|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
415-1133 |
0e+00 |
|
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: 1364.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGARIY 574
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKHLTGARIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 575 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLAVLKRALNVVGF 654
Cdd:cd14878 161 TYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREDVSTAERSLNREKLAVLKQALNVVGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 655 SSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 734
Cdd:cd14878 241 SSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 735 FFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHE 814
Cdd:cd14878 321 FYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 815 QVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTNAVYSPMKDGNGNVA 894
Cdd:cd14878 401 QTECVQEGVTMETAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAVYSPMKDGNGNVA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 895 LKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLsqtgslvsaypsfkfrghksalls 974
Cdd:cd14878 481 LKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKL------------------------ 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 975 kkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFD 1054
Cdd:cd14878 537 ---------------------------------------VTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFD 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62177127 1055 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKLQGWQMGVRKVFLK 1133
Cdd:cd14878 578 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
416-1133 |
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: 669.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRS--ADLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGA-------SRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQL 568
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSgssksssSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQF-DPTGRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 569 TGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ-TIQDDASTGERSLNREKLAVLKR 647
Cdd:cd00124 159 VGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDyLNSSGCDRIDGVDDAEEFQELLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 648 ALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 725
Cdd:cd00124 239 ALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 726 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSmqTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd00124 319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAES--TSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTNAvysp 885
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDFPDNQD-CLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF---- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 886 mkdgngnVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSenvvinhlfqsklsqtgslvsaypsfkf 965
Cdd:cd00124 472 -------SKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG---------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 966 rghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLMDIIGKLQKCTPHFIHCIRPN 1045
Cdd:cd00124 517 ----------------------------------------------------SQFRSQLDALMDTLNSTQPHFVRCIKPN 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQ-CKLQGWQ 1124
Cdd:cd00124 545 DEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLkLDSSGYQ 624
|
....*....
gi 62177127 1125 MGVRKVFLK 1133
Cdd:cd00124 625 LGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
404-1143 |
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: 616.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 404 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 483
Cdd:smart00242 9 EDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKY---RGKSRGELPPHVFAIADNAYRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 484 LFREQRPQCFILSGERGSGKSEASKQIIRHLTCRAGASRATldSRFKHVV----CILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:smart00242 86 MLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV--GSVEDQIlesnPILEAFGNAKTLRNNNSSRFGKFIEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 560 QFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ------TIQDDAstg 633
Cdd:smart00242 164 HFDA-KGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQggcltvDGIDDA--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 634 erslnrEKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSA-FVSDLQLLEQVAGMLQVSTDELASAL 712
Cdd:smart00242 240 ------EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 713 TTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQ 792
Cdd:smart00242 314 TKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYF----IGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 793 LCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQS 872
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDW-TFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 873 LLEssNTNAVYSPMKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQ 952
Cdd:smart00242 469 HHK--KHPHFSKPKKKGR---------TEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 953 TGslvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLMDIIGKLQ 1032
Cdd:smart00242 538 AG-------------------SKKR-----------------------------------FQTVGSQFKEQLNELMDTLN 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1033 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCR 1112
Cdd:smart00242 564 STNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTW-PPWGGDAKKACE 642
|
730 740 750
....*....|....*....|....*....|...
gi 62177127 1113 LVLQQCKL--QGWQMGVRKVFLKYWHADQLNDL 1143
Cdd:smart00242 643 ALLQSLGLdeDEYQLGKTKVFLRPGQLAELEEL 675
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
416-1133 |
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: 561.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLY---RGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCeRKQQLTGARIYT 575
Cdd:cd01379 79 SGESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT-STGAVTGARISE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 576 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGL-HLNNLCAHRYLNQTIQDDASTGERSLNREKLAVLKRALNVVGF 654
Cdd:cd01379 158 YLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKyKLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 655 SSLEVENLFVILAAILHLGDIRFTAL----NEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 730
Cdd:cd01379 238 TKEEVDSVYSILAAILHIGDIEFTEVesnhQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 731 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 810
Cdd:cd01379 318 EEATDARDAMAKALYGRLFSWIVNRINSLL-KPDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 811 FLHEQVECVQEGVTMET-AYSpgNQNGVLDFFFQKPSGFLTLLDEESQmiwsvesnFPKKL-QSLLESSNTNA----VYS 884
Cdd:cd01379 397 FAWEQQEYLNEGIDVDLiEYE--DNRPLLDMFLQKPMGLLALLDEESR--------FPKATdQTLVEKFHNNIkskyYWR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 885 PmkdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfk 964
Cdd:cd01379 467 P----------KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 965 frghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRP 1044
Cdd:cd01379 517 --------------------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKP 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1045 NNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtFLREKKEQSAAERCRLVLQQCKLQGWQ 1124
Cdd:cd01379 547 NDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA--FKWNEEVVANRENCRLILERLKLDNWA 624
|
....*....
gi 62177127 1125 MGVRKVFLK 1133
Cdd:cd01379 625 LGKTKVFLK 633
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
404-1133 |
3.89e-166 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 522.61 E-value: 3.89e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 404 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 483
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAY---RGKRRGELPPHIFAIADEAYRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 484 LFREQRPQCFILSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:pfam00063 79 MLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRLEEQILqsnpILEAFGNAKTVRNNNSSRFGKYIEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 560 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSlnr 639
Cdd:pfam00063 159 QF-DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDS--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 640 EKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 719
Cdd:pfam00063 235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 720 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHS-QDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMT 798
Cdd:pfam00063 315 GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASF----IGVLDIYGFEIFEKNSFEQLCINYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 799 NEKMHHYINEVLFLHEQVECVQEGVTmetaYSP---GNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFpkkLQSLLE 875
Cdd:pfam00063 391 NEKLQQFFNHHMFKLEQEEYVREGIE----WTFidfGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTF---LDKLYS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 876 SSNTNAVY-SPMKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtG 954
Cdd:pfam00063 464 TFSKHPHFqKPRLQGE---------THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPD-----Y 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 955 SLVSAYPSFKFRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLMDIIGKLQKC 1034
Cdd:pfam00063 530 ETAESAAANESGKSTPKRTKKKR-----------------------------------FITVGSQFKESLGELMKTLNST 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1035 TPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEqSAAERCRLV 1114
Cdd:pfam00063 575 NPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKG-DAKKGCEAI 653
|
730 740
....*....|....*....|.
gi 62177127 1115 LQQCKLQG--WQMGVRKVFLK 1133
Cdd:pfam00063 654 LQSLNLDKeeYQFGKTKIFFR 674
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
416-1133 |
4.79e-150 |
|
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: 477.90 E-value: 4.79e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLY---RNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASratldSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLTGA 571
Cdd:cd01381 79 SGESGAGKTESTKLILQYLAAISGQH-----SWIEQQILeanpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV-IEGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 572 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNqtiQDDASTGERSLNREKLAVLKRALNV 651
Cdd:cd01381 153 KIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLT---QGNCLTCEGRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 652 VGFSSLEVENLFVILAAILHLGDIRFTALNEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 729
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNldASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 730 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSmQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 809
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDS-SRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 810 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQmiwsvesnFPKKL-QSLLESSN----TNAVYS 884
Cdd:cd01381 389 IFKLEQEEYDKEGINWQHIEFVDNQD-VLDLIALKPMNIMSLIDEESK--------FPKGTdQTMLEKLHsthgNNKNYL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 885 PMKdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsaypsfk 964
Cdd:cd01381 460 KPK--------SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM------------ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 965 frghksallskkmtassiigenknylelskllkkkGTSTflqrleRGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIRP 1044
Cdd:cd01381 520 -----------------------------------GSET------RKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKP 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1045 NNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKE---QSAAERCRLVLQQCKLq 1121
Cdd:cd01381 559 NEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTdcrAATRKICCAVLGGDAD- 637
|
730
....*....|..
gi 62177127 1122 gWQMGVRKVFLK 1133
Cdd:cd01381 638 -YQLGKTKIFLK 648
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
416-1133 |
2.90e-149 |
|
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: 475.33 E-value: 2.90e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVR--SQRPPHLFWIADQAYRRLLETGRNQCILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQLTGARIYT 575
Cdd:cd14897 80 SGESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTE-NGQLLGAKIDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 576 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL---NQTIQDDASTGERSLNREKLAVLKRALNVV 652
Cdd:cd14897 159 YLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILrddNRNRPVFNDSEELEYYRQMFHDLTNIMKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 653 GFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 732
Cdd:cd14897 239 GFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 733 AEFFRDLLAKSLYSRLFSFLVNTMNSCLH-SQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 811
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWpDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 812 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTnavYSPMKDGNg 891
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDD-VLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPR---YVASPGNR- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 892 nvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsaypsfkfrghksa 971
Cdd:cd14897 474 --------VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 972 llskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPD 1051
Cdd:cd14897 521 ---------------------------------------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1052 TFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlrEKKEQSAAERCRLVLQQCKLQGWQMGVRKVF 1131
Cdd:cd14897 556 KFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS--NKVRSDDLGKCQKILKTAGIKGYQFGKTKVF 633
|
..
gi 62177127 1132 LK 1133
Cdd:cd14897 634 LK 635
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
403-1216 |
3.15e-148 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 496.91 E-value: 3.15e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 403 NDDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFH 482
Cdd:COG5022 68 VDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY---SGKNRLELEPHVFAIAEEAYR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 483 QLFREQRPQCFILSGERGSGKSEASKQIIRHLTcRAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFE 558
Cdd:COG5022 145 NLLSEKENQTIIISGESGAGKTENAKRIMQYLA-SVTSSSTVEISSIEKQILatnpILEAFGNAKTVRNDNSSRFGKYIK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 559 LQFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLN 638
Cdd:COG5022 224 IEFDE-NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 639 REKLAvlkRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFvSDLQLLEQVAGMLQVSTDELASALTTDIQY 718
Cdd:COG5022 303 FKITL---DALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIF-SDNSVLDKACYLLGIDPSLFVKWLVKRQIK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 719 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL-HSQDEQKSmqtldIGILDIFGFEEFQKNEFEQLCVNM 797
Cdd:COG5022 379 TGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLdHSAAASNF-----IGVLDIYGFEIFEKNSFEQLCINY 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 798 TNEKMHHYINEVLFLHEQVECVQEGVtmetAYSP----GNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSL 873
Cdd:COG5022 454 TNEKLQQFFNQHMFKLEQEEYVKEGI----EWSFidyfDNQPCIDLIEKKNPLGILSLLDEECVMPHATDESFTSKLAQR 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 874 LeSSNTNAVYSPMKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsqt 953
Cdd:COG5022 530 L-NKNSNPKFKKSRFRD---------NKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE---- 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 954 gslvsaypsfkfrghksallskkmtassiigENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQK 1033
Cdd:COG5022 596 -------------------------------ENIE--------------------SKGRFPTLGSRFKESLNSLMSTLNS 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1034 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR---EKKEQSAAER 1110
Cdd:COG5022 625 TQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWtgeYTWKEDTKNA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1111 CRLVLQQCKL--QGWQMGVRKVFLKywhADQLNDLCLQ----LQRKIITCQKVIRGFLARQHLLQRISiRQQEVTS-INS 1183
Cdd:COG5022 705 VKSILEELVIdsSKYQIGNTKVFFK---AGVLAALEDMrdakLDNIATRIQRAIRGRYLRRRYLQALK-RIKKIQViQHG 780
|
810 820 830
....*....|....*....|....*....|....
gi 62177127 1184 FLQNTE-DMGLKTYDALVIQNASDIARENDRLRS 1216
Cdd:COG5022 781 FRLRRLvDYELKWRLFIKLQPLLSLLGSRKEYRS 814
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
417-1133 |
1.04e-145 |
|
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: 466.31 E-value: 1.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLF----REQRPQC 492
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKS---SLPPHIFAVADRAYQSMLgrlaRGPKNQC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 493 FILSGERGSGKSEASKQIIRHLT--CRAGASratLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTG 570
Cdd:cd14889 80 IVISGESGAGKTESTKLLLRQIMelCRGNSQ---LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF--RNGHVKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 571 ARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDAstgERSLNREKLAVLKRALN 650
Cdd:cd14889 155 AKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKR---EVQYWKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 651 VVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSaFVSDLQ--LLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRH 728
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAL-KVENDSngWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 729 TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 808
Cdd:cd14889 311 TKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKD-DSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 809 VLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESsntNAVYSpmKD 888
Cdd:cd14889 390 HIFLMEQKEYKKEGIDWKEITYKDNKP-ILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG---NSYYG--KS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 889 GNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfrgh 968
Cdd:cd14889 464 RS-------KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPR--------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 969 ksallSKKMTASSiigenknylelskllkKKGTSTFLQrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSK 1048
Cdd:cd14889 528 -----AKLPQAGS----------------DNFNSTRKQ--------SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVK 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1049 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREKKEQSAAERCRLVLQQCKLQGWQMGVR 1128
Cdd:cd14889 579 VPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKLVGWKCGKT 654
|
....*
gi 62177127 1129 KVFLK 1133
Cdd:cd14889 655 RLFFK 659
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
421-1133 |
2.83e-143 |
|
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: 459.32 E-value: 2.83e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 421 IQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILSGERG 500
Cdd:cd01378 7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESY---RGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 501 SGKSEASKQIIRHLTCRAGASRATLdSRFKHVV----CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYTY 576
Cdd:cd01378 84 AGKTEASKRIMQYIAAVSGGSESEV-ERVKDMLlasnPLLEAFGNAKTLRNDNSSRFGKYMEIQF-DFKGEPVGGHITNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 577 LLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ-------TIQDDAStgerslnrekLAVLKRAL 649
Cdd:cd01378 162 LLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKsgcfdvdGIDDAAD----------FKEVLNAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 650 NVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM---IIR 726
Cdd:cd01378 232 KVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAA-ISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHS-QDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd01378 311 PLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAkSGGKKKV----IGVLDIYGFEIFEKNSFEQFCINYVNEKLQQI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 806 INEVLFLHEQVECVQEGVTMETayspgnqngvLDFFF---------QKPSGFLTLLDEESqmiwsvesNFPKK------L 870
Cdd:cd01378 387 FIELTLKAEQEEYVREGIEWTP----------IKYFNnkiicdlieEKPPGIFAILDDAC--------LTAGDatdqtfL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 871 QSLLESSNTNAVYSPMKDgngnvALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKL 950
Cdd:cd01378 449 QKLNQLFSNHPHFECPSG-----HFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 951 SQTgslvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLMDIIGK 1030
Cdd:cd01378 524 DLD--------------------SKKR-----------------------------------PPTAGTKFKNSANALVET 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1031 LQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtflrekKEQSAA-- 1108
Cdd:cd01378 549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS-------PKTWPAwd 621
|
730 740 750
....*....|....*....|....*....|.
gi 62177127 1109 ----ERCRLVLQQCKLQG--WQMGVRKVFLK 1133
Cdd:cd01378 622 gtwqGGVESILKDLNIPPeeYQMGKTKIFIR 652
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
1221-1568 |
9.10e-142 |
|
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal family of eukaryotic proteins that are substrates of tyrosine kinase in the brain. When first identified, the family members were referred to as unconventional myosin XVI, or Myr 8. However, proteins have now been identified as being integrally involved in neuronal function and morphogenesis. The family is involved in both the activation of phosphoinositide 3-kinase (PI3K) and the recruitment of the downstream effector WAVE complex to the close vicinity of PI3K; it also appears to regulate the brain size and neurite outgrowth in mice.
Pssm-ID: 464717 [Multi-domain] Cd Length: 379 Bit Score: 444.60 E-value: 9.10e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1221 PYHKEKLEVRNMQEEGSKR---------TDDKSGPRHFHPSSMSVCAAVDGLG-QCLVGPSIWSPSLHSVFSMDDSSSLP 1290
Cdd:pfam15439 1 LYRKEKLEKRRRQEEGIKRsgeevagkvRDISSEGRHFRMGFMTMPASQDRLPhPCAAGMSIRSQSLHSVGSGDEDGSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1291 SPRKQPPPKPKRDPNTRLSASYEAVSACLS-AAREAA--NEALARPRPHSDDYStmKKIPPRKPKRSPNTKLSGSYEEIS 1367
Cdd:pfam15439 81 SSRKQPPPKPKRDPSTKLSMSSEAVSAGLSaGAKETPseTEALSKPRPHSDEYS--RKIPPPKPKRSPNTQLSGSFDEIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1368 G--SRPGdarpagapgaaarvltpGTPQCALPPAAP---PGDEDDSEPVYIEMLGHAAR-------PDSPDPGESVYEEM 1435
Cdd:pfam15439 159 ApyIRPH-----------------GLLQRASSSDGPspaPLPDEEEEPVYIEMVGNVLRdfspttpDDDPDQSEAVYEEM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1436 KCCLPDDGGPGAGsfLLHGASPPLL-----HRAPEDE--------AAGPPGDACDIPPPFPNLLPHRPPLLVFPPTPVTC 1502
Cdd:pfam15439 222 KYPLPEDSGAANG--PPPLASSPLLadphsPISPESDsalpssqcATPTKKDLCDIPAPFPNLLPHRPPLLVFPPAPVTC 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62177127 1503 SPASDESPLTPLEVKKLPVLEtNLKYPVQPEgSSPLSPQYSKSQKGDGDRPASPGLALFNGSGRAS 1568
Cdd:pfam15439 300 SPASDESPLTPLEVKKLPVLE-NVSYSKQPA-SSPLSPQESKHQREDKDRPSSPGLAVLTPSGRAR 363
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
416-1133 |
7.13e-141 |
|
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: 452.93 E-value: 7.13e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFsssGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYF---GKRMGALPPHIFALAEAAYTNMQEDGKNQSVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLtcragASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGA 571
Cdd:cd14883 79 SGESGAGKTETTKLILQYL-----CAVTNNHSWVEQQILeantILEAFGNAKTVRNDNSSRFGKFIEVCF-DASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 572 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG--LSAEEKYGLHLNNLCAHRYLNQtiqDDASTGERSLNREKLAVLKRAL 649
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQ---SGCIRIDNINDKKDFDHLRLAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 650 NVVGFSSLEVENLFVILAAILHLGDIRFtALNEGNSA--FVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 727
Cdd:cd14883 230 NVLGIPEEMQEGIFSVLSAILHLGNLTF-EDIDGETGalTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 728 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 807
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRF----IGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 808 EVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNtnavYSPMK 887
Cdd:cd14883 385 HYVFKLEQEEYEKEGINWSHIVFTDNQE-CLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHP----YYEKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 888 DGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLF--QSKLSQTGSLVSAYPSFKF 965
Cdd:cd14883 460 DR------RRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtyPDLLALTGLSISLGGDTTS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 966 RGHKsallSKKMTASSiigenknylelskllkkkgtstflqrlergdpvTIASQLRkSLMDIigkLQKCTPHFIHCIRPN 1045
Cdd:cd14883 534 RGTS----KGKPTVGD---------------------------------TFKHQLQ-SLVDV---LSATQPWYVRCIKPN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEQSAAERCRLVLQQCKLQG--W 1123
Cdd:cd14883 573 SLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCL-DPRARSADHKETCGAVRALMGLGGLPEdeW 651
|
730
....*....|
gi 62177127 1124 QMGVRKVFLK 1133
Cdd:cd14883 652 QVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
418-1133 |
3.18e-135 |
|
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: 436.72 E-value: 3.18e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 418 LYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILS 496
Cdd:cd01384 4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQY---KGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 497 GERGSGKSEASKQIIRHLTCRAGasRATLDSRF--KHVV---CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGA 571
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRSveQQVLesnPLLEAFGNAKTVRNNNSSRFGKFVEIQF-DDAGRISGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 572 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiqdDASTGERSLNREKLAVLKRALNV 651
Cdd:cd01384 158 AIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQS---KCFELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 652 VGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSD---LQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRH 728
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 729 TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 808
Cdd:cd01384 315 DPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRL----IGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 809 VLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLqsllessntnavYSPMKD 888
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEFVDNQD-VLDLIEKKPGGIIALLDEACMFPRSTHETFAQKL------------YQTLKD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 889 GNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKD---SLSQNLLfvmKTSENVVINHLFQSKLSQTGSlvsayPSFKF 965
Cdd:cd01384 458 HKRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKDyvvAEHQALL---NASKCPFVAGLFPPLPREGTS-----SSSKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 966 rghksallskkmtaSSiigenknylelskllkkkgtstflqrlergdpvtIASQLRKSLMDIIGKLQKCTPHFIHCIRPN 1045
Cdd:cd01384 530 --------------SS----------------------------------IGSRFKQQLQELMETLNTTEPHYIRCIKPN 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAerCRLVLQQCKLQGWQM 1125
Cdd:cd01384 562 NLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAA--CKKILEKAGLKGYQI 639
|
....*...
