|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
437-1155 |
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: 1362.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGARIY 596
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKHLTGARIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 597 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLAVLKRALNVVGF 676
Cdd:cd14878 161 TYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREDVSTAERSLNREKLAVLKQALNVVGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 677 SSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 756
Cdd:cd14878 241 SSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 757 FFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHE 836
Cdd:cd14878 321 FYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 837 QVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTNAVYSPMKDGNGNVA 916
Cdd:cd14878 401 QTECVQEGVTMETAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAVYSPMKDGNGNVA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 917 LKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLsqtgslvsaypsfkfrghksalls 996
Cdd:cd14878 481 LKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKL------------------------ 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 997 kkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFD 1076
Cdd:cd14878 537 ---------------------------------------VTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFD 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312147315 1077 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKLQGWQMGVRKVFLK 1155
Cdd:cd14878 578 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
438-1155 |
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: 668.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRS--ADLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGA-------SRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQL 590
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSgssksssSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQF-DPTGRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 591 TGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ-TIQDDASTGERSLNREKLAVLKR 669
Cdd:cd00124 159 VGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDyLNSSGCDRIDGVDDAEEFQELLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 670 ALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 747
Cdd:cd00124 239 ALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 748 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSmqTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 827
Cdd:cd00124 319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAES--TSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 828 INEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTNAvysp 907
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDFPDNQD-CLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF---- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 908 mkdgngnVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSenvvinhlfqsklsqtgslvsaypsfkf 987
Cdd:cd00124 472 -------SKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG---------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 988 rghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLMDIIGKLQKCTPHFIHCIRPN 1067
Cdd:cd00124 517 ----------------------------------------------------SQFRSQLDALMDTLNSTQPHFVRCIKPN 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1068 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQ-CKLQGWQ 1146
Cdd:cd00124 545 DEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLkLDSSGYQ 624
|
....*....
gi 312147315 1147 MGVRKVFLK 1155
Cdd:cd00124 625 LGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
426-1165 |
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: 615.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 426 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 505
Cdd:smart00242 9 EDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKY---RGKSRGELPPHVFAIADNAYRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 506 LFREQRPQCFILSGERGSGKSEASKQIIRHLTCRAGASRATldSRFKHVV----CILEAFGHAKTTLNDLSSCFIKYFEL 581
Cdd:smart00242 86 MLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV--GSVEDQIlesnPILEAFGNAKTLRNNNSSRFGKFIEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 582 QFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ------TIQDDAstg 655
Cdd:smart00242 164 HFDA-KGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQggcltvDGIDDA--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 656 erslnrEKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSA-FVSDLQLLEQVAGMLQVSTDELASAL 734
Cdd:smart00242 240 ------EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 735 TTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQ 814
Cdd:smart00242 314 TKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYF----IGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 815 LCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQS 894
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDW-TFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 895 LLEssNTNAVYSPMKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQ 974
Cdd:smart00242 469 HHK--KHPHFSKPKKKGR---------TEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 975 TGslvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLMDIIGKLQ 1054
Cdd:smart00242 538 AG-------------------SKKR-----------------------------------FQTVGSQFKEQLNELMDTLN 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1055 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCR 1134
Cdd:smart00242 564 STNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTW-PPWGGDAKKACE 642
|
730 740 750
....*....|....*....|....*....|...
gi 312147315 1135 LVLQQCKL--QGWQMGVRKVFLKYWHADQLNDL 1165
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 ... |
438-1155 |
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 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLY---RGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCeRKQQLTGARIYT 597
Cdd:cd01379 79 SGESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT-STGAVTGARISE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 598 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGL-HLNNLCAHRYLNQTIQDDASTGERSLNREKLAVLKRALNVVGF 676
Cdd:cd01379 158 YLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAKyKLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 677 SSLEVENLFVILAAILHLGDIRFTAL----NEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 752
Cdd:cd01379 238 TKEEVDSVYSILAAILHIGDIEFTEVesnhQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 753 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 832
Cdd:cd01379 318 EEATDARDAMAKALYGRLFSWIVNRINSLL-KPDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 833 FLHEQVECVQEGVTMET-AYSpgNQNGVLDFFFQKPSGFLTLLDEESQmiwsvesnFPKKL-QSLLESSNTNA----VYS 906
Cdd:cd01379 397 FAWEQQEYLNEGIDVDLiEYE--DNRPLLDMFLQKPMGLLALLDEESR--------FPKATdQTLVEKFHNNIkskyYWR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 907 PmkdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfk 986
Cdd:cd01379 467 P----------KSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 987 frghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRP 1066
Cdd:cd01379 517 --------------------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKP 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1067 NNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtFLREKKEQSAAERCRLVLQQCKLQGWQ 1146
Cdd:cd01379 547 NDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA--FKWNEEVVANRENCRLILERLKLDNWA 624
|
....*....
