ 982
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEaaTLSEEERQKKERELqkKQQELQRKQQEAQQDLQ 111
|
....*.
gi 2462545112 983 SLKEEI 988
Cdd:COG2825 112 KRQQEL 117
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
786-806 |
7.86e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 35.37 E-value: 7.86e-03
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
840-976 |
8.63e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 840 IQLTYRVQRLQKKLEDQNKENHGLVEKLTSLAALRAGDVEKIQKLEAELEKAATHRRNYEEKGKR---YRDAVEEKLAKL 916
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqqFEEQLVELSTEV 897
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545112 917 QKHNSELETQKEQI------QLKLQEKTEEL---KEKMDNLTKQLFDDVQKEERQRMLLEKSFELKTQD 976
Cdd:TIGR00606 898 QSLIREIKDAKEQDspletfLEKDQQEKEELissKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
888-985 |
9.31e-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: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545112 888 LEKAATHRRNYEEKGKRYRDAVEEKLAKLQKHNSELETQKEQIQLKLQEKTEELKEKMDNLTKQLFDDVQ-----KEERQ 962
Cdd:pfam02841 195 TDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQErmlehKLQEQ 274
|
90 100
....*....|....*....|...
gi 2462545112 963 RMLLEKSFELKTQDYEKQIQSLK 985
Cdd:pfam02841 275 EELLKEGFKTEAESLQKEIQDLK 297
|
|
| |