gi 62177127 1126 GVRKVFLK 1133
Cdd:cd01384 640 GKTKVFLR 647
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
415-1133 |
3.55e-135 |
|
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: 438.35 E-value: 3.55e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSsgKLcSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNR--RL-GKLPPHIFAIADVAYHAMLRKKKNQCIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTC------RAGASRATLDSRfkhvvCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQL 568
Cdd:cd01385 78 ISGESGSGKTESTNFLLHHLTAlsqkgyGSGVEQTILGAG-----PVLEAFGNAKTAHNNNSSRFGKFIQVNYRE-NGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 569 TGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiqdDASTGERSLNREKLAVLKRA 648
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQS---DCYTLEGEDEKYEFERLKQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 649 LNVVGFSSLEVENLFVILAAILHLGDIRFT--ALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 726
Cdd:cd01385 229 MEMVGFLPETQRQIFSVLSAVLHLGNIEYKkkAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLIL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 806
Cdd:cd01385 309 PYKLPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 807 NEVLFLHEQVECVQEGVTMETAYSPGNqNGVLDFFFQKPSGFLTLLDEesqmiwsvESNFPKKL-QSLLESSNTNAVYSP 885
Cdd:cd01385 389 NQHIFKLEQEEYKKEGISWHNIEYTDN-TGCLQLISKKPTGLLCLLDE--------ESNFPGATnQTLLAKFKQQHKDNK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 886 MKDGNgnvALKDhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgSLVSAYPSFKF 965
Cdd:cd01385 460 YYEKP---QVME--PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVR-----------ELIGIDPVAVF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 966 RghkSALLS---KKMTASSIIGEN--KNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLMDIIGKLQKCTPHFIH 1040
Cdd:cd01385 524 R---WAVLRaffRAMAAFREAGRRraQRTAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIR 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1041 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKpladtFLREKKEQSAAERCRLVLQQCKL 1120
Cdd:cd01385 601 CIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQ-----VLLPKGLISSKEDIKDFLEKLNL 675
|
730
....*....|....*
gi 62177127 1121 Q--GWQMGVRKVFLK 1133
Cdd:cd01385 676 DrdNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
416-1133 |
6.81e-135 |
|
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: 436.49 E-value: 6.81e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQY---SGRALGELPPHLFAIANLAFAKMLDAKQNQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARIYT 575
Cdd:cd01387 79 SGESGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF--EGGVIVGAITSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 576 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiQDDASTGERSlnREKLAVLKRALNVVGFS 655
Cdd:cd01387 157 YLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQG-GNCEIAGKSD--ADDFRRLLAAMQVLGFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 656 SLEVENLFVILAAILHLGDIRF-----TALNEGNSaFVSDLQLlEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 730
Cdd:cd01387 234 SEEQDSIFRILASVLHLGNVYFhkrqlRHGQEGVS-VGSDAEI-QWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 731 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQksmqTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 810
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQD----TLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 811 FLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEesqmiwsvESNFPKKLQ-SLLESSN----TNAVYSP 885
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAFADNQP-VINLISKKPVGILHILDD--------ECNFPQATDhSFLEKCHyhhaLNELYSK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 886 MKDGngnvalkdhGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsaypsfkf 965
Cdd:cd01387 459 PRMP---------LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQ------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 966 rgHKSALLSKkmtassiigenknylelskllkkkGTSTFLQRLERGDpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPN 1045
Cdd:cd01387 517 --TDKAPPRL------------------------GKGRFVTMKPRTP--TVAARFQDSLLQLLEKMERCNPWFVRCLKPN 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKLQG-WQ 1124
Cdd:cd01387 569 HKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPKDmYR 648
|
....*....
gi 62177127 1125 MGVRKVFLK 1133
Cdd:cd01387 649 LGATKVFLR 657
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
416-1133 |
3.23e-132 |
|
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: 428.66 E-value: 3.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLcsSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY---RQKL--LDSPHVYAVADTAYREMMRDEINQSIII 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASRAtLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 575
Cdd:cd01383 77 SGESGAGKTETAKIAMQYLAALGGGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHF-DAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 576 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ----TIQ--DDAstgerslnrEKLAVLKRAL 649
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQsnclTIDgvDDA---------KKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 650 NVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 729
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 730 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 809
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRS---ISILDIYGFESFQKNSFEQLCINYANERLQQHFNRH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 810 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLessNTNAVYSpmkdg 889
Cdd:cd01383 383 LFKLEQEEYELDGIDWTKVDFEDNQE-CLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHL---KSNSCFK----- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 890 ngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSEnvviNHLFQsklsqtgslvsaypsfkfrghk 969
Cdd:cd01383 454 ------GERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCS----CQLPQ---------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 970 saLLSKKMTassiigenkNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKL 1049
Cdd:cd01383 502 --LFASKML---------DASRKALPLTKASGSDSQKQ-------SVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQL 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1050 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKpladtFLREKKE---QSAAERCRLVLQQCKLQG--WQ 1124
Cdd:cd01383 564 PGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYG-----FLLPEDVsasQDPLSTSVAILQQFNILPemYQ 638
|
....*....
gi 62177127 1125 MGVRKVFLK 1133
Cdd:cd01383 639 VGYTKLFFR 647
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
416-1133 |
6.30e-130 |
|
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: 421.56 E-value: 6.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd01380 2 AVLHNLKVRFCQrNAIYTYCGIVLVAINPYEDLPIYGEDIIQAY---SGQNMGELDPHIFAIAEEAYRQMARDEKNQSII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTcRAGASRATLDSRFKHVVC---ILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGA 571
Cdd:cd01380 79 VSGESGAGKTVSAKYAMRYFA-TVGGSSSGETQVEEKVLAsnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKN-YRIIGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 572 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ----TIQ--DDAstgerslnrEKLAVL 645
Cdd:cd01380 157 NMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQggspVIDgvDDA---------AEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 646 KRALNVVGFSSLEVENLFVILAAILHLGDIRFTAlNEGNSAFVS-DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 724
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKA-TRNDSASISpDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 725 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 804
Cdd:cd01380 307 VKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHSF--IGVLDIYGFETFEVNSFEQFCINYANEKLQQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 805 YINEVLFLHEQVECVQEGVTMETAYSPGNQnGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL-QSLLESSntNAVY 883
Cdd:cd01380 385 QFNQHVFKLEQEEYVKEEIEWSFIDFYDNQ-PCID-LIEGKLGILDLLDEECRLPKGSDENWAQKLyNQHLKKP--NKHF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 884 SPMKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvvinhlfqsklsqtgslvsaypsf 963
Cdd:cd01380 461 KKPRFSN---------TAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN------------------------ 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 964 kfrgHKSallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIR 1043
Cdd:cd01380 508 ----RKK--------------------------------------------TVGSQFRDSLILLMETLNSTTPHYVRCIK 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1044 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA---DTFLREKKEQSAAERCRLVLQQCKl 1120
Cdd:cd01380 540 PNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLpskEWLRDDKKKTCENILENLILDPDK- 618
|
730
....*....|...
gi 62177127 1121 qgWQMGVRKVFLK 1133
Cdd:cd01380 619 --YQFGKTKIFFR 629
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
415-1133 |
9.47e-128 |
|
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: 416.12 E-value: 9.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCF 493
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQY---SRRHLGELPPHIFAIANECYRCLWKRHDNQCI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 494 ILSGERGSGKSEASKQIIRHLTC----RAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQFCErK 565
Cdd:cd14873 78 LISGESGAGKTESTKLILKFLSVisqqSLELSLKEKTSCVEQAILesspIMEAFGNAKTVYNNNSSRFGKFVQLNICQ-K 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 566 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQT--IQDDASTGERSLNRekla 643
Cdd:cd14873 157 GNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSgcVEDKTISDQESFRE---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 644 VLKrALNVVGFSSLEVENLFVILAAILHLGDIRFtaLNEGnSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 723
Cdd:cd14873 233 VIT-AMEVMQFSKEEVREVSRLLAGILHLGNIEF--ITAG-GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 724 IIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSmqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 803
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKS-----IGILDIFGFENFEVNHFEQFNINYANEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 804 HYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSlLESSNTNAVY 883
Cdd:cd14873 384 EYFNKHIFSLEQLEYSREGLVWEDIDWIDNGE-CLD-LIEKKLGLLALINEESHFPQATDSTLLEKLHS-QHANNHFYVK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 884 SPMKDGNgnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvsaypsf 963
Cdd:cd14873 461 PRVAVNN-----------FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQ-------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 964 kfrghksallSKKMTASsiigenknylelskllkkkgtstflqrlERGDPvTIASQLRKSLMDIIGKLQKCTPHFIHCIR 1043
Cdd:cd14873 522 ----------DTLKCGS----------------------------KHRRP-TVSSQFKDSLHSLMATLSSSNPFFVRCIK 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1044 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlreKKEQSAAERCRLVLQQCKLQG- 1122
Cdd:cd14873 563 PNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL---ALPEDVRGKCTSLLQLYDASNs 639
|
730
....*....|..
gi 62177127 1123 -WQMGVRKVFLK 1133
Cdd:cd14873 640 eWQLGKTKVFLR 651
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
415-1126 |
2.13e-125 |
|
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: 409.17 E-value: 2.13e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPK---EMPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGaSRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 574
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAG-STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF-DNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 575 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLhlNNLCAHRYLNQTIQDDASTGERSLNREKLavlKRALNVVGF 654
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLSLSGCIEVEGVDDVADFEEV---VLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 655 SSLEVENLFVILAAILHLGDIRFTAL---NEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG--DMIIRRHT 729
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGggkSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcdPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 730 IQiAEFFRDLLAKSLYSRLFSFLVNTMNSclhSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 809
Cdd:cd14872 311 AQ-ATDACDALAKAAYSRLFDWLVKKINE---SMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 810 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQsllessNTNAVYSPMKDG 889
Cdd:cd14872 387 TFKLEEALYQSEGVKFEHIDFIDNQP-VLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAAN------QTHAAKSTFVYA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 890 NgnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsayPSFKFRghk 969
Cdd:cd14872 460 E----VRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------PPSEGD--- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 970 sallskkmtassiigenknylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKL 1049
Cdd:cd14872 519 ---------------------------------------QKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1050 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-ADTFLREKKeqSAAERCRLVLQ---QCKlQGWQM 1125
Cdd:cd14872 560 ARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLvKTIAKRVGP--DDRQRCDLLLKslkQDF-SKVQV 636
|
.
gi 62177127 1126 G 1126
Cdd:cd14872 637 G 637
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
416-1133 |
1.35e-123 |
|
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: 404.92 E-value: 1.35e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKY---KGKRREEMPPHIFAIADNAYRNMLQDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVC---------ILEAFGHAKTTLNDLSSCFIKYFELQFCErKQ 566
Cdd:cd01377 79 TGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLedqilqanpILEAFGNAKTVRNNNSSRFGKFIRIHFGS-TG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 567 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ----TI--QDDAstgerslnrE 640
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgelTIdgVDDA---------E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 641 KLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIqyFK 720
Cdd:cd01377 229 EFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPR--IK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 721 -GDMIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 798
Cdd:cd01377 307 vGREWVTKGqNKEQVVFSVGALAKALYERLFLWLVKRINKTL----DTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 799 NEKMHHYINEVLFLHEQVECVQEGVTMEtayspgnqngVLDF---------FFQKPS-GFLTLLDEESQMIWSVESNFPK 868
Cdd:cd01377 383 NEKLQQFFNHHMFVLEQEEYKKEGIEWT----------FIDFgldlqptidLIEKPNmGILSILDEECVFPKATDKTFVE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 869 KLQSLLESSNTNAVYSPMKDGngnvalKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS 948
Cdd:cd01377 453 KLYSNHLGKSKNFKKPKPKKS------EAH---FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKD 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 949 KLSQTGSlvsaypSFKFRGHKSALLskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDII 1028
Cdd:cd01377 524 YEESGGG------GGKKKKKGGSFR-----------------------------------------TVSQLHKEQLNKLM 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1029 GKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAA 1108
Cdd:cd01377 557 TTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKA 636
|
730 740
....*....|....*....|....*..
gi 62177127 1109 ErCRLVLQQCKL--QGWQMGVRKVFLK 1133
Cdd:cd01377 637 A-CEKILKALQLdpELYRIGNTKVFFK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
416-1133 |
1.65e-121 |
|
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: 399.07 E-value: 1.65e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcsSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSI----SKSPHVFSTASSAYQGMCNNKKSQTIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCrAGAS----RATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQ---- 566
Cdd:cd14888 78 ISGESGAGKTESTKYVMKFLAC-AGSEdikkRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKSkrms 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 567 ----QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHL--NNLCAHR-YLNQTIQDDASTGERSLNR 639
Cdd:cd14888 157 gdrgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYeeNDEKLAKgADAKPISIDMSSFEPHLKF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 640 EKLAV--------------LKR---ALNVVGFSSLEVENLFVILAAILHLGDIRFTAlNEGNS--AFVSDLQL--LEQVA 698
Cdd:cd14888 237 RYLTKsschelpdvddleeFEStlyAMQTVGISPEEQNQIFSIVAAILYLGNILFEN-NEACSegAVVSASCTddLEKVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 699 GMLQVSTDELASALTTDiqyfkgdMIIRRH-------TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSclhSQDEQKSMQT 771
Cdd:cd14888 316 SLLGVDAEDLLNALCYR-------TIKTAHefytkplRVDEAEDVRDALARALYSCLFDKVVERTNE---SIGYSKDNSL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 772 LDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTL 851
Cdd:cd14888 386 LFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCV-DLLQEKPLGIFCM 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 852 LDEESQmiwsvesnFPK-KLQSLlessnTNAVYSPMKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNL 930
Cdd:cd14888 465 LDEECF--------VPGgKDQGL-----CNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 931 LFVMKTSENVVINHLFQSKLSqtgslvsaypsfkfRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrler 1010
Cdd:cd14888 532 QEVIKNSKNPFISNLFSAYLR--------------RGTDGNTKKKKF--------------------------------- 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1011 gdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSR 1090
Cdd:cd14888 565 ---VTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYND 641
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 62177127 1091 YKPLADTFLREkkeqsaaercrlvlqqcKLQGWQMGVRKVFLK 1133
Cdd:cd14888 642 YRILLNGEGKK-----------------QLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
417-1091 |
4.07e-118 |
|
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: 389.78 E-value: 4.07e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFS-----SSGKLCSSLPPHLFSCVERAFHQLFREQRP 490
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiiqnGEYFDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 491 QCFILSGERGSGKSEASKQIIRHLT-------------------CRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSS 551
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTqlsqqeqnseevltltssiRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 552 CFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAE--EKYGLhLNNLCAHR--YLNQTIQ 627
Cdd:cd14907 163 RFGKYVSILVDKKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQllQQLGL-KNQLSGDRydYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 628 DDASTgersLNREKL-AVLKRALNVVGFSSLEVENLFVILAAILHLGDIRF--TALNEGNSAFVSDLQLLEQVAGMLQVS 704
Cdd:cd14907 242 YEVDT----INDEKLfKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVKNKETLQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 705 TDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSM----QTLDIGILDIF 780
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQQlfqnKYLSIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 781 GFEEFQKNEFEQLCVNMTNEKMHH-YINEVlFLHEQVECVQEGVT---METAYsPGNQNgVLDFFFQKPSGFLTLLDEES 856
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQlYISYV-FKAEEQEFKEEGLEdylNQLSY-TDNQD-VIDLLDKPPIGIFNLLDDSC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 857 QMIWSVESNFPKKLQSLLESSNTNAVYSPMKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKT 936
Cdd:cd14907 475 KLATGTDEKLLNKIKKQHKNNSKLIFPNKINK-----------DTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQN 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 937 SENVVINHLF----QSKLSQTGSLVSAYPSFKFRGHKsalLSKKMtassiigenknylelskllkkkgtstflqrlergd 1012
Cdd:cd14907 544 SKNRIISSIFsgedGSQQQNQSKQKKSQKKDKFLGSK---FRNQM----------------------------------- 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62177127 1013 pvtiasqlrKSLMDiigKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1091
Cdd:cd14907 586 ---------KQLMN---ELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQY 652
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
417-1133 |
1.41e-116 |
|
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: 384.88 E-value: 1.41e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFR----EQRPQC 492
Cdd:cd14892 3 LLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASSPPPHVFSIAERAYRAMKGvgkgQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 493 FILSGERGSGKSEASKQIIRHLTC----RAGASR----ATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQ 560
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLATasklAKGASTskgaANAHESIEECVLlsnlILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 561 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQtiqDDASTGERSLNRE 640
Cdd:cd14892 163 Y-NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQ---GNCVEVDGVDDAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 641 KLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFT--ALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTD-IQ 717
Cdd:cd14892 239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEenADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQtTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 718 YFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSClHSQDEQKSMQTLD-------IGILDIFGFEEFQKNEF 790
Cdd:cd14892 319 TARGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAC-HKQQTSGVTGGAAsptfspfIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 791 EQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQNG-VLDFFFQKPSGFLTLLDEesQMIWSVESNfPKK 869
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGI--DVSAIEFQDNQdCLDLIQKKPLGLLPLLEE--QMLLKRKTT-DKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 870 LQSLLESSN--TNAVYSPMKDGNgnvalkDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSEnvvinhlfq 947
Cdd:cd14892 473 LLTIYHQTHldKHPHYAKPRFEC------DE---FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS--------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 948 sklsqtgslvsaypsfKFRghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLrKSLMDI 1027
Cdd:cd14892 535 ----------------KFR---------------------------------------------------TQL-AELMEV 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1028 igkLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA------DTFLRE 1101
Cdd:cd14892 547 ---LWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvAASPDA 623
|
730 740 750
....*....|....*....|....*....|...
gi 62177127 1102 KKEQSAAERCR-LVLQQCKLQGWQMGVRKVFLK 1133
Cdd:cd14892 624 CDATTARKKCEeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
416-1133 |
7.94e-116 |
|
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: 382.97 E-value: 7.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRP---- 490
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLY---HGTTAGELPPHVFAIADHAYTQLIQSGVLdpsn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 491 QCFILSGERGSGKSEASKQIIRHLT--------CRAGASRATLDSRFKHVVC----------ILEAFGHAKTTLNDLSSC 552
Cdd:cd14890 79 QSIIISGESGAGKTEATKIIMQYLAritsgfaqGASGEGEAASEAIEQTLGSledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 553 FIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAH-RYLNQTIQ---- 627
Cdd:cd14890 159 FGKFIEIQF-DHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYfYLRGECSSipsc 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 628 DDAstgerslnrEKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEG-NSAFVSDLQLLEQVAGMLQVSTD 706
Cdd:cd14890 238 DDA---------KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTtVLEDATTLQSLKLAAELLGVNED 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 707 ELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQ 786
Cdd:cd14890 309 ALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTI----SSPDDKWGFIGVLDIYGFEKFE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 787 KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQN-GVLDFFFQKPSG----FLTLLDeesqmIW- 860
Cdd:cd14890 385 WNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGI--DWQYITFNDNqACLELIEGKVNGkpgiFITLDD-----CWr 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 861 --SVESNfpKKLQSLLESSntnavYSPMKDGNGNVALK-----------DHGTAFTIMHYAGRVMYDVVGAIEKNKDSLS 927
Cdd:cd14890 458 fkGEEAN--KKFVSQLHAS-----FGRKSGSGGTRRGSsqhphfvhpkfDADKQFGIKHYAGDVIYDASGFNEKNNETLN 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 928 QNLLFVMKTSEnvvinhlfqsklsqtgslvsaypsfkfrghksallskkmtaSSIigenknylelskllkkkgtstflqr 1007
Cdd:cd14890 531 AEMKELIKQSR-----------------------------------------RSI------------------------- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1008 leRGdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDF 1087
Cdd:cd14890 545 --RE--VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSF 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 62177127 1088 LSRYKPLADTflREKKEQsaaercrLVLQQCKLQG-----WQMGVRKVFLK 1133
Cdd:cd14890 621 FYDFQVLLPT--AENIEQ-------LVAVLSKMLGlgkadWQIGSSKIFLK 662
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
416-1133 |
1.23e-113 |
|
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: 376.04 E-value: 1.23e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14896 2 SVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASY---HPRKALNTTPHIFAIAASAYRLSQSTGQDQCILL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTC----RAGASRATLDSrfkhVVCILEAFGHAKTTLNDLSSCFIKYFELqfCERKQQLTGA 571
Cdd:cd14896 79 SGHSGSGKTEAAKKIVQFLSSlyqdQTEDRLRQPED----VLPILESFGHAKTILNANASRFGQVLRL--HLQHGVIVGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 572 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSlnrEKLAVLKRALNV 651
Cdd:cd14896 153 SVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDA---QDFEGLLKALQG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 652 VGFSSLEVENLFVILAAILHLGDIRFTAlNEGNS---AFVSDLQLLEQVAGMLQVSTDELASALT---TDIQYfkgDMII 725
Cdd:cd14896 230 LGLCAEELTAIWAVLAAILQLGNICFSS-SERESqevAAVSSWAEIHTAARLLQVPPERLEGAVThrvTETPY---GRVS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 726 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd14896 306 RPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDAT--IGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFpkkLQSLLESSNTNAVYSP 885
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIPQPPRES-CLDLLVDQPHSLLSILDDQTWLSQATDHTF---LQKCHYHHGDHPSYAK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 886 MKdgngnVALKdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkf 965
Cdd:cd14896 460 PQ-----LPLP----VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYG----------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 966 rghksallskkmtassiigenknylelskllkkkgtstflqrLERGDPvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPN 1045
Cdd:cd14896 520 ------------------------------------------LGQGKP-TLASRFQQSLGDLTARLGRSHVYFIHCLNPN 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADtflREKKEQSAAERCRLVLQQckLQG--- 1122
Cdd:cd14896 557 PGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS---ERQEALSDRERCGAILSQ--VLGaes 631
|
730
....*....|...