gi 312147315 1147 MGVRKVFLK 1155
Cdd:cd01379 625 LGKTKVFLK 633
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
426-1155 |
6.57e-166 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 522.23 E-value: 6.57e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 426 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 505
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAY---RGKRRGELPPHIFAIADEAYRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 506 LFREQRPQCFILSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFEL 581
Cdd:pfam00063 79 MLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRLEEQILqsnpILEAFGNAKTVRNNNSSRFGKYIEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 582 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSlnr 661
Cdd:pfam00063 159 QF-DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDS--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 662 EKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 741
Cdd:pfam00063 235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 742 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHS-QDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMT 820
Cdd:pfam00063 315 GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASF----IGVLDIYGFEIFEKNSFEQLCINYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 821 NEKMHHYINEVLFLHEQVECVQEGVTmetaYSP---GNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFpkkLQSLLE 897
Cdd:pfam00063 391 NEKLQQFFNHHMFKLEQEEYVREGIE----WTFidfGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTF---LDKLYS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 898 SSNTNAVY-SPMKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtG 976
Cdd:pfam00063 464 TFSKHPHFqKPRLQGE---------THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPD-----Y 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 977 SLVSAYPSFKFRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLMDIIGKLQKC 1056
Cdd:pfam00063 530 ETAESAAANESGKSTPKRTKKKR-----------------------------------FITVGSQFKESLGELMKTLNST 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1057 TPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEqSAAERCRLV 1136
Cdd:pfam00063 575 NPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKG-DAKKGCEAI 653
|
730 740
....*....|....*....|.
gi 312147315 1137 LQQCKLQG--WQMGVRKVFLK 1155
Cdd:pfam00063 654 LQSLNLDKeeYQFGKTKIFFR 674
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
438-1155 |
7.36e-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: 477.52 E-value: 7.36e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLY---RNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASratldSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLTGA 593
Cdd:cd01381 79 SGESGAGKTESTKLILQYLAAISGQH-----SWIEQQILeanpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV-IEGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 594 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNqtiQDDASTGERSLNREKLAVLKRALNV 673
Cdd:cd01381 153 KIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLT---QGNCLTCEGRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 674 VGFSSLEVENLFVILAAILHLGDIRFTALNEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 751
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNldASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 752 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSmQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 831
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDS-SRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 832 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQmiwsvesnFPKKL-QSLLESSN----TNAVYS 906
Cdd:cd01381 389 IFKLEQEEYDKEGINWQHIEFVDNQD-VLDLIALKPMNIMSLIDEESK--------FPKGTdQTMLEKLHsthgNNKNYL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 907 PMKdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsaypsfk 986
Cdd:cd01381 460 KPK--------SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM------------ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 987 frghksallskkmtassiigenknylelskllkkkGTSTflqrleRGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIRP 1066
Cdd:cd01381 520 -----------------------------------GSET------RKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKP 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1067 NNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKE---QSAAERCRLVLQQCKLq 1143
Cdd:cd01381 559 NEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTdcrAATRKICCAVLGGDAD- 637
|
730
....*....|..
gi 312147315 1144 gWQMGVRKVFLK 1155
Cdd:cd01381 638 -YQLGKTKIFLK 648
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
438-1155 |
3.93e-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: 474.95 E-value: 3.93e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVR--SQRPPHLFWIADQAYRRLLETGRNQCILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQLTGARIYT 597
Cdd:cd14897 80 SGESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTE-NGQLLGAKIDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 598 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL---NQTIQDDASTGERSLNREKLAVLKRALNVV 674
Cdd:cd14897 159 YLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILrddNRNRPVFNDSEELEYYRQMFHDLTNIMKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 675 GFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 754
Cdd:cd14897 239 GFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 755 AEFFRDLLAKSLYSRLFSFLVNTMNSCLH-SQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 833
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWpDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 834 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTnavYSPMKDGNg 913
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDD-VLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPR---YVASPGNR- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 914 nvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsaypsfkfrghksa 993
Cdd:cd14897 474 --------VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 994 llskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPD 1073
Cdd:cd14897 521 ---------------------------------------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1074 TFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlrEKKEQSAAERCRLVLQQCKLQGWQMGVRKVF 1153
Cdd:cd14897 556 KFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS--NKVRSDDLGKCQKILKTAGIKGYQFGKTKVF 633
|
..
gi 312147315 1154 LK 1155
Cdd:cd14897 634 LK 635
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
425-1238 |
2.83e-148 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 497.29 E-value: 2.83e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 425 NDDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFH 504
Cdd:COG5022 68 VDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY---SGKNRLELEPHVFAIAEEAYR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 505 QLFREQRPQCFILSGERGSGKSEASKQIIRHLTcRAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFE 580
Cdd:COG5022 145 NLLSEKENQTIIISGESGAGKTENAKRIMQYLA-SVTSSSTVEISSIEKQILatnpILEAFGNAKTVRNDNSSRFGKYIK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 581 LQFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLN 660
Cdd:COG5022 224 IEFDE-NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 661 REKLAvlkRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFvSDLQLLEQVAGMLQVSTDELASALTTDIQY 740
Cdd:COG5022 303 FKITL---DALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIF-SDNSVLDKACYLLGIDPSLFVKWLVKRQIK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 741 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL-HSQDEQKSmqtldIGILDIFGFEEFQKNEFEQLCVNM 819
Cdd:COG5022 379 TGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLdHSAAASNF-----IGVLDIYGFEIFEKNSFEQLCINY 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 820 TNEKMHHYINEVLFLHEQVECVQEGVtmetAYSP----GNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSL 895
Cdd:COG5022 454 TNEKLQQFFNQHMFKLEQEEYVKEGI----EWSFidyfDNQPCIDLIEKKNPLGILSLLDEECVMPHATDESFTSKLAQR 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 896 LeSSNTNAVYSPMKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsqt 975
Cdd:COG5022 530 L-NKNSNPKFKKSRFRD---------NKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE---- 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 976 gslvsaypsfkfrghksallskkmtassiigENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQK 1055
Cdd:COG5022 596 -------------------------------ENIE--------------------SKGRFPTLGSRFKESLNSLMSTLNS 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1056 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR---EKKEQSAAER 1132
Cdd:COG5022 625 TQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWtgeYTWKEDTKNA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1133 CRLVLQQCKL--QGWQMGVRKVFLKywhADQLNDLCLQ----LQRKIITCQKVIRGFLARQHLLQRISiRQQEVTS-INS 1205
Cdd:COG5022 705 VKSILEELVIdsSKYQIGNTKVFFK---AGVLAALEDMrdakLDNIATRIQRAIRGRYLRRRYLQALK-RIKKIQViQHG 780
|
810 820 830
....*....|....*....|....*....|....
gi 312147315 1206 FLQNTE-DMGLKTYDALVIQNASDIARENDRLRS 1238
Cdd:COG5022 781 FRLRRLvDYELKWRLFIKLQPLLSLLGSRKEYRS 814
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
439-1155 |
1.26e-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: 1.26e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 439 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLF----REQRPQC 514
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKS---SLPPHIFAVADRAYQSMLgrlaRGPKNQC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 515 FILSGERGSGKSEASKQIIRHLT--CRAGASratLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTG 592
Cdd:cd14889 80 IVISGESGAGKTESTKLLLRQIMelCRGNSQ---LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF--RNGHVKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 593 ARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDAstgERSLNREKLAVLKRALN 672
Cdd:cd14889 155 AKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKR---EVQYWKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 673 VVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSaFVSDLQ--LLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRH 750
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAL-KVENDSngWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 751 TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 830
Cdd:cd14889 311 TKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKD-DSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 831 VLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESsntNAVYSpmKD 910
Cdd:cd14889 390 HIFLMEQKEYKKEGIDWKEITYKDNKP-ILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG---NSYYG--KS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 911 GNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfrgh 990
Cdd:cd14889 464 RS-------KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPR--------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 991 ksallSKKMTASSiigenknylelskllkKKGTSTFLQrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSK 1070
Cdd:cd14889 528 -----AKLPQAGS----------------DNFNSTRKQ--------SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVK 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1071 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREKKEQSAAERCRLVLQQCKLQGWQMGVR 1150
Cdd:cd14889 579 VPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKLVGWKCGKT 654
|
....*
gi 312147315 1151 KVFLK 1155
Cdd:cd14889 655 RLFFK 659
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
443-1155 |
3.46e-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: 3.46e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 443 IQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILSGERG 522
Cdd:cd01378 7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESY---RGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 523 SGKSEASKQIIRHLTCRAGASRATLdSRFKHVV----CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYTY 598
Cdd:cd01378 84 AGKTEASKRIMQYIAAVSGGSESEV-ERVKDMLlasnPLLEAFGNAKTLRNDNSSRFGKYMEIQF-DFKGEPVGGHITNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 599 LLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ-------TIQDDAStgerslnrekLAVLKRAL 671
Cdd:cd01378 162 LLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKsgcfdvdGIDDAAD----------FKEVLNAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 672 NVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM---IIR 748
Cdd:cd01378 232 KVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAA-ISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 749 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHS-QDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 827
Cdd:cd01378 311 PLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAkSGGKKKV----IGVLDIYGFEIFEKNSFEQFCINYVNEKLQQI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 828 INEVLFLHEQVECVQEGVTMETayspgnqngvLDFFF---------QKPSGFLTLLDEESqmiwsvesNFPKK------L 892
Cdd:cd01378 387 FIELTLKAEQEEYVREGIEWTP----------IKYFNnkiicdlieEKPPGIFAILDDAC--------LTAGDatdqtfL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 893 QSLLESSNTNAVYSPMKDgngnvALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKL 972
Cdd:cd01378 449 QKLNQLFSNHPHFECPSG-----HFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 973 SQTgslvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLMDIIGK 1052
Cdd:cd01378 524 DLD--------------------SKKR-----------------------------------PPTAGTKFKNSANALVET 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1053 LQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtflrekKEQSAA-- 1130
Cdd:cd01378 549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS-------PKTWPAwd 621
|
730 740 750
....*....|....*....|....*....|.