gi 62177127 1123 --WQMGVRKVFLK 1133
Cdd:cd14896 632 plYHLGATKVLLK 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
416-1133 |
2.86e-113 |
|
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: 375.65 E-value: 2.86e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLcsSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14903 2 AILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKE--ELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 575
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIAGGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF-DKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 576 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAH--RYLNQTIQDDAstgerslNREKLAVLKRALNVVG 653
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYtgANKTIKIEGMS-------DRKHFARTKEALSLIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 654 FSSLEVENLFVILAAILHLGDIRFTA--LNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQ 731
Cdd:cd14903 232 VSEEKQEVLFEVLAGILHLGQLQIQSkpNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 732 IAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 811
Cdd:cd14903 312 QAEDCRDALAKAIYSNVFDWLVATINASL----GNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 812 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKpSGFLTLLDEESQMIWSVESNFPKKLQSLLEsSNTNAVYSPmkdgng 891
Cdd:cd14903 388 KTVQIEYEEEGIRWAHIDFADNQD-VLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHK-DEQDVIEFP------ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 892 nvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKSA 971
Cdd:cd14903 459 ----RTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 972 LLSKkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPD 1051
Cdd:cd14903 535 LTTT---------------------------------------TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPT 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1052 TFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYkplaDTFLREKKE--QSAAERCRLVLQQCKLQG---WQMG 1126
Cdd:cd14903 576 ELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKF----WLFLPEGRNtdVPVAERCEALMKKLKLESpeqYQMG 651
|
....*..
gi 62177127 1127 VRKVFLK 1133
Cdd:cd14903 652 LTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
415-1092 |
1.29e-109 |
|
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: 364.65 E-value: 1.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCF 493
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSY---QGKSLGTLPPHVFAIADKAYRDMKVLKQSQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 494 ILSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 573
Cdd:cd01382 78 IVSGESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHF-NEKSSVVGGFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 574 YTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLhlnnlcahryLNQTIQDDAstgerslnrEKLAVLKRALNVVG 653
Cdd:cd01382 157 SHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------LKDPLLDDV---------GDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 654 FSSLEVENLFVILAAILHLGDIRFTALNEGNSA----FVSDLQLLEQVAGMLQVSTDELASALTTDIQY-----FKGDMI 724
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgcnvKPKSEQSLEYAAELLGLDQDELRVSLTTRVMQttrggAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 725 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQdeqKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 804
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE---TSSYF--IGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 805 YINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFpkklqsllessnTNAVYS 884
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEYVDNQD-CIDLIEAKLVGILDLLDEESKLPKPSDQHF------------TSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 885 PMKDgNGNVA------LKDHGT-----AFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 953
Cdd:cd01382 440 KHKN-HFRLSiprkskLKIHRNlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNN 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 954 GSLVSAypsfkfrghksallSKKMTASSIigenknylelskllkkkgTSTFlqrlergdpvtiASQLrKSLMDiigKLQK 1033
Cdd:cd01382 519 KDSKQK--------------AGKLSFISV------------------GNKF------------KTQL-NLLMD---KLRS 550
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 62177127 1034 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYK 1092
Cdd:cd01382 551 TGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYK 609
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
416-1133 |
1.82e-109 |
|
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: 366.20 E-value: 1.82e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvsQLY----FSSSGKLCSSLPPHLFSCVERAFHQLFRE---- 487
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYdlhkYREEMPGWTALPPHVFSIAEGAYRSLRRRlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 488 ---QRPQCFILSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVC---------ILEAFGHAKTTLNDLSSCFIK 555
Cdd:cd14895 75 gasKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISgsellsanpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 556 Y----FELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAH--RYLNQTIQDD 629
Cdd:cd14895 155 FvrmfFEGHELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQefQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 630 ASTGERslNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGN---------------SAFVSDL--- 691
Cdd:cd14895 235 RNDGVR--DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLtvq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 692 QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL----HSQDEQK 767
Cdd:cd14895 313 QHLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqFALNPNK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 768 SMQ---TLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNqNGVLDFFFQ 843
Cdd:cd14895 393 AANkdtTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLqYQFIQDIL-LTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 844 KPSGFLTLLDEESQMIWSVESNFPKKL-QSLLESSNTNAVYSPMKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKN 922
Cdd:cd14895 471 RPSGIFSLLDEECVVPKGSDAGFARKLyQRLQEHSNFSASRTDQAD-----------VAFQIHHYAGAVRYQAEGFCEKN 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 923 KDSLSQNLLFVMKTSENVVINHLFQS-KLSQTGSLVSAYPsfKFRGHKSALLSkkmtassiigenknylelskllkkkgt 1001
Cdd:cd14895 540 KDQPNAELFSVLGKTSDAHLRELFEFfKASESAELSLGQP--KLRRRSSVLSS--------------------------- 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1002 stflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVR 1081
Cdd:cd14895 591 ------------VGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVR 658
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 62177127 1082 LSFSDFLSRYKPLADTflREKKEQSAAErcrlVLQQCKLQGWQMGVRKVFLK 1133
Cdd:cd14895 659 MKHADFVKQYRLLVAA--KNASDATASA----LIETLKVDHAELGKTRVFLR 704
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
416-1132 |
2.20e-107 |
|
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: 358.72 E-value: 2.20e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGK---LCSSLPPHLFSCVERAFHQLFREQRP-- 490
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYEHGERraaGERKLPPHVYAVADKAFRAMLFASRGqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 491 --QCFILSGERGSGKSEASKQIIRHLTC--------RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQ 560
Cdd:cd14901 82 cdQSILVSGESGAGKTETTKIIMNYLASvssatthgQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 561 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGerSLNRE 640
Cdd:cd14901 162 F-ASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDG--VDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 641 KLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAF-VSDLQLLEQVAGMLQVSTDELASALTTDIQYF 719
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFsMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 720 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTN 799
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASRF--IGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 800 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLeSSNT 879
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDA-CVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLL-AKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 880 NAVYSPMKDGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvvinhlfqsklsqtgSLVSA 959
Cdd:cd14901 475 SFSVSKLQQGKRQ---------FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSN---------------AFLSS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 960 YPSFKFRGHKSALLskkmtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrkslmdiiGKLQKCTPHFI 1039
Cdd:cd14901 531 TVVAKFKVQLSSLL-------------------------------------------------------EVLNATEPHFI 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1040 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTfLREKKEQ--SAAERCRLVLQQ 1117
Cdd:cd14901 556 RCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPD-GASDTWKvnELAERLMSQLQH 634
|
730 740
....*....|....*....|
gi 62177127 1118 CKLQG-----WQMGVRKVFL 1132
Cdd:cd14901 635 SELNIehlppFQVGKTKVFL 654
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
416-1091 |
5.82e-105 |
|
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: 351.55 E-value: 5.82e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRD---KLQPHVYATSTAAYKHMLTNEMNQSIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 574
Cdd:cd14904 79 VSGESGAGKTETTKIVMNHLASVAGGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQF-DGRGKLIGAKCE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 575 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIqddASTGERSLNREKL-AVLKRALNVVG 653
Cdd:cd14904 158 TYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSL---AQMQIPGLDDAKLfASTQKSLSLIG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 654 FSSLEVENLFVILAAILHLGDIRFTALNEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 733
Cdd:cd14904 235 LDNDAQRTLFKILSGVLHLGEVMFDKSDENGSR-ISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 734 EFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLH 813
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQ---IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 814 EQVECVQEGVTMETAYSPGNQnGVLDFFFQKpSGFLTLLDEESQMIWSVESNFPKKLQSLLESsntnavyspmKDGNGNV 893
Cdd:cd14904 391 VEEEYIREGLQWDHIEYQDNQ-GIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQT----------KKDNESI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 894 AL-KDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvSAYPSfkfrghksal 972
Cdd:cd14904 459 DFpKVKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---------SEAPS---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 973 lSKKMTASsiiGENKNylelskllkkkgtstflqrlergDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDT 1052
Cdd:cd14904 520 -ETKEGKS---GKGTK-----------------------APKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTE 572
|
650 660 670
....*....|....*....|....*....|....*....
gi 62177127 1053 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1091
Cdd:cd14904 573 FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY 611
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
412-1136 |
4.74e-99 |
|
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: 334.13 E-value: 4.74e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 412 LNDGSLLYEIQKRFGNNQIYTFIGD-ILLLVNPYKELPIYS--SM---VSQLYFSSSGKLcSSLPPHLFSCVERAFHQLF 485
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSdaSLgeyGSEYYDTTSGSK-EPLPPHAYDLAARAYLRMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 486 REQRPQCFILSGERGSGKSEASKQIIRHLTCRAGAS-RAT-LDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCE 563
Cdd:cd14879 80 RRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 564 RKQqLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNN-----LCAHRYLNQTI----QDDAstge 634
Cdd:cd14879 160 RGR-LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDpsdyaLLASYGCHPLPlgpgSDDA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 635 rslnrEKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGN--SAFVSDLQLLEQVAGMLQVSTDELASAL 712
Cdd:cd14879 235 -----EGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGeeSAVVKNTDVLDIVAAFLGVSPEDLETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 713 TTDIQYFKGDmiirRHTI----QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQtldIGILDIFGFEEF--- 785
Cdd:cd14879 310 TYKTKLVRKE----LCTVfldpEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATF---ISLLDFPGFQNRsst 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 786 QKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTM-ETAYsPGNQnGVLDFFFQKPSGFLTLLDEESqmiwsveS 864
Cdd:cd14879 383 GGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVpATSY-FDNS-DCVRLLRGKPGGLLGILDDQT-------R 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 865 NFPKKL-QSLLES-SNTNAVYSPMKDGNGNVALKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktsenvvi 942
Cdd:cd14879 454 RMPKKTdEQMLEAlRKRFGNHSSFIAVGNFATRSGSAS-FTVNHYAGEVTYSVEGFLERNGDVLS--------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 943 nhlfqsklsqtGSLVSAypsfkFRGhksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRK 1022
Cdd:cd14879 518 -----------PDFVNL-----LRG-------------------------------------------------ATQLNA 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1023 SLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREK 1102
Cdd:cd14879 533 ALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKST----LRGS 608
|
730 740 750
....*....|....*....|....*....|....*.
gi 62177127 1103 KEQSAAERCRLVLQQCKLQGWqMGVRKVFLKY--WH 1136
Cdd:cd14879 609 AAERIRQCARANGWWEGRDYV-LGNTKVFLSYaaWR 643
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
416-1101 |
2.44e-98 |
|
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: 334.26 E-value: 2.44e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVsqLYFSSSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLI--LNEYKDINQNKSPIPHIYAVALRAYQSMVSEKKNQSII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGASRATL-------DSRFKHVVC---ILEAFGHAKTTLNDLSSCFIKYFELQFCER 564
Cdd:cd14906 80 ISGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnNSIEKDILTsnpILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 565 KQQLTGARIYTYLLEKSRLVSQP-LGQSNFLIFYLLMDGLSAEE--KYGLHlNNLCAHRYLN------QTIQDDASTGER 635
Cdd:cd14906 160 DGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDErsKWGLN-NDPSKYRYLDarddviSSFKSQSSNKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 636 SLNR-----EKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNS-AFVSD--LQLLEQVAGMLQVSTDE 707
Cdd:cd14906 239 NHNNktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKyAYQKDkvTASLESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 708 LASALTTdiQYFK----GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQ-------TLDIGI 776
Cdd:cd14906 319 FKQALLN--RNLKaggrGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAggsnkknNLFIGV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 777 LDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEES 856
Cdd:cd14906 397 LDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKE-CIELIEKKSDGILSLLDDEC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 857 QMiwsvesnfPK-KLQSLLES-----SNTNAVYspmkdgngnVALKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNL 930
Cdd:cd14906 476 IM--------PKgSEQSLLEKynkqyHNTNQYY---------QRTLAKGT-LGIKHFAGDVTYQTDGWLEKNRDSLYSDV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 931 LFVMKTSENVVINHLFQSKLSQTGSlvsaypsfkfrghksalLSKKMTASsiigenknylelskllkkkgtstflqrler 1010
Cdd:cd14906 538 EDLLLASSNFLKKSLFQQQITSTTN-----------------TTKKQTQS------------------------------ 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1011 gdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSR 1090
Cdd:cd14906 571 ---NTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSR 647
|
730
....*....|.
gi 62177127 1091 YKPLADTFLRE 1101
Cdd:cd14906 648 YKCIVDMYNRK 658
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
416-1120 |
2.40e-97 |
|
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: 331.47 E-value: 2.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-----FSSSGKLCSSLPPHLFSCVERAFHQLFREQR 489
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtSTSPVSQLSELPPHVFAIGGKAFGGLLKPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 490 P-QCFILSGERGSGKSEASKQIIRHLTC---------RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:cd14902 82 RnQSILVSGESGSGKTESTKFLMQFLTSvgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 560 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG----------LSAEEKYGLHLNNLCAHRYLNQTIQDD 629
Cdd:cd14902 162 QF-GANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGadktlldllgLQKGGKYELLNSYGPSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 630 AStgerslnREKLAVlkRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAF-VSDLQL--LEQVAGMLQVSTD 706
Cdd:cd14902 241 AQ-------LYVETV--RAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATaVTAASRfhLAKCAELMGVDVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 707 ELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLD-----IGILDIFG 781
Cdd:cd14902 312 KLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSISDEDeelatIGILDIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 782 FEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiws 861
Cdd:cd14902 392 FESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAA-CLALFDDKSNGLFSLLDQECLM--- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 862 vesnfPKKLQsllESSNTNAVYSPMKDGNgnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVV 941
Cdd:cd14902 468 -----PKGSN---QALSTKFYRYHGGLGQ-----------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 942 InhlfqsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKnylelskllkkkgtstflQRLERGDPVTIAS--- 1018
Cdd:cd14902 529 V---------------------------VAIGADENRDSPGADNGA------------------AGRRRYSMLRAPSvsa 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1019 QLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdTF 1098
Cdd:cd14902 564 QFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFK-CF 642
|
730 740
....*....|....*....|..
gi 62177127 1099 LREKKEQSAAERCRLVLQQCKL 1120
Cdd:cd14902 643 LSTRDRAAKMNNHDLAQALVTV 664
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
417-1095 |
2.43e-96 |
|
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: 326.23 E-value: 2.43e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 417 LLYEIQKRFG--NNQIYTFIGDILLLVNPYKELPiySSMVSqLYFSSSGKLCsslPPHLFSCVERAFHQLfREQRP---- 490
Cdd:cd14891 3 ILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP--EPDKS-DYINTPLDPC---PPHPYAIAEMAYQQM-CLGSGrmqn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 491 QCFILSGERGSGKSEASKQIIRHLTCRA------------------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSC 552
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkrKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 553 FIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiqdDAST 632
Cdd:cd14891 156 FGKFMKLQFTKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQS---GCVS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 633 GERSLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRF----TALNEGNSAFVSDLQLLEQVAGMLQVSTDEL 708
Cdd:cd14891 233 DDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 709 ASALTT-DIQYFKGDMIIRRhTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQ- 786
Cdd:cd14891 313 EKVITQrEIVTRGETFTIKR-NAREAVYSRDAIAKSIYERLFLWIVQQINTSL----GHDPDPLPYIGVLDIFGFESFEt 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 787 KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsvesnf 866
Cdd:cd14891 388 KNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRE-CLDLIASKPNGILPLLDNEARN-------- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 867 PK----KLQSLLESSNTNAVYSPMKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLlfvmktsENVVi 942
Cdd:cd14891 459 PNpsdaKLNETLHKTHKRHPCFPRPHP------KDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDF-------EDLL- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 943 nhlfqsklsqtgslvsaypsfkfrgHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrK 1022
Cdd:cd14891 525 -------------------------ASSAKFSDQM--------------------------------------------Q 535
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62177127 1023 SLMDiigKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1095
Cdd:cd14891 536 ELVD---TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVL 605
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
416-1106 |
2.92e-96 |
|
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: 327.25 E-value: 2.92e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFS---------SSGKlcsSLPPHLFSCVERAFHQLFR 486
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQegllrsqgiESPQ---ALGPHVFAIADRSYRQMMS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 487 EQRP-QCFILSGERGSGKSEASKQIIRHLTCRAGAS-----------RATLDSRFKHVVCILEAFGHAKTTLNDLSSCFI 554
Cdd:cd14908 79 EIRAsQSILISGESGAGKTESTKIVMLYLTTLGNGEegapnegeelgKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 555 KYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE--KYGLH---LNNLCAHRYLNQTIQDD 629
Cdd:cd14908 159 KFIELGF-NRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEheKYEFHdgiTGGLQLPNEFHYTGQGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 630 ASTGERSLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAF---VSDLQLLEQVAGMLQVSTD 706
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEiaeEGNEKCLARVAKLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 707 ELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLH--SQDEQKSmqtlDIGILDIFGFEE 784
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRS----SVGVLDIFGFEC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 785 FQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQM-IWSVE 863
Cdd:cd14908 394 FAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQD-CLDTIQAKKKGILTMLDDECRLgIRGSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 864 SNFPKKLqsllessntNAVYSPMKDGNGNVALKDHGTA-------FTIMHYAGRVMYDV-VGAIEKNKDSLSqnllfvmK 935
Cdd:cd14908 473 ANYASRL---------YETYLPEKNQTHSENTRFEATSiqktkliFAVRHFAGQVQYTVeTTFCEKNKDEIP-------L 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 936 TSENvvinhLFQSklsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvt 1015
Cdd:cd14908 537 TADS-----LFES------------------------------------------------------------------- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1016 iASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1095
Cdd:cd14908 545 -GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLL 623
|
730
....*....|.