gi 312147315 1131 ----ERCRLVLQQCKLQG--WQMGVRKVFLK 1155
Cdd:cd01378 622 gtwqGGVESILKDLNIPPeeYQMGKTKIFIR 652
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
1243-1590 |
4.49e-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: 445.37 E-value: 4.49e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1243 PYHKEKLEVRNMQEEGSKR---------TDDKSGPRHFHPSSMSVCAAVDGLG-QCLVGPSIWSPSLHSVFSMDDSSSLP 1312
Cdd:pfam15439 1 LYRKEKLEKRRRQEEGIKRsgeevagkvRDISSEGRHFRMGFMTMPASQDRLPhPCAAGMSIRSQSLHSVGSGDEDGSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1313 SPRKQPPPKPKRDPNTRLSASYEAVSACLS-AAREAA--NEALARPRPHSDDYStmKKIPPRKPKRSPNTKLSGSYEEIS 1389
Cdd:pfam15439 81 SSRKQPPPKPKRDPSTKLSMSSEAVSAGLSaGAKETPseTEALSKPRPHSDEYS--RKIPPPKPKRSPNTQLSGSFDEIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1390 G--SRPGdarpagapgaaarvltpGTPQCALPPAAP---PGDEDDSEPVYIEMLGHAAR-------PDSPDPGESVYEEM 1457
Cdd:pfam15439 159 ApyIRPH-----------------GLLQRASSSDGPspaPLPDEEEEPVYIEMVGNVLRdfspttpDDDPDQSEAVYEEM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1458 KCCLPDDGGPGAGsfLLHGASPPLL-----HRAPEDE--------AAGPPGDACDIPPPFPNLLPHRPPLLVFPPTPVTC 1524
Cdd:pfam15439 222 KYPLPEDSGAANG--PPPLASSPLLadphsPISPESDsalpssqcATPTKKDLCDIPAPFPNLLPHRPPLLVFPPAPVTC 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312147315 1525 SPASDESPLTPLEVKKLPVLEtNLKYPVQPEgSSPLSPQYSKSQKGDGDRPASPGLALFNGSGRAS 1590
Cdd:pfam15439 300 SPASDESPLTPLEVKKLPVLE-NVSYSKQPA-SSPLSPQESKHQREDKDRPSSPGLAVLTPSGRAR 363
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
438-1155 |
1.05e-140 |
|
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: 1.05e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFsssGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYF---GKRMGALPPHIFALAEAAYTNMQEDGKNQSVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLtcragASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGA 593
Cdd:cd14883 79 SGESGAGKTETTKLILQYL-----CAVTNNHSWVEQQILeantILEAFGNAKTVRNDNSSRFGKFIEVCF-DASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 594 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG--LSAEEKYGLHLNNLCAHRYLNQtiqDDASTGERSLNREKLAVLKRAL 671
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQ---SGCIRIDNINDKKDFDHLRLAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 672 NVVGFSSLEVENLFVILAAILHLGDIRFtALNEGNSA--FVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 749
Cdd:cd14883 230 NVLGIPEEMQEGIFSVLSAILHLGNLTF-EDIDGETGalTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 750 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 829
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRF----IGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 830 EVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNtnavYSPMK 909
Cdd:cd14883 385 HYVFKLEQEEYEKEGINWSHIVFTDNQE-CLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHP----YYEKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 910 DGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLF--QSKLSQTGSLVSAYPSFKF 987
Cdd:cd14883 460 DR------RRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtyPDLLALTGLSISLGGDTTS 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 988 RGHKsallSKKMTASSiigenknylelskllkkkgtstflqrlergdpvTIASQLRkSLMDIigkLQKCTPHFIHCIRPN 1067
Cdd:cd14883 534 RGTS----KGKPTVGD---------------------------------TFKHQLQ-SLVDV---LSATQPWYVRCIKPN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1068 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEQSAAERCRLVLQQCKLQG--W 1145
Cdd:cd14883 573 SLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCL-DPRARSADHKETCGAVRALMGLGGLPEdeW 651
|
730
....*....|
gi 312147315 1146 QMGVRKVFLK 1155
Cdd:cd14883 652 QVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
440-1155 |
5.48e-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: 436.34 E-value: 5.48e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 440 LYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILS 518
Cdd:cd01384 4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQY---KGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 519 GERGSGKSEASKQIIRHLTCRAGasRATLDSRF--KHVV---CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGA 593
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRSveQQVLesnPLLEAFGNAKTVRNNNSSRFGKFVEIQF-DDAGRISGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 594 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiqdDASTGERSLNREKLAVLKRALNV 673
Cdd:cd01384 158 AIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQS---KCFELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 674 VGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSD---LQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRH 750
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 751 TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 830
Cdd:cd01384 315 DPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRL----IGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 831 VLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLqsllessntnavYSPMKD 910
Cdd:cd01384 391 HVFKMEQEEYTKEEIDWSYIEFVDNQD-VLDLIEKKPGGIIALLDEACMFPRSTHETFAQKL------------YQTLKD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 911 GNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKD---SLSQNLLfvmKTSENVVINHLFQSKLSQTGSlvsayPSFKF 987
Cdd:cd01384 458 HKRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKDyvvAEHQALL---NASKCPFVAGLFPPLPREGTS-----SSSKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 988 rghksallskkmtaSSiigenknylelskllkkkgtstflqrlergdpvtIASQLRKSLMDIIGKLQKCTPHFIHCIRPN 1067
Cdd:cd01384 530 --------------SS----------------------------------IGSRFKQQLQELMETLNTTEPHYIRCIKPN 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1068 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAerCRLVLQQCKLQGWQM 1147
Cdd:cd01384 562 NLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAA--CKKILEKAGLKGYQI 639
|
....*...