gi 62177127 1096 DTFLREKKEQS 1106
Cdd:cd14908 624 PLIPEVVLSWS 634
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
416-1133 |
1.22e-95 |
|
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: 325.01 E-value: 1.22e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14929 2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY---KGKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASRA-----TLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLTG 570
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESkkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM-LSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 571 ARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG--------LSAEEKYGLHLnnlCAHRYLNQTIQDDAstgerslnrEKL 642
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGkkelrdllLVSANPSDFHF---CSCGAVAVESLDDA---------EEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 643 AVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 722
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 723 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKM 802
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVL---DAKLSRQFF-IGILDITGFEILDYNSLEQLCINFTNEKL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 803 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSVESNFPKKLqslLESSNTNAV 882
Cdd:cd14929 382 QQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKL---FDNHFGKSV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 883 Y--SPMKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqTGSlvsay 960
Cdd:cd14929 458 HfqKPKPDK------KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIS-TDS----- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 961 psfkfrghksallskkmtaSSIIGENKNylelskllkKKGTSTFLqrlergdpvtIASQLRKSLMDIIGKLQKCTPHFIH 1040
Cdd:cd14929 526 -------------------AIQFGEKKR---------KKGASFQT----------VASLHKENLNKLMTNLKSTAPHFVR 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1041 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKL 1120
Cdd:cd14929 568 CINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEELLGSLEI 647
|
730
....*....|....*
gi 62177127 1121 QG--WQMGVRKVFLK 1133
Cdd:cd14929 648 DHtqYRFGITKVFFK 662
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
404-1171 |
3.31e-94 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 325.45 E-value: 3.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 404 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQ 483
Cdd:PTZ00014 99 GDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDS--DKLPPHVFTTARRALEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 484 LFREQRPQCFILSGERGSGKSEASKQIIRHLtcrAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:PTZ00014 177 LHGVKKSQTIIVSGESGAGKTEATKQIMRYF---ASSKSGNMDLKIQNAIMaanpVLEAFGNAKTIRNNNSSRFGRFMQL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 560 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ------TIqDDASTG 633
Cdd:PTZ00014 254 QL-GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPkcldvpGI-DDVKDF 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 634 ERSLNreklavlkrALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEG---NSAFVSD--LQLLEQVAGMLQVSTDEL 708
Cdd:PTZ00014 332 EEVME---------SFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltDAAAISDesLEVFNEACELLFLDYESL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 709 ASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKN 788
Cdd:PTZ00014 403 KKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVF----IGMLDIFGFEVFKNN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 789 EFEQLCVNMTNEKMH-HYINeVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFP 867
Cdd:PTZ00014 479 SLEQLFINITNEMLQkNFVD-IVFERESKLYKDEGISTEELEYTSNES-VIDLLCGKGKSVLSILEDQCLAPGGTDEKFV 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 868 KKLQSLLESsntNAVYSPMK-DGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLF 946
Cdd:PTZ00014 557 SSCNTNLKN---NPKYKPAKvDSNKN---------FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 947 QSKLSQTGslvsaypsfkfrghksallskKMTASSIIGenknylelskllkkkgtSTFLQRLergdpvtiasqlrKSLMD 1026
Cdd:PTZ00014 625 EGVEVEKG---------------------KLAKGQLIG-----------------SQFLNQL-------------DSLMS 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1027 IIgklQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEQS 1106
Cdd:PTZ00014 654 LI---NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL-DLAVSNDSSLD 729
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62177127 1107 AAERCRLVLQQCKL--QGWQMGVRKVFLKYWHADQLNdlclQLQRKIITCQK--------VIRGFLARQHLLQRI 1171
Cdd:PTZ00014 730 PKEKAEKLLERSGLpkDSYAIGKTMVFLKKDAAKELT----QIQREKLAAWEplvsvleaLILKIKKKRKVRKNI 800
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
416-1102 |
7.31e-91 |
|
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: 309.93 E-value: 7.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS--------LPPHLFSCVERAFHQLFR 486
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYLLSFEARSSStrnkgsdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 487 ----EQRPQCFILSGERGSGKSEASKQIIRHLTcRAGASRA-----------TLDSRFKHVVCILEAFGHAKTTLNDLSS 551
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLA-QAGDNNLaasvsmgkstsGIAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 552 CFIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEkyglhlnnlcahrylnqtiqddas 631
Cdd:cd14900 161 RFGKFIKLHF-TSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAA------------------------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 632 tgersLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGN--SAFVSDL-----QLLEQVAGMLQVS 704
Cdd:cd14900 216 -----RKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrlGQLKSDLapssiWSRDAAATLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 705 TDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLD-IGILDIFGFE 783
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHfIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 784 EFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVE 863
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQD-CVNLISQRPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 864 SNFPKKLQSLLEsSNTNAVYSPMKDGNGnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvin 943
Cdd:cd14900 450 TTLASKLYRACG-SHPRFSASRIQRARG---------LFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------ 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 944 HLFQSKLsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiasQLRKS 1023
Cdd:cd14900 508 DLFVYGL--------------------------------------------------------------------QFKEQ 519
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62177127 1024 LMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREK 1102
Cdd:cd14900 520 LTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRLL 598
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
424-1133 |
1.04e-90 |
|
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: 310.00 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 424 RFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklCSSLPPHLFSCVERAFHQLFREQRPQCFILSGERGSGK 503
Cdd:cd14876 10 RYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPD--LTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 504 SEASKQIIRHLtcrAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGArIYTYLLE 579
Cdd:cd14876 88 TEATKQIMRYF---ASAKSGNMDLRIQTAIMaanpVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS-VVAFLLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 580 KSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREklavLKRALNVVGFSSLEV 659
Cdd:cd14876 164 KSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEE----VLESLKSMGLTEEQI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 660 ENLFVILAAILHLGDIRFTALNEG---NSAFVS--DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 734
Cdd:cd14876 240 DTVFSIVSGVLLLGNVKITGKTEQgvdDAAAISneSLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 735 FFRDLLAKSLYSRLFSFLVNTMNSCLHSQDeqkSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINeVLFLH 813
Cdd:cd14876 320 MLKLSLAKAMYDKLFLWIIRNLNSTIEPPG---GFKNF-MGMLDIFGFEVFKNNSLEQLFINITNEMLQkNFID-IVFER 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 814 EQVECVQEGV-TMETAYSPGNQngVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESsntNAVYSPMK-DGNG 891
Cdd:cd14876 395 ESKLYKDEGIpTAELEYTSNAE--VIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKS---NGKFKPAKvDSNI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 892 NvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkfrghksa 971
Cdd:cd14876 470 N---------FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 972 llskKMTASSIIGenknylelskllkkkgtSTFLQRLErgdpvtiasqlrkSLMDIIGKLQkctPHFIHCIRPNNSKLPD 1051
Cdd:cd14876 524 ----KIAKGSLIG-----------------SQFLKQLE-------------SLMGLINSTE---PHFIRCIKPNETKKPL 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1052 TFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEQSAAERCRLVLQQCKL--QGWQMGVRK 1129
Cdd:cd14876 567 EWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL-DLGIANDKSLDPKVAALKLLESSGLseDEYAIGKTM 645
|
....
gi 62177127 1130 VFLK 1133
Cdd:cd14876 646 VFLK 649
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
416-1133 |
6.22e-90 |
|
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: 308.31 E-value: 6.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14909 2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMY---RGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHL--------TCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQ 567
Cdd:cd14909 79 TGESGAGKTENTKKVIAYFatvgaskkTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP-TGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 568 LTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG-LSAEEKYGLHLNNLCAHRYLNQ---TIQ--DDAstgerslnrEK 641
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGsVPGVKEMCLLSDNIYDYYIVSQgkvTVPnvDDG---------EE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 642 LAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 721
Cdd:cd14909 229 FSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 722 DMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQdeQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEK 801
Cdd:cd14909 309 EFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQ--QKRQHF--IGVLDIAGFEIFEYNGFEQLCINFTNEK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 802 MHHYINEVLFLHEQVECVQEGVtmETAYspgnqngvLDF---------FFQKPSGFLTLLDEESQMIWSVESNFPKKLQS 872
Cdd:cd14909 385 LQQFFNHHMFVLEQEEYKREGI--DWAF--------IDFgmdllacidLIEKPMGILSILEEESMFPKATDQTFSEKLTN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 873 L-LESSNTNAVYSPMKDGNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLS 951
Cdd:cd14909 455 ThLGKSAPFQKPKPPKPGQ-------QAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 952 QTGSLVSAYPSfkfRGHKSALLSkkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKL 1031
Cdd:cd14909 528 QSGGGEQAKGG---RGKKGGGFA----------------------------------------TVSSAYKEQLNSLMTTL 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1032 QKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR-EKKEQSAAER 1110
Cdd:cd14909 565 RSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQgEEDPKKAAEI 644
|
730 740
....*....|....*....|....*
gi 62177127 1111 CrlvLQQCKL--QGWQMGVRKVFLK 1133
Cdd:cd14909 645 I---LESIALdpDQYRLGHTKVFFR 666
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
416-1133 |
1.58e-89 |
|
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: 307.27 E-value: 1.58e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY---KGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLT--------------CRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQF 561
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 562 CErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQ--TIQDDASTGErsln 638
Cdd:cd14927 159 GP-TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQgvTTVDNMDDGE---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 639 reKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 718
Cdd:cd14927 234 --ELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 719 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMT 798
Cdd:cd14927 312 VGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFF----IGVLDIAGFEIFEFNSFEQLCINFT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 799 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLES 876
Cdd:cd14927 388 NEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACID-LIEKPLGILSILEEECMFPKASDASFKAKLydNHLGKS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 877 SNTNavySPMKDGNgnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTgsl 956
Cdd:cd14927 467 PNFQ---KPRPDKK-----RKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSD--- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 957 vSAYPsfkfrgHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpvTIASQLRK-SLMDIIGKLQKCT 1035
Cdd:cd14927 536 -STED------PKSGVKEKRKKAASF--------------------------------QTVSQLHKeNLNKLMTNLRATQ 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1036 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL------ADTFLREKKeqsAAE 1109
Cdd:cd14927 577 PHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILnpsaipDDKFVDSRK---ATE 653
|
730 740
....*....|....*....|....
gi 62177127 1110 RCRLVLQQCKLQgWQMGVRKVFLK 1133
Cdd:cd14927 654 KLLGSLDIDHTQ-YQFGHTKVFFK 676
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
416-1133 |
3.93e-89 |
|
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: 306.14 E-value: 3.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY---KGIKRHEVPPHVFAITDSAYRNMLGDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVC-----------------ILEAFGHAKTTLNDLSSCFIKYFE 558
Cdd:cd14911 79 TGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVNpavligeleqqllqanpILEAFGNAKTVKNDNSSRFGKFIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 559 LQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQ-----DDASTG 633
Cdd:cd14911 159 INF-DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLpvpgvDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 634 ERSLNreklavlkrALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALT 713
Cdd:cd14911 238 QATVK---------SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 714 TDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQL 793
Cdd:cd14911 309 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL---DRTKRQGASFIGILDMAGFEIFELNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 794 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSl 873
Cdd:cd14911 386 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDKLVS- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 874 leSSNTNAVYspMKDGNGNVAlkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqt 953
Cdd:cd14911 464 --AHSMHPKF--MKTDFRGVA------DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD----- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 954 gslvsaypsfkfrghksallskkmtaSSIIGenknylelsKLLKKKGTSTFLQRLERGDPVTIASQLRKSLMDIIGKLQK 1033
Cdd:cd14911 529 --------------------------AEIVG---------MAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRN 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1034 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRL 1113
Cdd:cd14911 574 TNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVI-PKGFMDGKKACEK 652
|
730 740
....*....|....*....|..
gi 62177127 1114 VLQQCKLQG--WQMGVRKVFLK 1133
Cdd:cd14911 653 MIQALELDSnlYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
416-1133 |
6.26e-89 |
|
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: 305.78 E-value: 6.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY---RGKKRHEMPPHIYAISESAYRCMLQDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRA--------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQ 567
Cdd:cd14920 79 TGESGAGKTENTKKVIQYLAHVAsshkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 568 LTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL-NQTIqddASTGERslNREKLAVLK 646
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsNGYI---PIPGQQ--DKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 647 RALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 726
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 806
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 807 NEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSVESNFPKKLQSllESSNTNAVYS 884
Cdd:cd14920 390 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHSKFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 885 PMKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTG-SLVSAYPSF 963
Cdd:cd14920 468 PRQ-------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGlDQVTGMTET 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 964 KFrghKSALLSKKmtassiigenknylelskllkkkgtstflqrlerGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIR 1043
Cdd:cd14920 540 AF---GSAYKTKK----------------------------------GMFRTVGQLYKESLTKLMATLRNTNPNFVRCII 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1044 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQQCKLQG- 1122
Cdd:cd14920 583 PNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACERMIRALELDPn 661
|
730
....*....|..
gi 62177127 1123 -WQMGVRKVFLK 1133
Cdd:cd14920 662 lYRIGQSKIFFR 673
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
416-1133 |
7.06e-88 |
|
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: 302.11 E-value: 7.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLF-REQRPQCF 493
Cdd:cd14875 2 TLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDP--RLLPPHIWQVAHKAFNAIFvQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 494 ILSGERGSGKSEASKQIIRHL-----------TCRAGASRatLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFC 562
Cdd:cd14875 80 VISGESGSGKTENAKMLIAYLgqlsymhssntSQRSIADK--IDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 563 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGL-HLNNLCAHRYLN--QTIQDDASTGERSLNR 639
Cdd:cd14875 158 PTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNggNTFVRRGVDGKTLDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 640 EKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTAlNEGNSAFVSDLQLLEQVAGMLQVSTDELASALttdiqyf 719
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES-DQNDKAQIADETPFLTACRLLQLDPAKLRECF------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 720 kgdmIIRRHT--IQI------AEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTldIGILDIFGFEEFQKNEFE 791
Cdd:cd14875 310 ----LVKSKTslVTIlankteAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGCKY--IGLLDIFGFENFTRNSFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 792 QLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQ 871
Cdd:cd14875 384 QLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECV-NMFDQKRTGIFSMLDEECNFKGGTTERFTTNLW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 872 SllESSNTNAVYSPMKDGNGNvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqskls 951
Cdd:cd14875 463 D--QWANKSPYFVLPKSTIPN--------QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIR-------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 952 qtgSLVSAYPSFKFRGHksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKL 1031
Cdd:cd14875 525 ---TLLSTEKGLARRKQ----------------------------------------------TVAIRFQRQLTDLRTEL 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1032 QKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFlSRY------KPLADTFLREKKEQ 1105
Cdd:cd14875 556 ESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF-CRYfylimpRSTASLFKQEKYSE 634
|
730 740 750
....*....|....*....|....*....|...
gi 62177127 1106 SAaerCRLVLQQCKLQGWQ-----MGVRKVFLK 1133
Cdd:cd14875 635 AA---KDFLAYYQRLYGWAkpnyaVGKTKVFLR 664
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
415-1133 |
1.59e-86 |
|
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: 298.47 E-value: 1.59e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGASRATLDS--------RFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 566
Cdd:cd14921 78 CTGESGAGKTENTKKVIQYLAVVASSHKGKKDTsitgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 567 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLavlk 646
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETL---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 647 RALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 726
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 806
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 807 NEVLFLHEQVECVQEGV-------------TMETAYSPGNqngvldfffqkPSGFLTLLDEESQMIWSVESNFPKKLQSl 873
Cdd:cd14921 390 NHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKSFVEKLCT- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 874 lESSNTNAVYSPMKdgngnvaLKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 953
Cdd:cd14921 458 -EQGNHPKFQKPKQ-------LKDK-TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 954 GSLVSAypsfkfrghksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQK 1033
Cdd:cd14921 529 GLDQMA----------------KMTESSLPSASKT--------------------KKGMFRTVGQLYKEQLGKLMTTLRN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1034 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRL 1113
Cdd:cd14921 573 TTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACIL 651
|
730 740
....*....|....*....|..
gi 62177127 1114 VLQQCKLQG--WQMGVRKVFLK 1133
Cdd:cd14921 652 MIKALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
415-1133 |
4.75e-86 |
|
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: 296.94 E-value: 4.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMY---KGKKRTEMPPHLFSISDNAYHDMLMDRENQSML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGASR------ATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQL 568
Cdd:cd14934 78 ITGESGAGKTENTKKVIQYFANIGGTGKqssdgkGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT-TGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 569 TGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQ--TIQDDASTGErslnreKLAVL 645
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQgvTVVDNMDDGE------ELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 646 KRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 725
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 726 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTL----DTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtnavY 883
Cdd:cd14934 387 FNHHMFVLEQEEYKREGIEWVFIDFGLDLQACID-LLEKPMGIFSILEEQCVFPKATDATFKAALydNHLGKSSN----F 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 884 SPMKDGNGnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvsaypsf 963
Cdd:cd14934 462 LKPKGGKG----KGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGS-------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 964 kfrghksallSKKMTASSIIgenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIR 1043
Cdd:cd14934 530 ----------KKQKRGSSFM-------------------------------TVSNFYREQLNKLMTTLHSTAPHFVRCIV 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1044 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-----ADTFLREKKeqsAAErcrLVLQQC 1118
Cdd:cd14934 569 PNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLnpnviPQGFVDNKK---ASE---LLLGSI 642
|
730
....*....|....*..
gi 62177127 1119 KLQ--GWQMGVRKVFLK 1133
Cdd:cd14934 643 DLDvnEYKIGHTKVFFR 659
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
415-1133 |
1.54e-85 |
|
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: 295.78 E-value: 1.54e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGA------------SRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFc 562
Cdd:cd14932 78 CTGESGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 563 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLnqtiqddaSTGERSL----N 638
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFL--------SNGNVTIpgqqD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 639 REKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 718
Cdd:cd14932 229 KELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 719 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 798
Cdd:cd14932 309 VGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 799 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSVESNFPKKLQSllES 876
Cdd:cd14932 386 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQ--EQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 877 SNTNAVYSPMKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgsl 956
Cdd:cd14932 464 GNNPKFQKPKK-------LKDDAD-FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD-------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 957 vsaypsfkfrghksallskkmtASSIIGENKNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLMDIIGKLQKCTP 1036
Cdd:cd14932 528 ----------------------VDRIVGLDKVAGMGESLHGAFKTRKGMFR-------TVGQLYKEQLMNLMTTLRNTNP 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1037 HFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQ 1116
Cdd:cd14932 579 NFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMVK 657
|
730
....*....|....*....
gi 62177127 1117 QCKLQG--WQMGVRKVFLK 1133
Cdd:cd14932 658 ALELDPnlYRIGQSKVFFR 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
416-1133 |
1.88e-85 |
|
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: 295.42 E-value: 1.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGAS----------RATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERK 565
Cdd:cd14913 79 TGESGAGKTVNTKRVIQYFATIAATGdlakkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 566 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQtiqddastGERSL----NRE 640
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELiELLLITTNPYDYPFISQ--------GEILVasidDAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 641 KLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 720
Cdd:cd14913 230 ELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 721 GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNE 800
Cdd:cd14913 310 NEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF----IGVLDIAGFEIFEYNSLEQLCINFTNE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 801 KMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSN 878
Cdd:cd14913 386 KLQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 879 tnavYSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvs 958
Cdd:cd14913 465 ----FQKPKVVKGRAE-----AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 959 aypsfkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHF 1038
Cdd:cd14913 526 ------FATADADSGKKKVAKKK-------------------GSSFQ---------TVSALFRENLNKLMSNLRTTHPHF 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1039 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQC 1118
Cdd:cd14913 572 VRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASI 651
|
730
....*....|....*..
gi 62177127 1119 KLQ--GWQMGVRKVFLK 1133
Cdd:cd14913 652 DIDhtQYKFGHTKVFFK 668
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
416-1133 |
4.82e-84 |
|
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: 290.49 E-value: 4.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklcSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSR---SDNAPHIFSVADSAYQDMLHHEEPQHIIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLtCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 575
Cdd:cd14882 79 SGESYSGKTTNARLLIKHL-CYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTF-GSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 576 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEK---YGLHLNNlcAHRYLnQTIQDDASTGERSL------NREKLAVLK 646
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlkeYNLKAGR--NYRYL-RIPPEVPPSKLKYRrddpegNVERYKEFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 647 RALNVVGFSSLEVENLFVILAAILHLGDIRFTalnEGN-SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 725
Cdd:cd14882 234 EILKDLDFNEEQLETVRKVLAAILNLGEIRFR---QNGgYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 726 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd14882 311 RKHTTEEARDARDVLASTLYSRLVDWIINRINMKM-SFPRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQmiwsvesnfpkklqsllESSNTNAVYSP 885
Cdd:cd14882 390 YNQRIFISEMLEMEEEDIPTINLRFYDNKTAV-DQLMTKPDGLFYIIDDASR-----------------SCQDQNYIMDR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 886 MKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLVSAYPSFKF 965
Cdd:cd14882 452 IKEKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--SQVRNMRTLAATFRA 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 966 rghkSALLSKKMTAssiIGENknylelskllkKKGTstflqrlergdpvtiasqlrkslmdiigklqkctpHFIHCIRPN 1045
Cdd:cd14882 530 ----TSLELLKMLS---IGAN-----------SGGT-----------------------------------HFVRCIRSD 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlrEKKEQSAAERCRLVLQQCKLQGWQM 1125
Cdd:cd14882 557 LEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDF--DETVEMTKDNCRLLLIRLKMEGWAI 634
|
....*...