gi 312147315 1148 GVRKVFLK 1155
Cdd:cd01384 640 GKTKVFLR 647
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
437-1155 |
5.88e-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: 437.96 E-value: 5.88e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSsgKLcSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNR--RL-GKLPPHIFAIADVAYHAMLRKKKNQCIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTC------RAGASRATLDSRfkhvvCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQL 590
Cdd:cd01385 78 ISGESGSGKTESTNFLLHHLTAlsqkgyGSGVEQTILGAG-----PVLEAFGNAKTAHNNNSSRFGKFIQVNYRE-NGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 591 TGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiqdDASTGERSLNREKLAVLKRA 670
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQS---DCYTLEGEDEKYEFERLKQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 671 LNVVGFSSLEVENLFVILAAILHLGDIRFT--ALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 748
Cdd:cd01385 229 MEMVGFLPETQRQIFSVLSAVLHLGNIEYKkkAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLIL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 749 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 828
Cdd:cd01385 309 PYKLPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 829 NEVLFLHEQVECVQEGVTMETAYSPGNqNGVLDFFFQKPSGFLTLLDEesqmiwsvESNFPKKL-QSLLESSNTNAVYSP 907
Cdd:cd01385 389 NQHIFKLEQEEYKKEGISWHNIEYTDN-TGCLQLISKKPTGLLCLLDE--------ESNFPGATnQTLLAKFKQQHKDNK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 908 MKDGNgnvALKDhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgSLVSAYPSFKF 987
Cdd:cd01385 460 YYEKP---QVME--PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVR-----------ELIGIDPVAVF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 988 RghkSALLS---KKMTASSIIGEN--KNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLMDIIGKLQKCTPHFIH 1062
Cdd:cd01385 524 R---WAVLRaffRAMAAFREAGRRraQRTAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIR 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1063 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKpladtFLREKKEQSAAERCRLVLQQCKL 1142
Cdd:cd01385 601 CIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQ-----VLLPKGLISSKEDIKDFLEKLNL 675
|
730
....*....|....*
gi 312147315 1143 Q--GWQMGVRKVFLK 1155
Cdd:cd01385 676 DrdNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
438-1155 |
7.96e-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: 7.96e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQY---SGRALGELPPHLFAIANLAFAKMLDAKQNQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARIYT 597
Cdd:cd01387 79 SGESGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF--EGGVIVGAITSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 598 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiQDDASTGERSlnREKLAVLKRALNVVGFS 677
Cdd:cd01387 157 YLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQG-GNCEIAGKSD--ADDFRRLLAAMQVLGFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 678 SLEVENLFVILAAILHLGDIRF-----TALNEGNSaFVSDLQLlEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 752
Cdd:cd01387 234 SEEQDSIFRILASVLHLGNVYFhkrqlRHGQEGVS-VGSDAEI-QWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 753 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQksmqTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 832
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQD----TLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 833 FLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEesqmiwsvESNFPKKLQ-SLLESSN----TNAVYSP 907
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAFADNQP-VINLISKKPVGILHILDD--------ECNFPQATDhSFLEKCHyhhaLNELYSK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 908 MKDGngnvalkdhGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsaypsfkf 987
Cdd:cd01387 459 PRMP---------LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQ------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 988 rgHKSALLSKkmtassiigenknylelskllkkkGTSTFLQRLERGDpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPN 1067
Cdd:cd01387 517 --TDKAPPRL------------------------GKGRFVTMKPRTP--TVAARFQDSLLQLLEKMERCNPWFVRCLKPN 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1068 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKLQG-WQ 1146
Cdd:cd01387 569 HKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPKDmYR 648
|
....*....
gi 312147315 1147 MGVRKVFLK 1155
Cdd:cd01387 649 LGATKVFLR 657
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
438-1155 |
4.42e-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: 428.27 E-value: 4.42e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLcsSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY---RQKL--LDSPHVYAVADTAYREMMRDEINQSIII 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASRAtLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 597
Cdd:cd01383 77 SGESGAGKTETAKIAMQYLAALGGGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHF-DAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 598 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ----TIQ--DDAstgerslnrEKLAVLKRAL 671
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQsnclTIDgvDDA---------KKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 672 NVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 751
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 752 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 831
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRS---ISILDIYGFESFQKNSFEQLCINYANERLQQHFNRH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 832 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLessNTNAVYSpmkdg 911
Cdd:cd01383 383 LFKLEQEEYELDGIDWTKVDFEDNQE-CLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHL---KSNSCFK----- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 912 ngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSEnvviNHLFQsklsqtgslvsaypsfkfrghk 991
Cdd:cd01383 454 ------GERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCS----CQLPQ---------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 992 saLLSKKMTassiigenkNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKL 1071
Cdd:cd01383 502 --LFASKML---------DASRKALPLTKASGSDSQKQ-------SVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQL 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1072 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKpladtFLREKKE---QSAAERCRLVLQQCKLQG--WQ 1146
Cdd:cd01383 564 PGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYG-----FLLPEDVsasQDPLSTSVAILQQFNILPemYQ 638
|
....*....
gi 312147315 1147 MGVRKVFLK 1155
Cdd:cd01383 639 VGYTKLFFR 647
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
438-1155 |
9.97e-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: 421.18 E-value: 9.97e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd01380 2 AVLHNLKVRFCQrNAIYTYCGIVLVAINPYEDLPIYGEDIIQAY---SGQNMGELDPHIFAIAEEAYRQMARDEKNQSII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTcRAGASRATLDSRFKHVVC---ILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGA 593
Cdd:cd01380 79 VSGESGAGKTVSAKYAMRYFA-TVGGSSSGETQVEEKVLAsnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKN-YRIIGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 594 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ----TIQ--DDAstgerslnrEKLAVL 667
Cdd:cd01380 157 NMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQggspVIDgvDDA---------AEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 668 KRALNVVGFSSLEVENLFVILAAILHLGDIRFTAlNEGNSAFVS-DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 746
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKA-TRNDSASISpDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 747 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 826
Cdd:cd01380 307 VKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHSF--IGVLDIYGFETFEVNSFEQFCINYANEKLQQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 827 YINEVLFLHEQVECVQEGVTMETAYSPGNQnGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL-QSLLESSntNAVY 905
Cdd:cd01380 385 QFNQHVFKLEQEEYVKEEIEWSFIDFYDNQ-PCID-LIEGKLGILDLLDEECRLPKGSDENWAQKLyNQHLKKP--NKHF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 906 SPMKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvvinhlfqsklsqtgslvsaypsf 985
Cdd:cd01380 461 KKPRFSN---------TAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN------------------------ 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 986 kfrgHKSallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIR 1065
Cdd:cd01380 508 ----RKK--------------------------------------------TVGSQFRDSLILLMETLNSTTPHYVRCIK 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1066 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA---DTFLREKKEQSAAERCRLVLQQCKl 1142
Cdd:cd01380 540 PNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLpskEWLRDDKKKTCENILENLILDPDK- 618
|
730
....*....|...
gi 312147315 1143 qgWQMGVRKVFLK 1155
Cdd:cd01380 619 --YQFGKTKIFFR 629
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
437-1155 |
1.12e-127 |
|
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: 1.12e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCF 515
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQY---SRRHLGELPPHIFAIANECYRCLWKRHDNQCI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 516 ILSGERGSGKSEASKQIIRHLTC----RAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQFCErK 587
Cdd:cd14873 78 LISGESGAGKTESTKLILKFLSVisqqSLELSLKEKTSCVEQAILesspIMEAFGNAKTVYNNNSSRFGKFVQLNICQ-K 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 588 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQT--IQDDASTGERSLNRekla 665
Cdd:cd14873 157 GNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSgcVEDKTISDQESFRE---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 666 VLKrALNVVGFSSLEVENLFVILAAILHLGDIRFtaLNEGnSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 745
Cdd:cd14873 233 VIT-AMEVMQFSKEEVREVSRLLAGILHLGNIEF--ITAG-GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 746 IIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSmqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 825
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKS-----IGILDIFGFENFEVNHFEQFNINYANEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 826 HYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSlLESSNTNAVY 905
Cdd:cd14873 384 EYFNKHIFSLEQLEYSREGLVWEDIDWIDNGE-CLD-LIEKKLGLLALINEESHFPQATDSTLLEKLHS-QHANNHFYVK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 906 SPMKDGNgnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvsaypsf 985
Cdd:cd14873 461 PRVAVNN-----------FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQ-------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 986 kfrghksallSKKMTASsiigenknylelskllkkkgtstflqrlERGDPvTIASQLRKSLMDIIGKLQKCTPHFIHCIR 1065
Cdd:cd14873 522 ----------DTLKCGS----------------------------KHRRP-TVSSQFKDSLHSLMATLSSSNPFFVRCIK 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1066 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlreKKEQSAAERCRLVLQQCKLQG- 1144
Cdd:cd14873 563 PNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL---ALPEDVRGKCTSLLQLYDASNs 639
|
730
....*....|..
gi 312147315 1145 -WQMGVRKVFLK 1155
Cdd:cd14873 640 eWQLGKTKVFLR 651
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
437-1148 |
2.25e-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: 409.55 E-value: 2.25e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPK---EMPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGaSRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 596
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAG-STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF-DNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 597 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLhlNNLCAHRYLNQTIQDDASTGERSLNREKLavlKRALNVVGF 676
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLSLSGCIEVEGVDDVADFEEV---VLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 677 SSLEVENLFVILAAILHLGDIRFTAL---NEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG--DMIIRRHT 751
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGggkSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcdPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 752 IQiAEFFRDLLAKSLYSRLFSFLVNTMNSclhSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 831
Cdd:cd14872 311 AQ-ATDACDALAKAAYSRLFDWLVKKINE---SMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 832 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQsllessNTNAVYSPMKDG 911
Cdd:cd14872 387 TFKLEEALYQSEGVKFEHIDFIDNQP-VLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAAN------QTHAAKSTFVYA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 912 NgnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsayPSFKFRghk 991
Cdd:cd14872 460 E----VRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------PPSEGD--- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 992 sallskkmtassiigenknylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKL 1071
Cdd:cd14872 519 ---------------------------------------QKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1072 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-ADTFLREKKeqSAAERCRLVLQ---QCKlQGWQM 1147
Cdd:cd14872 560 ARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLvKTIAKRVGP--DDRQRCDLLLKslkQDF-SKVQV 636
|
.