gi 62177127 1126 GVRKVFLK 1133
Cdd:cd14882 635 GKTKVFLK 642
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
421-1132 |
1.17e-82 |
|
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: 285.85 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 421 IQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFREQRPQCFILSGERG 500
Cdd:cd14881 7 LQARFYAKEFFTNVGPILLSVNPYRDVG------NPLTLTSTRS--SPLAPQLLKVVQEAVRQQSETGYPQAIILSGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 501 SGKSEASKQIIRHLTCRAGASRATldSRFKHV---VCILEAFGHAKTTLNDLSSCFIKYFELQFCErkQQLTGARIYTYL 577
Cdd:cd14881 79 SGKTYASMLLLRQLFDVAGGGPET--DAFKHLaaaFTVLRSLGSAKTATNSESSRIGHFIEVQVTD--GALYRTKIHCYF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 578 LEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAH--RYLNQ--TIQDDASTGERslnrekLAVLKRALNVVG 653
Cdd:cd14881 155 LDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPAnlRYLSHgdTRQNEAEDAAR------FQAWKACLGILG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 654 FSSLEVENlfvILAAILHLGDIRFTALNEGNSAFVSDLQLlEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 733
Cdd:cd14881 229 IPFLDVVR---VLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 734 EFFRDLLAKSLYSRLFSFLVNTMNSC--LHSQdeqKSMQTLD--IGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 809
Cdd:cd14881 305 NMTRDALAKALYCRTVATIVRRANSLkrLGST---LGTHATDgfIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 810 LFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESnFPKKLQslLESSNTNAVYSPmkdg 889
Cdd:cd14881 382 IFKSSIESCRDEGIQCEVEVDYVDNVPCIDLISSLRTGLLSMLDVECSPRGTAES-YVAKIK--VQHRQNPRLFEA---- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 890 ngnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtsenvvinhlfqsklSQTGslvsaypSFKFRGHk 969
Cdd:cd14881 455 -----KPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY---------------KQNC-------NFGFATH- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 970 sallskkmtassiigenknylelskllkkkgTSTFLQRLErgdpvtiasQLRKSLMdiigklqKCTPHFIHCIRPNNSKL 1049
Cdd:cd14881 507 -------------------------------TQDFHTRLD---------NLLRTLV-------HARPHFVRCIRSNTTET 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1050 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKLQ-------- 1121
Cdd:cd14881 540 PNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILQFLEAQppsklssv 619
|
730
....*....|...
gi 62177127 1122 --GWQMGVRKVFL 1132
Cdd:cd14881 620 stSWALGKRHIFL 632
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
415-1133 |
9.11e-82 |
|
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: 284.68 E-value: 9.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGASRAT-----LDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLT 569
Cdd:cd14919 78 CTGESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 570 GARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLavlkRAL 649
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETM----EAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 650 NVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 729
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 730 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 809
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 810 LFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSVESNFPKKlqsLLESSNTNAVYSPMK 887
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEK---VVQEQGTHPKFQKPK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 888 DgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfrg 967
Cdd:cd14919 467 Q------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVA-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 968 hksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNS 1047
Cdd:cd14919 532 --------GMSETALPGAFKT--------------------RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHE 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1048 KLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQQCKLQG--WQM 1125
Cdd:cd14919 584 KKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRI 662
|
....*...
gi 62177127 1126 GVRKVFLK 1133
Cdd:cd14919 663 GQSKVFFR 670
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
415-1092 |
2.61e-81 |
|
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: 284.68 E-value: 2.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-------FSSSGKLCSSLPPHLFSCVERAFHQLFR 486
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqFGDRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 487 EQRPQCFILSGERGSGKSEASKQIIRHLTCRAG-----------------ASRATLDSRFKHVVCILEAFGHAKTTLNDL 549
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppasPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 550 SSCFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG----LSAEEKYGLHLN-NLCAHRYLNQ 624
Cdd:cd14899 161 SSRFGKFIELRFRDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSgGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 625 TIQDDASTGERslNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEG--NSAFVSDLQLLEQVAG--- 699
Cdd:cd14899 241 SLCSKRRDGVK--DGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKgdDTVFADEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 700 -------MLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQ--------- 763
Cdd:cd14899 319 hftkaaeLLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 764 ----DEQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQnGVLD 839
Cdd:cd14899 399 sdvdDEEDATDF--IGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNR-ACLE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 840 FFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTNAVYSpmkdgngNVALKDHGTAFTIMHYAGRVMYDVVGAI 919
Cdd:cd14899 476 LFEHRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFR-------SAPLIQRTTQFVVAHYAGCVTYTIDGFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 920 EKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKSAllsKKMTASsiigenknylelskllkkk 999
Cdd:cd14899 549 AKNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRA---KSAIAA------------------- 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1000 gtstflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYP 1079
Cdd:cd14899 607 --------------VSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFP 672
|
730
....*....|...
gi 62177127 1080 VRLSFSDFLSRYK 1092
Cdd:cd14899 673 VRLTHKQFLGRYR 685
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
415-1133 |
3.79e-81 |
|
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: 282.73 E-value: 3.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGA------------SRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFc 562
Cdd:cd15896 78 CTGESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 563 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKL 642
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 643 avlkRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 722
Cdd:cd15896 237 ----EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 723 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 802
Cdd:cd15896 313 YVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 803 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSVESNFPKKLqsLLESSNTN 880
Cdd:cd15896 390 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKV--LQEQGTHP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 881 AVYSPMKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsay 960
Cdd:cd15896 468 KFFKPKK-------LKDEAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVG------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 961 psfkfrghksalLSKKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQKCTPHFIH 1040
Cdd:cd15896 534 ------------LDKVSGMSEMPGAFKT--------------------RKGMFRTVGQLYKEQLSKLMATLRNTNPNFVR 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1041 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQQCKL 1120
Cdd:cd15896 582 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMIKSLEL 660
|
730
....*....|....*
gi 62177127 1121 QG--WQMGVRKVFLK 1133
Cdd:cd15896 661 DPnlYRIGQSKVFFR 675
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
416-1133 |
5.10e-81 |
|
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: 282.38 E-value: 5.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAG----------ASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCErK 565
Cdd:cd14917 79 TGESGAGKTVNTKRVIQYFAVIAAigdrskkdqtPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA-T 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 566 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTIQDDASTGERslnrEKLAV 644
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDA----EELMA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 645 LKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 724
Cdd:cd14917 234 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 725 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 804
Cdd:cd14917 314 TKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 805 YINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNTNav 882
Cdd:cd14917 390 FFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLfdNHLGKSNNFQ-- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 883 yspmKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvsayps 962
Cdd:cd14917 467 ----KPRNIKGKPEAH---FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN-------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 963 fkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCI 1042
Cdd:cd14917 526 --YAGADAPIEKGKGKAKK-------------------GSSFQ---------TVSALHRENLNKLMTNLRSTHPHFVRCI 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1043 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKL-- 1120
Cdd:cd14917 576 IPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIdh 655
|
730
....*....|...
gi 62177127 1121 QGWQMGVRKVFLK 1133
Cdd:cd14917 656 NQYKFGHTKVFFK 668
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
415-1133 |
5.22e-80 |
|
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: 279.29 E-value: 5.22e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY---RGKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGASRA--------TLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 566
Cdd:cd14930 78 CTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 567 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLnqTIQDDASTG-ERSLNREKLavl 645
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGqERELFQETL--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 646 kRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 725
Cdd:cd14930 232 -ESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 726 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd14930 311 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASF---LGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSVESNFPKKLQSllESSNTNAVY 883
Cdd:cd14930 388 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQ--EQGGHPKFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 884 SPMKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS-----KLSQTGSLVS 958
Cdd:cd14930 466 RPRH-------LRDQAD-FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGD 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 959 AYPSFKFRghksallskkmtassiigenknylelskllkkkgtstflqrleRGDPVTIASQLRKSLMDIIGKLQKCTPHF 1038
Cdd:cd14930 538 GPPGGRPR-------------------------------------------RGMFRTVGQLYKESLSRLMATLSNTNPSF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1039 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQQC 1118
Cdd:cd14930 575 VRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQAL 653
|
730
....*....|....*..
gi 62177127 1119 KLQG--WQMGVRKVFLK 1133
Cdd:cd14930 654 ELDPnlYRVGQSKIFFR 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
416-1133 |
4.73e-79 |
|
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: 276.61 E-value: 4.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRA------------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcE 563
Cdd:cd14910 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 564 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMdglSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLA 643
Cdd:cd14910 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIM---SNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 644 VLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 723
Cdd:cd14910 235 ATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 724 IIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 803
Cdd:cd14910 315 VTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 804 HYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtna 881
Cdd:cd14910 391 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSNN--- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 882 vYSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYP 961
Cdd:cd14910 467 -FQKPKPAKGKVE-----AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 962 SFKFRGhksallskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHC 1041
Cdd:cd14910 541 GGKKKG----------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPHFVRC 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1042 IRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRLVLQQC 1118
Cdd:cd14910 578 IIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQfidSKKASEKLLGSIDID 657
|
730
....*....|....*
gi 62177127 1119 KLQgWQMGVRKVFLK 1133
Cdd:cd14910 658 HTQ-YKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
416-1133 |
1.91e-78 |
|
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: 274.63 E-value: 1.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTC-----------RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 564
Cdd:cd14916 79 TGESGAGKTVNTKRVIQYFASiaaigdrskkeNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 565 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQTIQDDASTGERslnrEKLA 643
Cdd:cd14916 158 TGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELlDMLLVTNNPYDYAFVSQGEVSVASIDDS----EELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 644 VLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 723
Cdd:cd14916 234 ATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 724 IIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 803
Cdd:cd14916 314 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 804 HYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNTNa 881
Cdd:cd14916 390 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLydNHLGKSNNFQ- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 882 vyspmKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqtgslVSAYP 961
Cdd:cd14916 468 -----KPRNVKGKQEAH---FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS-----ADTGD 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 962 SFKFRGHKSAllskkmtassiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHC 1041
Cdd:cd14916 535 SGKGKGGKKK-----------------------------GSSFQ---------TVSALHRENLNKLMTNLKTTHPHFVRC 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1042 IRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKL- 1120
Cdd:cd14916 577 IIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDId 656
|
730
....*....|....
gi 62177127 1121 -QGWQMGVRKVFLK 1133
Cdd:cd14916 657 hNQYKFGHTKVFFK 670
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
416-1133 |
6.38e-78 |
|
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: 273.14 E-value: 6.38e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRA------------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCE 563
Cdd:cd14915 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 564 rKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQtiqddastGERSL----N 638
Cdd:cd14915 159 -TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELiEMLLITTNPYDFAFVSQ--------GEITVpsidD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 639 REKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 718
Cdd:cd14915 230 QEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 719 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMT 798
Cdd:cd14915 310 VGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 799 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLES 876
Cdd:cd14915 386 NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 877 SNtnavYSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvinHLFQSKLSQTgsl 956
Cdd:cd14915 465 NN----FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVV------------GLYQKSGMKT--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 957 vsayPSFKFRGHKSAllSKKMTASSIIGENKNylelskllkkkgtSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTP 1036
Cdd:cd14915 521 ----LAFLFSGGQTA--EAEGGGGKKGGKKKG-------------SSFQ---------TVSALFRENLNKLMTNLRSTHP 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1037 HFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRL 1113
Cdd:cd14915 573 HFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQfidSKKASEKLLG 652
|
730 740
....*....|....*....|
gi 62177127 1114 VLQQCKLQgWQMGVRKVFLK 1133
Cdd:cd14915 653 SIDIDHTQ-YKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
416-1133 |
7.12e-78 |
|
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: 273.15 E-value: 7.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRA------------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcE 563
Cdd:cd14912 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeitsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 564 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQTIQDDASTGERslnrEKL 642
Cdd:cd14912 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELiEMLLITTNPYDYPFVSQGEISVASIDDQ----EEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 643 AVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 722
Cdd:cd14912 234 MATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 723 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKM 802
Cdd:cd14912 314 YVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 803 HHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtn 880
Cdd:cd14912 390 QQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSAN-- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 881 avYSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLVSAY 960
Cdd:cd14912 467 --FQKPKVVKGKAE-----AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSG--AQTAEGASAG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 961 PSFKFRGHKSAllskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIH 1040
Cdd:cd14912 538 GGAKKGGKKKG------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPHFVR 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1041 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRLVLQQ 1117
Cdd:cd14912 579 CIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQfidSKKASEKLLASIDI 658
|
730
....*....|....*.
gi 62177127 1118 CKLQgWQMGVRKVFLK 1133
Cdd:cd14912 659 DHTQ-YKFGHTKVFFK 673
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
417-1133 |
9.41e-77 |
|
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: 269.68 E-value: 9.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILS 496
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 497 GERGSGKSEASKQIIRHLTC----------RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 566
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATiavtgekkkeESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 567 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMdglSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLAVLK 646
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIT---SNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 647 RALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 726
Cdd:cd14918 236 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 806
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 807 NEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtnavYS 884
Cdd:cd14918 392 NHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLydQHLGKSAN----FQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 885 PMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktseNVVINHLFQSKLSQTGSLVSAYPSFK 964
Cdd:cd14918 467 KPKVVKGKAE-----AHFSLIHYAGTVDYNITGWLDKNKDPLN-----------DTVVGLYQKSAMKTLASLFSTYASAE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 965 frGHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRP 1044
Cdd:cd14918 531 --ADSGAKKGAKKKGSSF-------------------------------QTVSALFRENLNKLMTNLRSTHPHFVRCIIP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1045 NNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRLVLQQCKLQ 1121
Cdd:cd14918 578 NETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQfidSKKASEKLLASIDIDHTQ 657
|
730
....*....|..
gi 62177127 1122 gWQMGVRKVFLK 1133
Cdd:cd14918 658 -YKFGHTKVFFK 668
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
421-1133 |
3.10e-76 |
|
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: 267.52 E-value: 3.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 421 IQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLC--SSLPPHLFSCVERAFHQLFREQRPQCFILSG 497
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSRGfpSDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 498 ERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIYTYL 577
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL-LVGPDGGLKGGKITSYM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 578 LEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGErslNREKLAVLKRALNVVgFSSL 657
Cdd:cd14886 166 LELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGID---DQKEFAPVRSQLEKL-FSKN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 658 EVENLFVILAAILHLGDIRF---TALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 734
Cdd:cd14886 242 EIDSFYKCISGILLAGNIEFseeGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 735 FFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVlFLH 813
Cdd:cd14886 322 VNIRAVAKDLYGALFELCVDTLNEIIQFDADARPW----IGILDIYGFEFFERNTYEQLLINYANERLQqYFINQV-FKS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 814 EQVECVQEGVTMETAYSPGNQNGVLdfFFQKPS-GFLTLLDEESQmiwsVESNFPKKLQSLLESSNTNAVYSPMKDGNGN 892
Cdd:cd14886 397 EIQEYEIEGIDHSMITFTDNSNVLA--VFDKPNlSIFSFLEEQCL----IQTGSSEKFTSSCKSKIKNNSFIPGKGSQCN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 893 valkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgslvsaypsfkfrghksal 972
Cdd:cd14886 471 ---------FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN----------------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 973 lskkMTASSIIGENKNYLelskllkkkgtSTFLqrlergdpvtiASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDT 1052
Cdd:cd14886 513 ----KAFSDIPNEDGNMK-----------GKFL-----------GSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1053 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL---ADTFLREKKEQSAAERCRLVLQQCKLQGWQMGVRK 1129
Cdd:cd14886 567 YETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTK 646
|
....
gi 62177127 1130 VFLK 1133
Cdd:cd14886 647 VFLR 650
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
416-1133 |
3.51e-75 |
|
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: 265.01 E-value: 3.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRA-----------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 564
Cdd:cd14923 79 TGESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 565 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEkygLHLNNLCAHRYLNQTIQDDASTGERSLNREKLAV 644
Cdd:cd14923 158 TGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL---IDLLLISTNPFDFPFVSQGEVTVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 645 LKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 724
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 725 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 804
Cdd:cd14923 315 TKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 805 YINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtnav 882
Cdd:cd14923 391 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN---- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 883 YSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvSAYps 962
Cdd:cd14923 466 FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-----------SNY-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 963 fkfrghksallskkmtASSIIGENknylelskllkkkGTSTFLQRLERGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCI 1042
Cdd:cd14923 528 ----------------AGAEAGDS-------------GGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCL 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1043 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRLVLQQCK 1119
Cdd:cd14923 579 IPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQfidSKNASEKLLNSIDVDR 658
|
730
....*....|....