gi 312147315 1148 G 1148
Cdd:cd14872 637 G 637
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
438-1155 |
1.64e-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: 1.64e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKY---KGKRREEMPPHIFAIADNAYRNMLQDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVC---------ILEAFGHAKTTLNDLSSCFIKYFELQFCErKQ 588
Cdd:cd01377 79 TGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLedqilqanpILEAFGNAKTVRNNNSSRFGKFIRIHFGS-TG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 589 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ----TI--QDDAstgerslnrE 662
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgelTIdgVDDA---------E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 663 KLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIqyFK 742
Cdd:cd01377 229 EFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPR--IK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 743 -GDMIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 820
Cdd:cd01377 307 vGREWVTKGqNKEQVVFSVGALAKALYERLFLWLVKRINKTL----DTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 821 NEKMHHYINEVLFLHEQVECVQEGVTMEtayspgnqngVLDF---------FFQKPS-GFLTLLDEESQMIWSVESNFPK 890
Cdd:cd01377 383 NEKLQQFFNHHMFVLEQEEYKKEGIEWT----------FIDFgldlqptidLIEKPNmGILSILDEECVFPKATDKTFVE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 891 KLQSLLESSNTNAVYSPMKDGngnvalKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS 970
Cdd:cd01377 453 KLYSNHLGKSKNFKKPKPKKS------EAH---FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKD 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 971 KLSQTGSlvsaypSFKFRGHKSALLskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDII 1050
Cdd:cd01377 524 YEESGGG------GGKKKKKGGSFR-----------------------------------------TVSQLHKEQLNKLM 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1051 GKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAA 1130
Cdd:cd01377 557 TTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKA 636
|
730 740
....*....|....*....|....*..
gi 312147315 1131 ErCRLVLQQCKL--QGWQMGVRKVFLK 1155
Cdd:cd01377 637 A-CEKILKALQLdpELYRIGNTKVFFK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
438-1155 |
3.93e-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: 398.30 E-value: 3.93e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcsSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSI----SKSPHVFSTASSAYQGMCNNKKSQTIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCrAGAS----RATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQ---- 588
Cdd:cd14888 78 ISGESGAGKTESTKYVMKFLAC-AGSEdikkRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKSkrms 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 589 ----QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHL--NNLCAHR-YLNQTIQDDASTGERSLNR 661
Cdd:cd14888 157 gdrgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYeeNDEKLAKgADAKPISIDMSSFEPHLKF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 662 EKLAV--------------LKR---ALNVVGFSSLEVENLFVILAAILHLGDIRFTAlNEGNS--AFVSDLQL--LEQVA 720
Cdd:cd14888 237 RYLTKsschelpdvddleeFEStlyAMQTVGISPEEQNQIFSIVAAILYLGNILFEN-NEACSegAVVSASCTddLEKVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 721 GMLQVSTDELASALTTDiqyfkgdMIIRRH-------TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSclhSQDEQKSMQT 793
Cdd:cd14888 316 SLLGVDAEDLLNALCYR-------TIKTAHefytkplRVDEAEDVRDALARALYSCLFDKVVERTNE---SIGYSKDNSL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 794 LDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTL 873
Cdd:cd14888 386 LFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCV-DLLQEKPLGIFCM 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 874 LDEESQmiwsvesnFPK-KLQSLlessnTNAVYSPMKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNL 952
Cdd:cd14888 465 LDEECF--------VPGgKDQGL-----CNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 953 LFVMKTSENVVINHLFQSKLSqtgslvsaypsfkfRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrler 1032
Cdd:cd14888 532 QEVIKNSKNPFISNLFSAYLR--------------RGTDGNTKKKKF--------------------------------- 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1033 gdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSR 1112
Cdd:cd14888 565 ---VTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYND 641
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 312147315 1113 YKPLADTFLREkkeqsaaercrlvlqqcKLQGWQMGVRKVFLK 1155
Cdd:cd14888 642 YRILLNGEGKK-----------------QLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
439-1113 |
5.07e-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: 389.39 E-value: 5.07e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 439 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFS-----SSGKLCSSLPPHLFSCVERAFHQLFREQRP 512
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiiqnGEYFDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 513 QCFILSGERGSGKSEASKQIIRHLT-------------------CRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSS 573
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTqlsqqeqnseevltltssiRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 574 CFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAE--EKYGLhLNNLCAHR--YLNQTIQ 649
Cdd:cd14907 163 RFGKYVSILVDKKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQllQQLGL-KNQLSGDRydYLKKSNC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 650 DDASTgersLNREKL-AVLKRALNVVGFSSLEVENLFVILAAILHLGDIRF--TALNEGNSAFVSDLQLLEQVAGMLQVS 726
Cdd:cd14907 242 YEVDT----INDEKLfKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVKNKETLQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 727 TDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSM----QTLDIGILDIF 802
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQQlfqnKYLSIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 803 GFEEFQKNEFEQLCVNMTNEKMHH-YINEVlFLHEQVECVQEGVT---METAYsPGNQNgVLDFFFQKPSGFLTLLDEES 878
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQlYISYV-FKAEEQEFKEEGLEdylNQLSY-TDNQD-VIDLLDKPPIGIFNLLDDSC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 879 QMIWSVESNFPKKLQSLLESSNTNAVYSPMKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKT 958
Cdd:cd14907 475 KLATGTDEKLLNKIKKQHKNNSKLIFPNKINK-----------DTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQN 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 959 SENVVINHLF----QSKLSQTGSLVSAYPSFKFRGHKsalLSKKMtassiigenknylelskllkkkgtstflqrlergd 1034
Cdd:cd14907 544 SKNRIISSIFsgedGSQQQNQSKQKKSQKKDKFLGSK---FRNQM----------------------------------- 585