gi 62177127 1120 LQgWQMGVRKVFLK 1133
Cdd:cd14923 659 EQ-YRFGHTKVFFK 671
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
416-1095 |
9.88e-75 |
|
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: 263.63 E-value: 9.88e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFREQRP--QC 492
Cdd:cd14880 2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQP--QKLKPHIFTVGEQTYRNVKSLIEPvnQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 493 FILSGERGSGKSEASKQIIRHLTCRAgASRAT---------LDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcE 563
Cdd:cd14880 80 IVVSGESGAGKTWTSRCLMKFYAVVA-ASPTSweshkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL-N 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 564 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiqddastgERSLNREKLA 643
Cdd:cd14880 158 RAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP--------ERNLEEDCFE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 644 VLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTalNEGNSAFVSDLQLLEQV-----AGMLQVSTDELASALTT-DIQ 717
Cdd:cd14880 230 VTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFA--DSEDEAQPCQPMDDTKEsvrtsALLLKLPEDHLLETLQIrTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 718 YFKGDMIIRRHTIQI-AEFFRDLLAKSLYSRLFSFLVNTMNSCLHSqdEQKSMQTLdIGILDIFGFEEFQKNEFEQLCVN 796
Cdd:cd14880 308 AGKQQQVFKKPCSRAeCDTRRDCLAKLIYARLFDWLVSVINSSICA--DTDSWTTF-IGLLDVYGFESFPENSLEQLCIN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 797 MTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsVESNFPKKLQSLLE 875
Cdd:cd14880 385 YANEKLqQHFVAHYL-RAQQEEYAVEGLEWSFINYQDNQT-CLDLIEGSPISICSLINEECRL---NRPSSAAQLQTRIE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 876 SsntnAVYSPMKDGNGNVALKdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsqtgs 955
Cdd:cd14880 460 S----ALAGNPCLGHNKLSRE---PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 956 lvsaypsfkfrghksallSKKMTASSIIGENknylelskllkkkgtstflqrleRGDPVTIASQLRKSLMDIIGKLQKCT 1035
Cdd:cd14880 527 ------------------PEEKTQEEPSGQS-----------------------RAPVLTVVSKFKASLEQLLQVLHSTT 565
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1036 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1095
Cdd:cd14880 566 PHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLR 625
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
428-1133 |
1.50e-74 |
|
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: 264.59 E-value: 1.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 428 NQIYTFIGDILLLVNPYKELPIYS-SMVSQLYFSSSgklcSSLPPHLFSCVERAFHQLFREQRPQCFILSGERGSGKSEA 506
Cdd:cd14887 22 NCIYTYTGTLLIAVNPYRFFNLYDrQWISRFDTEAN----SRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTET 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 507 SKQIIRHLTC----RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKqQLTGARIYTYLLEKSR 582
Cdd:cd14887 98 SKHVLTYLAAvsdrRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG-KLTRASVATYLLANER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 583 LVSQPLGQSNFLIFYllmdglsaeekyglhlnNLCAHRYLNQTiqDDASTGERSLNREKLAVLKRALNVVGFSSLEVENL 662
Cdd:cd14887 177 VVRIPSDEFSFHIFY-----------------ALCNAAVAAAT--QKSSAGEGDPESTDLRRITAAMKTVGIGGGEQADI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 663 FVILAAILHLGDIRFTALNE--------------GNSAFVSDL-QLLE--------QVAGMLQVSTDELASALTTDIQYF 719
Cdd:cd14887 238 FKLLAAILHLGNVEFTTDQEpetskkrkltsvsvGCEETAADRsHSSEvkclssglKVTEASRKHLKTVARLLGLPPGVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 720 KGDMI-----IRR-------HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLH----------SQDEQKSMQTLDIGIL 777
Cdd:cd14887 318 GEEMLrlalvSRSvretrsfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQrsakpsesdsDEDTPSTTGTQTIGIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 778 DIFGFEEFQ---KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVL-DFFFQKPSGFLTLLD 853
Cdd:cd14887 398 DLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSFPLaSTLTSSPSSTSPFSP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 854 EESQMIWSVESNFPKKLQSLLESSNTNAVYSPMKDGNGNV----------------------ALKDHGTAFTIMHYAGRV 911
Cdd:cd14887 478 TPSFRSSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSdlfyeklnkniinsakyknitpALSRENLEFTVSHFACDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 912 MYDVVGAIEKNKDSLSQNLlfvmktsenvvinhlfqsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKNyle 991
Cdd:cd14887 558 TYDARDFCRANREATSDEL---------------------------------------ERLFLACSTYTRLVGSKKN--- 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 992 lskllkkKGTSTFLQRLErgdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMV 1071
Cdd:cd14887 596 -------SGVRAISSRRS-----TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLL 663
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62177127 1072 KIFRYGYPVRLSFSDFLSRYkplaDTFLREKKEQSAAER--CRLVLQQCKLQ--GWQMGVRKVFLK 1133
Cdd:cd14887 664 RVMADGFPCRLPYVELWRRY----ETKLPMALREALTPKmfCKIVLMFLEINsnSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
416-1097 |
2.18e-70 |
|
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: 248.27 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsslpPHLFSCVERAFHQLFREQRpQCFIL 495
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE------PHVYDVAEASVQDLLVHGN-QTIVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAgASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcerKQQLTGARIYT 575
Cdd:cd14898 75 SGESGSGKTENAKLVIKYLVERT-ASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF---DGKITGAKFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 576 YLLEKSRLVSQPLGQSNFLIFYLLmdglsaeekyglhlnnlCAHRYLNqtIQDD-------ASTGERSLN-REKLAVLKR 647
Cdd:cd14898 151 YLLEKSRVTHHEKGERNFHIFYQF-----------------CASKRLN--IKNDfidtsstAGNKESIVQlSEKYKMTCS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 648 ALNVVGFSSL-EVENLfviLAAILHLGDIRFTalNEGNSAFVSDlQLLEQVAGMLQVSTDELASALTT-DIQYfKGDMII 725
Cdd:cd14898 212 AMKSLGIANFkSIEDC---LLGILYLGSIQFV--NDGILKLQRN-ESFTEFCKLHNIQEEDFEESLVKfSIQV-KGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 726 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEqksmqtLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGE------RSISVLDIFGFEIFESNGLDQLCINWTNEKIQND 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDffFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLessntnavysp 885
Cdd:cd14898 359 FIKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRD--FEKPCGLMDLISEESFNAWGNVKNLLVKIKKYL----------- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 886 mkdgNGNVALKdHGTAFTIMHYAGRVMYDVVGAIEKNKDSlsqnllfvmktsenvvinhlfqsklsqtGSLvsaypsfkf 965
Cdd:cd14898 426 ----NGFINTK-ARDKIKVSHYAGDVEYDLRDFLDKNREK----------------------------GQL--------- 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 966 RGHKSALLSKKMTASSIIGENKNylelskllkkkgtstflqrlergdpvtiasqlrkSLMDIIGKLQKCTPHFIHCIRPN 1045
Cdd:cd14898 464 LIFKNLLINDEGSKEDLVKYFKD----------------------------------SMNKLLNSINETQAKYIKCIRPN 509
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 62177127 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT 1097
Cdd:cd14898 510 EECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
417-1133 |
2.71e-70 |
|
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: 249.40 E-value: 2.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgklcsslppHLFSCVERAFHQLFR-EQRPQCFIL 495
Cdd:cd14874 3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC-------------HISGVAENALDRIKSmSSNAESIVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGASRATLDSrfKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARI-Y 574
Cdd:cd14874 70 GGESGSGKSYNAFQVFKYLTSQPKSKVTTKHS--SAIESVFKSFGCAKTLKNDEATRFGCSIDLLY--KRNVLTGLNLkY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 575 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQtiqdDASTGERSLNREKLAVLKRALNVVGF 654
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQ----GNSTENIQSDVNHFKHLEDALHVLGF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 655 SSLEVENLFVILAAILHLGDIRFTAL----NEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQyfKGDMIirrhTI 730
Cdd:cd14874 222 SDDHCISIYKIISTILHIGNIYFRTKrnpnVEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSE--DGTTI----DL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 731 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 810
Cdd:cd14874 296 NAALDNRDSFAMLIYEELFKWVLNRIGLHL-----KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 811 FLHEQVECVQEGVTMETAYSPGNQNG-VLDFFFQKPSGFLTLLDEESQmiwsvesnFPK-KLQSLLESSNTNAVyspMKD 888
Cdd:cd14874 371 FHDQLVDYAKDGISVDYKVPNSIENGkTVELLFKKPYGLLPLLTDECK--------FPKgSHESYLEHCNLNHT---DRS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 889 GNGNVALKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVsaypsfkfrgh 968
Cdd:cd14874 440 SYGKARNKER-LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMI----------- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 969 ksallskkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSK 1048
Cdd:cd14874 508 ---------------------------------------------VSQAQFILRGAQEIADKINGSHAHFVRCIKSNNER 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1049 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL--ADTflreKKEQSAAERCRLVLQQcklQG---- 1122
Cdd:cd14874 543 QPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLlpGDI----AMCQNEKEIIQDILQG---QGvkye 615
|
730
....*....|...
gi 62177127 1123 --WQMGVRKVFLK 1133
Cdd:cd14874 616 ndFKIGTEYVFLR 628
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
416-1091 |
1.19e-66 |
|
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: 239.99 E-value: 1.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcssLPPHLFSCVERAFHQLFREQRPQCFI 494
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRG-----LPPHLFALAAKAISDMQDFRRDQLIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 495 LSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIY 574
Cdd:cd14905 77 IGGESGSGKSENTKIIIQYLLTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEM-FYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 575 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ--TIQDDASTGERSLNReklavLKRALNVV 652
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQggSISVESIDDNRVFDR-----LKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 653 GFSSLEVENLFVILAAILHLGDIRFtaLNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDiqyfkgdmiiRRHTIQI 732
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTF--FQKNGKTEVKDRTLIESLSHNITFDSTKLENILISD----------RSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 733 AEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 812
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKL-----KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 813 HEQVECVQEGVTMETAYS-PGNQNGVldfffQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTNAvYSPMKdgng 891
Cdd:cd14905 374 QEQREYQTERIPWMTPISfKDNEESV-----EMMEKIINLLDQESKNINSSDQIFLEKLQNFLSRHHLFG-KKPNK---- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 892 nvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtseNVVINHLFQS----KLSQTGSLVSAYPSFKFRG 967
Cdd:cd14905 444 ----------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHK---NSITKYLFSRdgvfNINATVAELNQMFDAKNTA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 968 HKSALLSKK--MTASSIIGENKNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLMDiigklQKCTPHFIHCIRPN 1045
Cdd:cd14905 511 KKSPLSIVKvlLSCGSNNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINN-----SNCDFHFIRCIKPN 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 62177127 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1091
Cdd:cd14905 586 SKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRF 631
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
416-1092 |
9.20e-66 |
|
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: 237.50 E-value: 9.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS----LPPHLFSCVERAFHQLFREQRP 490
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAASaapfPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 491 QCFILSGERGSGKSEASKQIIRHLT-CRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQ-- 567
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHyIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENTqk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 568 ------LTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL--------NQTIQDDASTG 633
Cdd:cd14884 162 nmfngcFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLlnpdeshqKRSVKGTLRLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 634 ERSLNREKLAVLK---------RALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAgMLQVS 704
Cdd:cd14884 242 SDSLDPSEEEKAKdeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKAAAECLQIEEEDLENVIKYK-NIRVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 705 TDelasalttdiqyfkgdmIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLD--------IG 775
Cdd:cd14884 321 HE-----------------VIRTErRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDiysineaiIS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 776 ILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVLFlHEQVECVQEGVTMETAYSPgNQNGVLDFffqkPSGFLTLLDE 854
Cdd:cd14884 384 ILDIYGFEELSGNDFDQLCINLANEKLNnYYINNEIE-KEKRIYARENIICCSDVAP-SYSDTLIF----IAKIFRRLDD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 855 ESQM-----------IWSVESNFPKKLQslLESSNTNAVYSPMKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNK 923
Cdd:cd14884 458 ITKLknqgqkktddhFFRYLLNNERQQQ--LEGKVSYGFVLNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 924 DSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfkfrghksallskkmtasSIIGENKNYLelskllkkkgtst 1003
Cdd:cd14884 536 DKIETSIETLISCSSNRFLRE------------------------------------ANNGGNKGNF------------- 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1004 flqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLS 1083
Cdd:cd14884 567 ----------LSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
....*....
gi 62177127 1084 FSDFLSRYK 1092
Cdd:cd14884 637 KKETAAALK 645
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
416-1133 |
2.57e-63 |
|
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: 230.66 E-value: 2.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 495
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMF---KGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 496 SGERGSGKSEASKQIIRHLTCRAGAS--RATLDsRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 573
Cdd:cd01386 79 LGRSGSGKTTNCRHILEYLVTAAGSVggVLSVE-KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDF-DQAGQLASASI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 574 YTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLC--AHRYLNQTIQDDastgERSLNREKLAVLKRALNV 651
Cdd:cd01386 157 QTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAesNSFGIVPLQKPE----DKQKAAAAFSKLQAAMKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 652 VGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASAL------------TTDIQYF 719
Cdd:cd01386 233 LGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 720 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQdeQKSMQTldIGILDIFGFE--EFQKNE----FEQL 793
Cdd:cd01386 313 SPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSS--HHSTSS--ITIVDTPGFQnpAHSGSQrgatFEDL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 794 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPS--------------GFLTLLDEESQMI 859
Cdd:cd01386 389 CHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedrrGLLWLLDEEALYP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 860 WSVESNFPKKLQSllessntnaVYSPMKDGNGNVALK--DHGTAFTIMHYAGR--VMYDVVGaieknkdslsqnllFVMK 935
Cdd:cd01386 469 GSSDDTFLERLFS---------HYGDKEGGKGHSLLRrsEGPLQFVLGHLLGTnpVEYDVSG--------------WLKA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 936 TSENVvinhlfqSKLSQTGSLVSAYPSFKFRGHKSALLSKKMTassiigenknylelskllkkkgtstflqrlergdpvt 1015
Cdd:cd01386 526 AKENP-------SAQNATQLLQESQKETAAVKRKSPCLQIKFQ------------------------------------- 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1016 iasqlrkslMD-IIGKLQKCTPHFIHCIRPN------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRL 1082
Cdd:cd01386 562 ---------VDaLIDTLRRTGLHFVHCLLPQhnagkderstssPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHM 632
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 62177127 1083 SFSDFLSRYKPLADTFLREKKEQS--AAERcRLV---LQQCKLQ--GWQMGVRKVFLK 1133
Cdd:cd01386 633 PLGEFRRRFQVLAPPLTKKLGLNSevADER-KAVeelLEELDLEksSYRIGLSQVFFR 689
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
424-1133 |
1.64e-60 |
|
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: 221.04 E-value: 1.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 424 RFGNNQIYTFIGDILLLVNPYKELPIYSSmvsqlyfSSSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILSGERGSGK 503
Cdd:cd14937 10 RYKKNYIYTIAEPMLISINPYQVIDVDIN-------EYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGSGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 504 SEASKQIIRHLTCRAGA----SRATLDSRFkhvvcILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGARIYTYLLE 579
Cdd:cd14937 83 TEASKLVIKYYLSGVKEdneiSNTLWDSNF-----ILEAFGNAKTLKNNNSSRYGKYIKIELDEY-QNIVSSSIEIFLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 580 KSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL-NQTIQ----DDASTGER---SLNREKLAVLKralnv 651
Cdd:cd14937 157 NIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIvNKNVVipeiDDAKDFGNlmiSFDKMNMHDMK----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 652 vgfsslevENLFVILAAILHLGDIRFTALNEGNSAFVSDL-----QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 726
Cdd:cd14937 232 --------DDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELdknnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 806
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNY----IGILDIFGFEIFSKNSLEQLLINIANEEIHSIY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 807 NEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfffqkpsgfltLLDEESQMIWSVESNF--PKKLQSLLESSNTNAVys 884
Cdd:cd14937 380 LYIVYEKETELYKAEDILIESVKYTTNES-IID-----------LLRGKTSIISILEDSClgPVKNDESIVSVYTNKF-- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 885 pMKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSkLSQTGSLvsaypsfk 964
Cdd:cd14937 446 -SKHEKYASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-VEVSESL-------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 965 frGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrKSLMDIIGKLQKCTPHFIHCIRP 1044
Cdd:cd14937 516 --GRKNLITFKYL--------------------------------------------KNLNNIISYLKSTNIYFIKCIKP 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1045 NNSKLPDTFDNFYVSAQLQYIGVLEMVKI---FRYGYpvrlSFSDFLSRYKPL-----ADTFLREKKEQSaaercRLVLQ 1116
Cdd:cd14937 550 NENKEKNNFNQKKVFPQLFSLSIIETLNIsffFQYKY----TFDVFLSYFEYLdystsKDSSLTDKEKVS-----MILQN 620
|
730
....*....|....*..
gi 62177127 1117 QCKLQGWQMGVRKVFLK 1133
Cdd:cd14937 621 TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
417-1092 |
2.32e-60 |
|
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: 222.92 E-value: 2.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKL-------CSSLPPHLFSCVERAFHQLFREQR 489
Cdd:cd14893 3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQTplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 490 PQCFILSGERGSGKSEASKQIIRHLtCRAGASRA-------------TLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKY 556
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYL-CEIGDETEprpdsegasgvlhPIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 557 FELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE--KYGLHLNNlCAHRYlNQTIQDDASTGE 634
Cdd:cd14893 162 ISVEF-SKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNK-CVNEF-VMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 635 RSLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRF-------TALNEGNSAFVSDLQ--------LLEQVAG 699
Cdd:cd14893 239 FALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQscalkdpaQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 700 MLQVSTDELASALTTDiQYFKGD-----MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL-----HSQDEQKSM 769
Cdd:cd14893 319 LLEVEPVVLDNYFRTR-QFFSKDgnktvSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSNIVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 770 QTLDIGILDIFGFEEF--QKNEFEQLCVNMTNEKMHH-YINEVL-----FLHEQVECVQEGVTMETAYS-PGNQNGVLDF 840
Cdd:cd14893 398 NSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHfYVQNTLainfsFLEDESQQVENRLTVNSNVDiTSEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 841 FFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLE-----------SSNTNAVYSPMKDGNgnvalkdhgTAFTIMHYAG 909
Cdd:cd14893 478 FEDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEavgglsrpnmgADTTNEYLAPSKDWR---------LLFIVQHHCG 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 910 RVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAyPSFKFRGHKSALLSKKMTASSiigENKNy 989
Cdd:cd14893 549 KVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAA-KQTEERGSTSSKFRKSASSAR---ESKN- 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 990 lelskllkkKGTSTFLQRLERGDPVTIAsqlrkslMDIIGKlqkctpHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLE 1069
Cdd:cd14893 624 ---------ITDSAATDVYNQADALLHA-------LNHTGK------NFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVE 681
|
730 740
....*....|....*....|...
gi 62177127 1070 MVKIFRYGYPVRLSFSDFLSRYK 1092
Cdd:cd14893 682 LMQASRSIFTVHLTYGHFFRRYK 704
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
45-325 |
1.51e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 166.67 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 45 LKRLKHAKNPKVHFNLTDMLQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDE 124
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 125 DFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyldENGVDLtslrqmklqrpmsmltd 204
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA-------------NGNLEI----------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 205 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLV 284
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 62177127 285 NCNEEKASDIAASEFIEEMLLKAEIAWEEKMKEPLSASTLA 325
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
44-337 |
5.95e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 159.35 E-value: 5.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 44 FLKRLKHAKNPKVHFNLTDMLQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQD 123
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 124 EDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyldENGVDLtslrqmklqrpmsmlt 203
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY-------------NGNLEI---------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 204 dVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHL 283
Cdd:COG0666 136 -VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 62177127 284 VNCNEEKASDIAASEF---IEEMLLKAEIAWEEKMKEPLSASTLAQEEPYEEIIHDL 337
Cdd:COG0666 215 KDNDGKTALDLAAENGnleIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
416-1132 |
1.96e-40 |
|
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: 161.54 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgkLCSSLPPHL----FSCVERAFHQLFREQRPQ 491
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKY------KCIDCIEDLslneYHVVHNALKNLNELKRNQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 492 CFILSGERGSGKSEASKQIIRHLTCRAGASRATLDSR-----------------------FKHVVCILEAFGHAKTTLND 548
Cdd:cd14938 76 SIIISGESGSGKSEIAKNIINFIAYQVKGSRRLPTNLndqeednihneentdyqfnmsemLKHVNVVMEAFGNAKTVKNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 549 LSSCFIKYFELQFceRKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNqtiqD 628
Cdd:cd14938 156 NSSRFSKFCTIHI--ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLN----N 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 629 DASTGERSLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDI---------------RFTALNEGNSAFVSDLQL 693
Cdd:cd14938 230 EKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkafrkksllmgkNQCGQNINYETILSELEN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 694 LEQVAGMLQVSTDELASAL-----TTDIQYFKGDMI------IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNsCLHS 762
Cdd:cd14938 310 SEDIGLDENVKNLLLACKLlsfdiETFVKYFTTNYIfndsilIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN-EKCT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 763 QDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFF 842
Cdd:cd14938 389 QLQNININTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 843 QKPSGFL-TLLDEESQMIWSVESNFPkklQSLLESSNTNAVYSPMKDGNGNvalkdhGTAFTIMHYAGRVMYDVVGAIEK 921
Cdd:cd14938 469 GPTEGSLfSLLENVSTKTIFDKSNLH---SSIIRKFSRNSKYIKKDDITGN------KKTFVITHSCGDIIYNAENFVEK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 922 NKDSLSQNLLFVMKTSENVVINHLFQsklsqtgslvsaypSFKFRghksallskkmTASSIIGENKNYLELSKLlkkkgt 1001
Cdd:cd14938 540 NIDILTNRFIDMVKQSENEYMRQFCM--------------FYNYD-----------NSGNIVEEKRRYSIQSAL------ 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1002 STFLQRLERGDPVTIaSQLRKSLMDIIGKLQKCTPHFIHCIRPNNSK-LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPV 1080
Cdd:cd14938 589 KLFKRRYDTKNQMAV-SLLRNNLTELEKLQETTFCHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPH 667
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 62177127 1081 RLSFSDFLSRYKpladtflreKKEQSAAERCRLVLQQCKL--QGWQMGVRKVFL 1132
Cdd:cd14938 668 KFTLNEFLSIFD---------IKNEDLKEKVEALIKSYQIsnYEWMIGNNMIFL 712
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
535-1101 |
7.81e-24 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 109.83 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 535 ILEAFGHAKTTLNDLSSCFIKYFELQFC----ERKQQLTGARIYTYLLEKSRLVSQPLGQS------NFLIFYLLMDGLS 604
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVAfglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 605 AEE-----KYGLHLNNL--CAHRYLNQTIQDDA------STGERSLNREKLAVlkRALNVVGFSSLEVENLFVILAAILH 671
Cdd:cd14894 335 AFPfmrllAKELHLDGIdcSALTYLGRSDHKLAgfvskeDTWKKDVERWQQVI--DGLDELNVSPDEQKTIFKVLSAVLW 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 672 LGDIRFTALNEGNSAFVSD---LQLLEQVAGMLQV-STDELASALTTDIQYFKGDMIIRRHTIQIAEF--FRDLLAKSLY 745
Cdd:cd14894 413 LGNIELDYREVSGKLVMSStgaLNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVnhVRDTLARLLY 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 746 SRLFSFLVNTMN-----SCLHSQDEQKSMQTLD--------IGILDIFGFEEFQKNEFEQLCVNMTNEKMhhYINEvlfl 812
Cdd:cd14894 493 QLAFNYVVFVMNeatkmSALSTDGNKHQMDSNAsapeavslLKIVDVFGFEDLTHNSLDQLCINYLSEKL--YARE---- 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 813 hEQVecvqegvtMETAYSP-------GNQNGVLdFFFQKPSGF------LTLLDEESQMIWSVESNFPKKLQSLLESSNT 879
Cdd:cd14894 567 -EQV--------IAVAYSSrphltarDSEKDVL-FIYEHPLGVfasleeLTILHQSENMNAQQEEKRNKLFVRNIYDRNS 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 880 NAVYSP---MKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvviNHLfqSKLSQTGSL 956
Cdd:cd14894 637 SRLPEPprvLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNS---SHF--CRMLNESSQ 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 957 VSAYPSfkfrghksallskkmTASSIIGENKNylelskllKKKGTSTFLqrlergdpvtiaSQLRKSLMDIIGKLQKCTP 1036
Cdd:cd14894 712 LGWSPN---------------TNRSMLGSAES--------RLSGTKSFV------------GQFRSHVNVLTSQDDKNMP 756
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62177127 1037 HFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG----YPVRLSFSDFLSRYKPLadtfLRE 1101
Cdd:cd14894 757 FYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSsssySAIDISKSTLLTRYGSL----LRE 821
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
67-280 |
6.35e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 103.98 E-value: 6.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 67 AIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARY-----DNAFIAEILIDRGVNVNHQDEDFWTPMHIA-CACDN-P 139
Cdd:PHA03100 42 AKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAiSKKSNsY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 140 DIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLrqmklqrpmsmlTDVKHFLSSGGNVNEKN 219
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLIDKGVDINAK------------NRVNYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62177127 220 DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQAN 280
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
72-304 |
4.17e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 98.20 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 72 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACAC-----DNPDIVLLLV 146
Cdd:PHA03100 14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 147 LAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLR-------QMKLQRPMSMLTDVKHFLSSGGNVNEKN 219
Cdd:PHA03100 94 EYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNsdgenllHLYLESNKIDLKILKLLIDKGVDINAKN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 220 degvtllhmacasgykeVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLVNCNEEKASDIAASEF 299
Cdd:PHA03100 174 -----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
|
....*
gi 62177127 300 IEEML 304
Cdd:PHA03100 237 NKEIF 241
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
441-559 |
3.78e-19 |
|
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: 86.63 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 441 VNPYKELPIYSSmvSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILSGERGSGKSEASKQIIRHLTCRAGA 520
Cdd:cd01363 5 VNPFKELPIYRD--SKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFN 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 62177127 521 SRATLDSRF-----KHVVC----------ILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:cd01363 83 GINKGETEGwvyltEITVTledqilqanpILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
59-279 |
1.32e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 92.43 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 59 NLTDMLQDAIIHHNDKE------VLRLLKEGADPHTLVSSGGSLLHLCAR--YDNAFIaEILIDRGVNVNHQDEDFWTPM 130
Cdd:PHA02876 267 NSIDDCKNTPLHHASQApslsrlVPKLLERGADVNAKNIKGETPLYLMAKngYDTENI-RTLIMLGADVNAADRLYITPL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 131 HIACACD-NPDIVLLLVLAGANVLLQDVNGNIPLDYAveGTESSSILLTYLDENGVDLTSLRQmKLQRPMSM-------L 202
Cdd:PHA02876 346 HQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYA--AVRNNVVIINTLLDYGADIEALSQ-KIGTALHFalcgtnpY 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62177127 203 TDVKHFLSSGGNVNEKNDEGVTLLHMACASGYK-EVVSLILEHGGDLNIVDDQYWTPLHLAAKYgqTNLVKLLLMHQA 279
Cdd:PHA02876 423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGA 498
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
205-285 |
7.74e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 205 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHgGDLNIVDDQyWTPLHLAAKYGQTNLVKLLLMHQANPHLV 284
Cdd:pfam12796 13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVK 90
|
.
gi 62177127 285 N 285
Cdd:pfam12796 91 D 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
64-156 |
6.53e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 64 LQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRgVNVNHQDEDfWTPMHIACACDNPDIVL 143
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 62177127 144 LLVLAGANVLLQD 156
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
75-284 |
5.82e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.60 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 75 EVLRLL-KEGADPHTLVSSGGSLLHLCARYDN--AFIAEILIDRGVNVNHQDEDFWTPMHI-----ACacdNPDIVLLLV 146
Cdd:PHA03095 98 DVIKLLiKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVllksrNA---NVELLRLLI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 147 LAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLRQMKLQRPMSMLT-------DVKHFLSSGGNVNEKN 219
Cdd:PHA03095 175 DAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgssckrsLVLPLLIAGISINARN 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62177127 220 DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLV 284
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
104-289 |
7.87e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.77 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 104 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVllQDVNGNIPLDYAVEGTESSSILLTYLDEN 183
Cdd:PHA02874 13 DIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADI--NHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 184 GVDLTSLRQMKLQRPMsmltdVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAA 263
Cdd:PHA02874 91 GVDTSILPIPCIEKDM-----IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
|
170 180
....*....|....*....|....*.
gi 62177127 264 KYGQTNLVKLLLMHQANPHLVNCNEE 289
Cdd:PHA02874 166 KHNFFDIIKLLLEKGAYANVKDNNGE 191
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
102-287 |
2.46e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 74.23 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 102 RYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLqdvngnIPLDyAVEGTESSSILLTYLD 181
Cdd:PHA02874 44 RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIP-CIEKDMIKTILDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 182 ENGVDLTSLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHL 261
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180
....*....|....*....|....*.
gi 62177127 262 AAKYGQTNLVKLLLMHQANPhLVNCN 287
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHI-MNKCK 221
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
85-285 |
2.47e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 74.68 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 85 DPHTLVSSGGSLLHLCARYDNAFIAEI--LIDRGVNVNHQDEDFWTPMH--IACACDN-PDIVLLLVLAGANVLLQDVNG 159
Cdd:PHA03095 4 DESVDIIMEAALYDYLLNASNVTVEEVrrLLAAGADVNFRGEYGKTPLHlyLHYSSEKvKDIVRLLLEAGADVNAPERCG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 160 NIPLDYavegtesssilltYLdENGvdlTSLRQMKLqrpmsmltdvkhFLSSGGNVNEKNDEGVTLLHmACASGY---KE 236
Cdd:PHA03095 84 FTPLHL-------------YL-YNA---TTLDVIKL------------LIKAGADVNAKDKVGRTPLH-VYLSGFninPK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 62177127 237 VVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTN--LVKLLLMHQANPHLVN 285
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVD 184
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
74-289 |
5.37e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.52 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 74 KEVLRLLKEGADP-----------HTLVSSGGSL-------------------------LHLCARYDN-AFIAEILIDRG 116
Cdd:PHA03095 28 EEVRRLLAAGADVnfrgeygktplHLYLHYSSEKvkdivrllleagadvnapercgftpLHLYLYNATtLDVIKLLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 117 VNVNHQDEDFWTPMHIACA--CDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDL------- 187
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVyavddrf 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 188 -TSLRQMKL-----QRPMSMLTDvkhflsSGGNVNEKNDEGVTLLH-MACASGYKE-VVSLILEHGGDLNIVDDQYWTPL 259
Cdd:PHA03095 188 rSLLHHHLQsfkprARIVRELIR------AGCDPAATDMLGNTPLHsMATGSSCKRsLVLPLLIAGISINARNRYGQTPL 261
|
250 260 270
....*....|....*....|....*....|
gi 62177127 260 HLAAKYGQTNLVKLLLMHQANPHLVNCNEE 289
Cdd:PHA03095 262 HYAAVFNNPRACRRLIALGADINAVSSDGN 291
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
73-303 |
6.54e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 73.38 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 73 DKEVLRLLKE-GADPHTLV-SSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGA 150
Cdd:PHA02878 146 EAEITKLLLSyGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 151 NVLLQDVNGNIPLDYAVEGTESSSILltyldengvdltslrqmklqrpmsmltdvKHFLSSGGNVNEKND-EGVTLLHMA 229
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDIL-----------------------------KLLLEHGVDVNAKSYiLGLTALHSS 276
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62177127 230 CASgyKEVVSLILEHGGDLNIVDDQYWTPLHLAAK-YGQTNLVKLLLMHqanphlVNCNEEKASDIAASE-FIEEM 303
Cdd:PHA02878 277 IKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILISN------ICLLKRIKPDIKNSEgFIDNM 344
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
226-277 |
1.48e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.14 E-value: 1.48e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 62177127 226 LHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMH 277
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
97-252 |
3.11e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.98 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 97 LHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLlvlaganvLLQDVNGNIpldyavegtesssil 176
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL--------LLEHADVNL--------------- 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62177127 177 ltyldengvdltslrqmklqrpmsmltdvkhflssggnvnekNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVD 252
Cdd:pfam12796 58 ------------------------------------------KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
222-275 |
9.90e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.52 E-value: 9.90e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62177127 222 GVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLL 275
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
59-280 |
2.99e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.55 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 59 NLTDMLQDAIIHH-----NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDedfwtpMHIA 133
Cdd:PHA02876 172 NAKDIYCITPIHYaaergNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND------LSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 134 CACDNPDI--VLLLVLAGANVLLQDVNGNIPLDYAVEgTESSSILLTYLDENGVDLTSlRQMKLQRPMSMLT-------D 204
Cdd:PHA02876 246 KAIRNEDLetSLLLYDAGFSVNSIDDCKNTPLHHASQ-APSLSRLVPKLLERGADVNA-KNIKGETPLYLMAkngydteN 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62177127 205 VKHFLSSGGNVNEKNDEGVTLLHMACA-SGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQAN 280
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
72-310 |
5.79e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 66.91 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 72 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGAN 151
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 152 VLLQDVNGNIPLDYAVEgtesssilltYLDengvdltslrqmklqrpmsmLTDVKHFLSSGGNVNEKNDEGVTLLHMACA 231
Cdd:PHA02874 183 ANVKDNNGESPLHNAAE----------YGD--------------------YACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 232 sgYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYG-QTNLVKLLLMHQANPHLVNCNEEKASDIAASEFIEEMLLKAEIA 310
Cdd:PHA02874 233 --HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIA 310
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
104-280 |
3.45e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.08 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 104 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDEN 183
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 184 GVDLTSLRQMKLQRPMSMLTDVKHFlSSGGNVNEKNDEGVTLLHMAC-ASGYKEVVSLILEHGGDLNIVDDQYWTPLHLA 262
Cdd:PHA02876 236 NINKNDLSLLKAIRNEDLETSLLLY-DAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
|
170
....*....|....*....
gi 62177127 263 AKYG-QTNLVKLLLMHQAN 280
Cdd:PHA02876 315 AKNGyDTENIRTLIMLGAD 333
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
14-261 |
5.70e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.42 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 14 GQRQRLVKRMRCEQI----KAYYEREKAFQKQEGFLKRL--------KHAKNPKVHFNLTdMLQDAIIHH---NDKEVLR 78
Cdd:PLN03192 433 GEKERVVGTLGCGDIfgevGALCCRPQSFTFRTKTLSQLlrlktstlIEAMQTRQEDNVV-ILKNFLQHHkelHDLNVGD 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 79 LLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILiDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVN 158
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 159 GNIPLDYAVEGTESSSILLTYL------DENGVDLTSLRQMKlqrpmSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACAS 232
Cdd:PLN03192 591 GNTALWNAISAKHHKIFRILYHfasisdPHAAGDLLCTAAKR-----NDLTAMKELLKQGLNVDSEDHQGATALQVAMAE 665
|
250 260 270
....*....|....*....|....*....|
gi 62177127 233 GYKEVVSLILEHGGDLNIVD-DQYWTPLHL 261
Cdd:PLN03192 666 DHVDMVRLLIMNGADVDKANtDDDFSPTEL 695
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
64-287 |
6.08e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.39 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 64 LQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIacACDNPDIVL 143
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHD--AVEEGDVKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 144 LLVLAGANVLLQDV---NGNIPLDYAVEgtesssilltyldengvdLTSLRQMKLqrpmsmltdvkhFLSSGGNVNEKND 220
Cdd:PHA02875 84 VEELLDLGKFADDVfykDGMTPLHLATI------------------LKKLDIMKL------------LIARGADPDIPNT 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62177127 221 EGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLVNCN 287
Cdd:PHA02875 134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
112-166 |
1.52e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 52.35 E-value: 1.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 62177127 112 LIDRG-VNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYA 166
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
97-289 |
1.96e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 59.12 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 97 LHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIAC-----------------------------ACDNPD------- 140
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdAFNNRNveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 141 ----------------------------IVLLLVLAGANVLLQDVN-GNIPLDYAVEG--TESSSILLTYLDE-NGVDLT 188
Cdd:PHA02878 121 ltnrykniqtidlvyidkkskddiieaeITKLLLSYGADINMKDRHkGNTALHYATENkdQRLTELLLSYGANvNIPDKT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 189 SLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMacASGY---KEVVSLILEHGGDLNIVDD-QYWTPLHLAAK 264
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI--SVGYckdYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
|
250 260
....*....|....*....|....*
gi 62177127 265 YGQTnlVKLLLMHQANPHLVNCNEE 289
Cdd:PHA02878 279 SERK--LKLLLEYGADINSLNSYKL 301
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
205-282 |
2.12e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 2.12e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62177127 205 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPH 282
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1390-1650 |
5.14e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.41 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1390 GTPQCALPPAAPPGDEDDSEPvyiemlghaarPDSPDPGESvyeemkcclpddgGPGAGSFLLHGASPPLLH--RAPEDE 1467
Cdd:PHA03247 2549 GDPPPPLPPAAPPAAPDRSVP-----------PPRPAPRPS-------------EPAVTSRARRPDAPPQSArpRAPVDD 2604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1468 AAGPPGDACDIPPPfPNllPHRPPllvfPPTPvtcSPASDESPLTPLEVKKLPVLETNLKYPVQPEGSSP-------LSP 1540
Cdd:PHA03247 2605 RGDPRGPAPPSPLP-PD--THAPD----PPPP---SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrlgRAA 2674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1541 QYSKSQKGDGDRPASPGLALFNGSGRASPPSTPPP---PPPPPGPPPAPYRPCAHLAFPPEPA-----PVNAGKAGPSAE 1612
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEpapHALVSATPLPPGPAAARQASPALPAapappAVPAGPATPGGP 2754
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 62177127 1613 APKVHPK-----PNSAPVAGPCSSFPKIPYSPVKATRADARKA 1650
Cdd:PHA03247 2755 ARPARPPttagpPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
64-251 |
5.77e-08 |
|
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal family of eukaryotic proteins that are substrates of tyrosine kinase in the brain. When first identified, the family members were referred to as unconventional myosin XVI, or Myr 8. However, proteins have now been identified as being integrally involved in neuronal function and morphogenesis. The family is involved in both the activation of phosphoinositide 3-kinase (PI3K) and the recruitment of the downstream effector WAVE complex to the close vicinity of PI3K; it also appears to regulate the brain size and neurite outgrowth in mice.
Pssm-ID: 464717 [Multi-domain] Cd Length: 379 Bit Score: 57.09 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 64 LQDAIIHHNDKEvLRLLKEGADPHTLVSSGGSLLHL-----CARYDN---AFIAEILI--DRGVNVNHQDED--FWTPMH 131
Cdd:pfam15439 6 KLEKRRRQEEGI-KRSGEEVAGKVRDISSEGRHFRMgfmtmPASQDRlphPCAAGMSIrsQSLHSVGSGDEDgsLPSSRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 132 IACACDNPDIVLLLVLAGANVLLQDVNGNIpldyaVEGTESSSILLTYLDENgVDLTSLRQMKLQR-PMSMLT------- 203
Cdd:pfam15439 85 QPPPKPKRDPSTKLSMSSEAVSAGLSAGAK-----ETPSETEALSKPRPHSD-EYSRKIPPPKPKRsPNTQLSgsfdeip 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62177127 204 -------DVKHFLSSGG---NVNEKNDE---------GVTLLHMACA----------SGYKEVVSLILEHGGDLNIV 251
Cdd:pfam15439 159 apyirphGLLQRASSSDgpsPAPLPDEEeepvyiemvGNVLRDFSPTtpdddpdqseAVYEEMKYPLPEDSGAANGP 235
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
92-362 |
8.58e-08 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 57.23 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 92 SGGSLLH--LCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDN--PDIVLLLVLAGANVLLQDVNGNIP-LDYA 166
Cdd:PHA02716 176 TGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPiMTYI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 167 VE----GTESSSILLTYLDENGVD-----LTSLRQMKLQRPMSMltdVKHFLSSGGNVNEKNDEGVTLLHMACASGY--K 235
Cdd:PHA02716 256 INidniNPEITNIYIESLDGNKVKnipmiLHSYITLARNIDISV---VYSFLQPGVKLHYKDSAGRTCLHQYILRHNisT 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 236 EVVSLILEHGGDLNIVDDQYWTPLHlaakygqTNLVKLLLMHQANPH--------LVNCNEEKASDIAASEFIEEMLLKA 307
Cdd:PHA02716 333 DIIKLLHEYGNDLNEPDNIGNTVLH-------TYLSMLSVVNILDPEtdndirldVIQCLISLGADITAVNCLGYTPLTS 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 62177127 308 EIAweekmkeplsastLAQEEPYEEIIHDLpvLSSKLSPLVLPIAKQDSLLEKDI 362
Cdd:PHA02716 406 YIC-------------TAQNYMYYDIIDCL--ISDKVLNMVKHRILQDLLIRVDD 445
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
93-146 |
2.68e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 2.68e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 62177127 93 GGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLV 146
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
214-262 |
3.50e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.50 E-value: 3.50e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 62177127 214 NVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLA 262
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
130-286 |
6.97e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.84 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 130 MHIACACD-----NPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILL-----TYLDENGVDLTSLRQMKLQRpm 199
Cdd:PHA02875 1 MDQVALCDailfgELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLlmkhgAIPDVKYPDIESELHDAVEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 200 SMLTDVKHFLSSGGNVNEK-NDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQ 278
Cdd:PHA02875 79 GDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
....*...
gi 62177127 279 ANPHLVNC 286
Cdd:PHA02875 159 ACLDIEDC 166
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
137-290 |
9.32e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.69 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 137 DNP--DIVLLLVLAGANVLLQDVNGNIPLdyavegtesSSILLTYLDENgvdltslrqmklqrpmSMLTDVKHFLSSGGN 214
Cdd:PHA02798 47 DSPstDIVKLFINLGANVNGLDNEYSTPL---------CTILSNIKDYK----------------HMLDIVKILIENGAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 215 VNEKNDEGVTLLHMACASGY---KEVVSLILEHGGDLNIVDDQYWTPLHLAAKYG---QTNLVKLLLMHQANPHLVNcNE 288
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHN-NK 180
|
..
gi 62177127 289 EK 290
Cdd:PHA02798 181 EK 182
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1333-1649 |
5.44e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1333 PRPHSDDYStmkkIPPRKPKRSPNTKLSGSYEeisgSRPGdaRPAGAPGAAARVLTPGTPQCALPPAAPPGDEDDSEPvy 1412
Cdd:PHA03247 2559 APPAAPDRS----VPPPRPAPRPSEPAVTSRA----RRPD--APPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDP-- 2626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1413 iEMLGHAARPDSPDPGESVYEEMKCCLPDDGGPG---------AGSFLLHGASPPLLHRAPEDEAA-GPPGDACDIPPPF 1482
Cdd:PHA03247 2627 -PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrarRLGRAAQASSPPQRPRRRAARPTvGSLTSLADPPPPP 2705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1483 PNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETnlkyPVQPEG----SSPLSPQYSKSQKGDGDRPASP-- 1556
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG----PATPGGparpARPPTTAGPPAPAPPAAPAAGPpr 2781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1557 -----GLALFNGSGRASPPSTPPPPPPPPGPPPAPYRPCAHLAFPPEPAPVNAGKAGPS-AEAPKVHPKPNSAPVA---- 1626
Cdd:PHA03247 2782 rltrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPpPPGPPPPSLPLGGSVApggd 2861
|
330 340
....*....|....*....|....*..
gi 62177127 1627 ----GPCSSFPKIPYSPvkaTRADARK 1649
Cdd:PHA03247 2862 vrrrPPSRSPAAKPAAP---ARPPVRR 2885
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
37-168 |
6.48e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.05 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 37 AFQKQEGFLKRLKHAKNPK-VHFNLTDMLQDAIIHHNDK-EVLRLLKEGAD--PHTLVSSGG-----------SLLHLCA 101
Cdd:PTZ00322 12 AFAAQLFFGTEGSRKRRAKpISFERMAAIQEEIARIDTHlEALEATENKDAtpDHNLTTEEVidpvvahmltvELCQLAA 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62177127 102 RYDnAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVE 168
Cdd:PTZ00322 92 SGD-AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
241-295 |
1.31e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 1.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 62177127 241 ILEHGG-DLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLVNCNEEKASDIA 295
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
48-265 |
2.58e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 48.83 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 48 LKHAKNPKVHF-NLTDMLQDAIIHHNDKEVLRLLKEGADPHTLV-SSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDED 125
Cdd:PHA02875 55 MKHGAIPDVKYpDIESELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 126 FWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSilltyldengvdltslrqmklqrpmsmltdV 205
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI------------------------------C 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62177127 206 KHFLSSGGNVNEKNDEG-VTLLHMACASGYKEVVSLILEHGGDLNI---VDDQYWTPLHLAAKY 265
Cdd:PHA02875 185 KMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNImfmIEGEECTILDMICNM 248
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
256-285 |
3.01e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 42.66 E-value: 3.01e-05
10 20 30
....*....|....*....|....*....|.
gi 62177127 256 WTPLHLAA-KYGQTNLVKLLLMHQANPHLVN 285
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
108-275 |
6.04e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 47.91 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 108 IAEILIDRGVNVNHQDEDFWTPM-----HIACACDNPDIVLLLVLAGANVLLQDVNGNIPLdYAV--EGTESSSILLTYL 180
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL-YCLlsNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 181 DENGVDLTSLRQMKlqrpmsmLTDVKHFLSSGGNVNekndegvtllhmacasgyKEVVSLILEHGGDLNIVDDQY-WTPL 259
Cdd:PHA02798 132 IENGADTTLLDKDG-------FTMLQVYLQSNHHID------------------IEIIKLLLEKGVDINTHNNKEkYDTL 186
|
170 180
....*....|....*....|
gi 62177127 260 HLAAKYG----QTNLVKLLL 275
Cdd:PHA02798 187 HCYFKYNidriDADILKLFV 206
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
221-250 |
1.09e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 1.09e-04
10 20 30
....*....|....*....|....*....|
gi 62177127 221 EGVTLLHMACASGYKEVVSLILEHGGDLNI 250
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
73-167 |
1.78e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.17 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 73 DKEVLR-LLKEGADPHTLVSSGGSLLHLCARYDNAFIAEI--LIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAG 149
Cdd:PHA03095 201 RARIVReLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
|
90
....*....|....*...
gi 62177127 150 ANVLLQDVNGNIPLDYAV 167
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMV 298
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
254-283 |
1.88e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 1.88e-04
10 20 30
....*....|....*....|....*....|
gi 62177127 254 QYWTPLHLAAKYGQTNLVKLLLMHQANPHL 283
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
221-253 |
2.25e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.97 E-value: 2.25e-04
10 20 30
....*....|....*....|....*....|....
gi 62177127 221 EGVTLLHMACAS-GYKEVVSLILEHGGDLNIVDD 253
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
73-195 |
2.36e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.42 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 73 DKEVLRLL-KEGAD-PHTLVSSGGSLLHLCARYD---NAFIAEILIDRGVNVNHQDEDFWTPMHI-ACACD-NPDIVLLL 145
Cdd:PHA02859 65 NVEILKFLiENGADvNFKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLL 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 62177127 146 VLAGANVLLQDVNGNIPLdYAVEGTESSSILLTYLDENGVDLTSLRQMKL 195
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNIL-YSYILFHSDKKIFDFLTSLGIDINETNKSGY 193
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
221-250 |
2.71e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.93 E-value: 2.71e-04
10 20 30
....*....|....*....|....*....|
gi 62177127 221 EGVTLLHMACASGYKEVVSLILEHGGDLNI 250
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1325-1650 |
3.91e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.55 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1325 AANEALARPRPHSDDYSTMKKIPPRKPKRSPntklsgsyeeiSGSRPGDARPAGAPGAAARVLTPGTPQCALPPAAPPGD 1404
Cdd:PHA03307 133 DLSEMLRPVGSPGPPPAASPPAAGASPAAVA-----------SDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1405 EDDSEPVYIEMLGHAARPDSPDPGESvyeemkcclpDDGGPGAGSFLLHGASPPLLHRAPEDEAAGPPGDACDIPPPFPN 1484
Cdd:PHA03307 202 ASPRPPRRSSPISASASSPAPAPGRS----------AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1485 LLPHRPPllvfPPTPVTCSPASDESPLTPlevkklpvletnlkyPVQP--EGSSPLSPQYSKSQKGDGDRPASPGLALFN 1562
Cdd:PHA03307 272 ASGWNGP----SSRPGPASSSSSPRERSP---------------SPSPssPGSGPAPSSPRASSSSSSSRESSSSSTSSS 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1563 GSGRASPPSTpPppppppgpppapyrpcahlafPPEPAPVNAGKAGPSAEAPkvhPKPNSAPVAGPCSSFPKIpySPVKA 1642
Cdd:PHA03307 333 SESSRGAAVS-P---------------------GPSPSRSPSPSRPPPPADP---SSPRKRPRPSRAPSSPAA--SAGRP 385
|
....*...
gi 62177127 1643 TRADARKA 1650
Cdd:PHA03307 386 TRRRARAA 393
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
255-282 |
5.49e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.78 E-value: 5.49e-04
10 20
....*....|....*....|....*...
gi 62177127 255 YWTPLHLAAKYGQTNLVKLLLMHQANPH 282
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1309-1526 |
5.53e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1309 SASYEAVSACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPAGAPGAAARVLT 1388
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPA 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1389 PgTPQCALPPAA----PPGDEDDSEPVYIEMLGHAAR-PDSPDPGESVYEEMKCCLPDDGGPGAGSFLLHGASPPLLHRA 1463
Cdd:PRK12323 456 A-APAAAARPAAagprPVAAAAAAAPARAAPAAAPAPaDDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADP 534
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62177127 1464 PEDEAAGPPGdacdiPPPFPNLLPHRPPLLVFPPTPvtcsPASDESPLTPLEVKKLPVLETNL 1526
Cdd:PRK12323 535 DDAFETLAPA-----PAAAPAPRAAAATEPVVAPRP----PRASASGLPDMFDGDWPALAARL 588
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1325-1556 |
7.64e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 44.68 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1325 AANEALARPRPHSDDYSTMKKIP-----PRKPKRSPNTKlsgsyEEISGSRPGdarpagapgaaarvlTPGTPQCALPPA 1399
Cdd:PTZ00449 602 SAQRPTRPKSPKLPELLDIPKSPkrpesPKSPKRPPPPQ-----RPSSPERPE---------------GPKIIKSPKPPK 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1400 AP--PGDEDDSEPVYIEMLGHAARPD----SPDPGESVYEEMKCCLPDDGGPgagSFLLHGASPPLLHRAPEDEAAgPPG 1473
Cdd:PTZ00449 662 SPkpPFDPKFKEKFYDDYLDAAAKSKetktTVVLDESFESILKETLPETPGT---PFTTPRPLPPKLPRDEEFPFE-PIG 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1474 DAcDIPPPFPNLLPHRPpllVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQPEgSSPLSPQySKSQKGDGDRP 1553
Cdd:PTZ00449 738 DP-DAEQPDDIEFFTPP---EEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDEAM-KRPDSPS-EHEDKPPGDHP 811
|
...
gi 62177127 1554 ASP 1556
Cdd:PTZ00449 812 SLP 814
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1389-1552 |
1.70e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.52 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1389 PGTPQCALPPAAPPGDEDDSEPVYIEMLGHAARPDSPDPGESVYEEMKcclPDDGGPGAgsfllhgASPPLLHRAPEDEA 1468
Cdd:PHA03378 698 PRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRAR---PPAAAPGR-------ARPPAAAPGRARPP 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1469 AGPPGDACDIPPP--------FPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETN-------LKYPVQPE 1533
Cdd:PHA03378 768 AAAPGAPTPQPPPqappapqqRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGvkrgrpsLKKPAALE 847
|
170
....*....|....*....
gi 62177127 1534 GSSPLSPQYSkSQKGDGDR 1552
Cdd:PHA03378 848 RQAAAGPTPS-PGSGTSDK 865
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1308-1651 |
2.02e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1308 LSASYEAVSACLSAAREAANealaRPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDArpagapgaaarvl 1387
Cdd:PHA03307 44 VSDSAELAAVTVVAGAAACD----RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSP------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1388 TPGTPQCALPPAA---PPGDEDDSEPVYIEMLGHAARPDSPDPGESVyeemkcCLPDDGGPGAGsfllHGASPPLLHRA- 1463
Cdd:PHA03307 107 TPPGPSSPDPPPPtppPASPPPSPAPDLSEMLRPVGSPGPPPAASPP------AAGASPAAVAS----DAASSRQAALPl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1464 ---PEDEAAGPPGDACDIPPPFPNLLPHRPPllvfPPTPVTCSPASDESPLTP--LEVKKLPVLETNLKYPVQ-----PE 1533
Cdd:PHA03307 177 sspEETARAPSSPPAEPPPSTPPAAASPRPP----RRSSPISASASSPAPAPGrsAADDAGASSSDSSSSESSgcgwgPE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1534 GSSPLSPQYSKSQKGDGDRPASPGLALFN-GSGRASPPSTPPPPPPPPGPPPAPYRPCAH-------------LAFPPEP 1599
Cdd:PHA03307 253 NECPLPRPAPITLPTRIWEASGWNGPSSRpGPASSSSSPRERSPSPSPSSPGSGPAPSSPrasssssssressSSSTSSS 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 62177127 1600 APVNAGKAGPSAEAPKVHPKPNSAPVAGPCSSFPKIPySPVKATRADARKAG 1651
Cdd:PHA03307 333 SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP-RPSRAPSSPAASAG 383
|
|
| NYAP_C |
pfam15452 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_C is a C-terminal ... |
1630-1858 |
2.30e-03 |
|
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_C is a C-terminal family of eukaryotic proteins that are substrates of tyrosine kinase in the brain. When first identified, the family members were referred to as unconventional myosin XVI, or Myr 8. However, proteins have now been identified as being integrally involved in neuronal function and morphogenesis. The family is involved in both the activation of phosphoinositide 3-kinase (PI3K) and the recruitment of the downstream effector WAVE complex to the close vicinity of PI3K; it also appears to regulate the brain size and neurite outgrowth in mice.
Pssm-ID: 464724 Cd Length: 259 Bit Score: 41.87 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1630 SSFPKIPYSPVKATRADARKAGSSASPPAPYSPPSSRPLSSPL--DELASLFNSGRSVLRKSAAGRKIREAEGFETNMNI 1707
Cdd:pfam15452 1 RSSPSVPHSTVKNQVQEGAKGGNAASISCGSAIAGSRSRTPTSplEELTSLFGSGWSLQRKLSSGRKSKEPAEKTDEARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1708 SS----------RDD-----PSTSEITSETQDRN---ANNHGIQLSN----SLSSAITAENGNSISNGLPEEdGYSRlSI 1765
Cdd:pfam15452 81 WSgsteplprmeREErghhgAGASGIPVRAQGWDgvdGPPGFRALSRlglpSPCQTFPACHRNGEPKEVCRL-GRSA-ST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1766 SGTGTSTFQRHRDSHT--TQVIHQLRLSENESV----ALQELLDWRRKLCEE------------GQDWQQIL----HHAE 1823
Cdd:pfam15452 159 SGVRQAGGDVPRQSSLplRQALSQSQVPPMQWVerdgKLLEVIERKRCLCKEikarrrpdkglcKQDSMPILpswrKNPE 238
|
250 260 270
....*....|....*....|....*....|....*
gi 62177127 1824 PRvpppppckkpsllkKPEGASCNRLPSELWDTTI 1858
Cdd:pfam15452 239 TR--------------KSGTPPCSRQQTVFWDTAI 259
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1389-1647 |
2.63e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1389 PGTPQCALPPaappgdeDDSEPvyiemlgHAARPdSPDPGESVYeemkcclPDDGGPGAGSFLlhgaSPPLLHRAPEDEA 1468
Cdd:PHA03247 2475 PGAPVYRRPA-------EARFP-------FAAGA-APDPGGGGP-------PDPDAPPAPSRL----APAILPDEPVGEP 2528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1469 AGP-------------PGDACDIPPPFPNLLPhrppllvfPPTPVTCSPASDESPlTPLEvkklPVLETNLKYP-VQPEG 1534
Cdd:PHA03247 2529 VHPrmltwirgleelaSDDAGDPPPPLPPAAP--------PAAPDRSVPPPRPAP-RPSE----PAVTSRARRPdAPPQS 2595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1535 SSPLSPqysksqKGDGDRPASPGlalfngsgrASPPSTPPPPPPPPGpppapyrpcahlAFPPEPAPVNAGKAGPSAEAP 1614
Cdd:PHA03247 2596 ARPRAP------VDDRGDPRGPA---------PPSPLPPDTHAPDPP------------PPSPSPAANEPDPHPPPTVPP 2648
|
250 260 270
....*....|....*....|....*....|...
gi 62177127 1615 KVHPKPNSAPvagPCSSFPKIPYSPVKATRADA 1647
Cdd:PHA03247 2649 PERPRDDPAP---GRVSRPRRARRLGRAAQASS 2678
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
1388-1651 |
2.72e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 42.74 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1388 TPGTPQCALP---PAAPPGDEDDSEPvyiemlGHAARPDSP-----DPGeSVYEE--MKCCLPDDGGPGagsfllhgasp 1457
Cdd:PHA03379 412 TYGTPRPPVEkprPEVPQSLETATSH------GSAQVPEPPpvhdlEPG-PLHDQhsMAPCPVAQLPPG----------- 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1458 PLLHRAPEDEAAGPPGDACDIPPPFPNLLPH--RP----PLLVFPPTPVTCSPasdesplTPLEVKKLPVLETNLKYPVQ 1531
Cdd:PHA03379 474 PLQDLEPGDQLPGVVQDGRPACAPVPAPAGPivRPweasLSQVPGVAFAPVMP-------QPMPVEPVPVPTVALERPVC 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1532 PegssplspqysksqkgdgdrpaSPGLALFNGSGRASPPSTPPPPPPPPGPPPAPYRpcahlafPPEPAPVNAGKAGPSA 1611
Cdd:PHA03379 547 P----------------------APPLIAMQGPGETSGIVRVRERWRPAPWTPNPPR-------SPSQMSVRDRLARLRA 597
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 62177127 1612 EA-PKVHP----------KPNSAPVAGPC----SSFPKIPYSPVkatrADARKAG 1651
Cdd:PHA03379 598 EAqPYQASvevqppqltqVSPQQPMEYPLepeqQMFPGSPFSQV----ADVMRAG 648
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
127-156 |
3.05e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.88 E-value: 3.05e-03
10 20 30
....*....|....*....|....*....|.
gi 62177127 127 WTPMHIACA-CDNPDIVLLLVLAGANVLLQD 156
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
1321-1504 |
3.18e-03 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 42.25 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1321 AAREAANEAlarPRPHSDDYSTMKKIPPRKPKRSPNT----KLSGSYEEISGSRPGDARPAGAPGAAARVLTPGTPQCAL 1396
Cdd:PHA03321 486 AAPPPEPAA---APSPATYYTRMGGGPPRLPPRNRATetlrPDWGPPAAAPPEQMEDPYLEPDDDRFDRRDGAAAAATSH 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1397 PPAAPPGDE--------DDSEPVYIEMlghaarpdspdPGESVYEEMkccLPD-DGGPGAGSFLLHGASPPLLHRAP--- 1464
Cdd:PHA03321 563 PREAPAPDDdpiyegvsDSEEPVYEEI-----------PTPRVYQNP---LPRpMEGAGEPPDLDAPTSPWVEEENPiyg 628
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 62177127 1465 -EDEAAGPPGDACDIPPPFPNLLPHRPPLLVFPPTPVTCSP 1504
Cdd:PHA03321 629 wGDSPLFSPPPAARFPPPDPALSPEPPALPAHRPRPGALAP 669
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
57-261 |
3.40e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 42.31 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 57 HFNLTDMLQDAiiHHNDKEVL-RLLK-EGADPHTLVSSGGSLLHLCARYDNAFIAEILID---RGVNVNHQDEDFW--TP 129
Cdd:cd22192 15 RISESPLLLAA--KENDVQAIkKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDLYQgeTA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 130 MHIACACDNPDIVLLLVLAGANVLLQDVNGnipldyavegtesssillTYLdengvdltslrqmkLQRPMSMLTDVKHFL 209
Cdd:cd22192 93 LHIAVVNQNLNLVRELIARGADVVSPRATG------------------TFF--------------RPGPKNLIYYGEHPL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 62177127 210 SsggnvnekndegvtllHMACAsGYKEVVSLILEHGGDLNIVDDQYWTPLHL 261
Cdd:cd22192 141 S----------------FAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
214-288 |
3.76e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 42.38 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 214 NVNEKNDEGVTLLHMAcASGYKEVVSLILEH-------GGDLNIVDDQYW-------TPLHLAAKYGQTNLVKLLLMHQA 279
Cdd:TIGR00870 74 NLSCRGAVGDTLLHAI-SLEYVDAVEAILLHllaafrkSGPLELANDQYTseftpgiTALHLAAHRQNYEIVKLLLERGA 152
|
90
....*....|
gi 62177127 280 NPHL-VNCNE 288
Cdd:TIGR00870 153 SVPArACGDF 162
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
79-133 |
4.04e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 4.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 62177127 79 LLKEG-ADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIA 133
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
259-309 |
4.32e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.17 E-value: 4.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 62177127 259 LHLAAKYGQTNLVKLLLMHQANPHLVNCNEEKASDIAAS----EFIEEMLLKAEI 309
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKnghlEIVKLLLEHADV 55
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
237-284 |
5.14e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.59 E-value: 5.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 62177127 237 VVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLV 284
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNII 207
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1321-1633 |
5.15e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1321 AAREAANE--ALARPRPHSddystmKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPAGAPGAAARVLTPGTPQcalPP 1398
Cdd:PHA03247 2687 AARPTVGSltSLADPPPPP------PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA---RP 2757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1399 AAPPGDEDDSEPVYIEMLGHAARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLLHGASPPLLHRAPEDEAAGPPGDACDI 1478
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT 2837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 1479 PPPFPNLlPHRPPLL----VFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQPEGSSPLSPQysksqkgDGDRPA 1554
Cdd:PHA03247 2838 APPPPPG-PPPPSLPlggsVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPD-------QPERPP 2909
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62177127 1555 SPglalfngsgrASPPSTPPPPPPPPgpppapyrpcahlafPPEPAPVNAGKAGPSAEAPkvhPKPNSAPVAGPCSSFP 1633
Cdd:PHA03247 2910 QP----------QAPPPPQPQPQPPP---------------PPQPQPPPPPPPRPQPPLA---PTTDPAGAGEPSGAVP 2960
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
125-152 |
5.16e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 5.16e-03
10 20
....*....|....*....|....*...
gi 62177127 125 DFWTPMHIACACDNPDIVLLLVLAGANV 152
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
127-152 |
5.75e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.08 E-value: 5.75e-03
10 20
....*....|....*....|....*.
gi 62177127 127 WTPMHIACACDNPDIVLLLVLAGANV 152
Cdd:pfam13606 3 NTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
64-183 |
6.31e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.40 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62177127 64 LQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHL----CARYDnafIAEILIDRGVNVNHQDEDF-WTPMHIacACDN 138
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIsvgyCKDYD---ILKLLLEHGVDVNAKSYILgLTALHS--SIKS 279
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 62177127 139 PDIVLLLVLAGANVLLQDVNGNIPLdyavegtesSSILLTYLDEN 183
Cdd:PHA02878 280 ERKLKLLLEYGADINSLNSYKLTPL---------SSAVKQYLCIN 315
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
223-295 |
7.38e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 7.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62177127 223 VTLLHMAcASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLVNCNEEKASDIA 295
Cdd:PTZ00322 84 VELCQLA-ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
|
| |