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312147315 1035 pvtiasqlrKSLMDiigKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1113
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 ... |
439-1155 |
1.54e-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: 1.54e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 439 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFR----EQRPQC 514
Cdd:cd14892 3 LLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASSPPPHVFSIAERAYRAMKGvgkgQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 515 FILSGERGSGKSEASKQIIRHLTC----RAGASR----ATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQ 582
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLATasklAKGASTskgaANAHESIEECVLlsnlILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 583 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQtiqDDASTGERSLNRE 662
Cdd:cd14892 163 Y-NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQ---GNCVEVDGVDDAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 663 KLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFT--ALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTD-IQ 739
Cdd:cd14892 239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEenADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQtTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 740 YFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSClHSQDEQKSMQTLD-------IGILDIFGFEEFQKNEF 812
Cdd:cd14892 319 TARGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAC-HKQQTSGVTGGAAsptfspfIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 813 EQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQNG-VLDFFFQKPSGFLTLLDEesQMIWSVESNfPKK 891
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGI--DVSAIEFQDNQdCLDLIQKKPLGLLPLLEE--QMLLKRKTT-DKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 892 LQSLLESSN--TNAVYSPMKDGNgnvalkDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSEnvvinhlfq 969
Cdd:cd14892 473 LLTIYHQTHldKHPHYAKPRFEC------DE---FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS--------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 970 sklsqtgslvsaypsfKFRghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLrKSLMDI 1049
Cdd:cd14892 535 ----------------KFR---------------------------------------------------TQL-AELMEV 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1050 igkLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA------DTFLRE 1123
Cdd:cd14892 547 ---LWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvAASPDA 623
|
730 740 750
....*....|....*....|....*....|...
gi 312147315 1124 KKEQSAAERCR-LVLQQCKLQGWQMGVRKVFLK 1155
Cdd:cd14892 624 CDATTARKKCEeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
438-1155 |
8.63e-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: 8.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRP---- 512
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLY---HGTTAGELPPHVFAIADHAYTQLIQSGVLdpsn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 513 QCFILSGERGSGKSEASKQIIRHLT--------CRAGASRATLDSRFKHVVC----------ILEAFGHAKTTLNDLSSC 574
Cdd:cd14890 79 QSIIISGESGAGKTEATKIIMQYLAritsgfaqGASGEGEAASEAIEQTLGSledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 575 FIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAH-RYLNQTIQ---- 649
Cdd:cd14890 159 FGKFIEIQF-DHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYfYLRGECSSipsc 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 650 DDAstgerslnrEKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEG-NSAFVSDLQLLEQVAGMLQVSTD 728
Cdd:cd14890 238 DDA---------KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTtVLEDATTLQSLKLAAELLGVNED 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 729 ELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQ 808
Cdd:cd14890 309 ALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTI----SSPDDKWGFIGVLDIYGFEKFE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 809 KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQN-GVLDFFFQKPSG----FLTLLDeesqmIW- 882
Cdd:cd14890 385 WNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGI--DWQYITFNDNqACLELIEGKVNGkpgiFITLDD-----CWr 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 883 --SVESNfpKKLQSLLESSntnavYSPMKDGNGNVALK-----------DHGTAFTIMHYAGRVMYDVVGAIEKNKDSLS 949
Cdd:cd14890 458 fkGEEAN--KKFVSQLHAS-----FGRKSGSGGTRRGSsqhphfvhpkfDADKQFGIKHYAGDVIYDASGFNEKNNETLN 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 950 QNLLFVMKTSEnvvinhlfqsklsqtgslvsaypsfkfrghksallskkmtaSSIigenknylelskllkkkgtstflqr 1029
Cdd:cd14890 531 AEMKELIKQSR-----------------------------------------RSI------------------------- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1030 leRGdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDF 1109
Cdd:cd14890 545 --RE--VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSF 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 312147315 1110 LSRYKPLADTflREKKEQsaaercrLVLQQCKLQG-----WQMGVRKVFLK 1155
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 ... |
438-1155 |
1.69e-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: 375.66 E-value: 1.69e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14896 2 SVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASY---HPRKALNTTPHIFAIAASAYRLSQSTGQDQCILL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTC----RAGASRATLDSrfkhVVCILEAFGHAKTTLNDLSSCFIKYFELqfCERKQQLTGA 593
Cdd:cd14896 79 SGHSGSGKTEAAKKIVQFLSSlyqdQTEDRLRQPED----VLPILESFGHAKTILNANASRFGQVLRL--HLQHGVIVGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 594 RIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSlnrEKLAVLKRALNV 673
Cdd:cd14896 153 SVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDA---QDFEGLLKALQG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 674 VGFSSLEVENLFVILAAILHLGDIRFTAlNEGNS---AFVSDLQLLEQVAGMLQVSTDELASALT---TDIQYfkgDMII 747
Cdd:cd14896 230 LGLCAEELTAIWAVLAAILQLGNICFSS-SERESqevAAVSSWAEIHTAARLLQVPPERLEGAVThrvTETPY---GRVS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 748 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 827
Cdd:cd14896 306 RPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDAT--IGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 828 INEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFpkkLQSLLESSNTNAVYSP 907
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIPQPPRES-CLDLLVDQPHSLLSILDDQTWLSQATDHTF---LQKCHYHHGDHPSYAK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 908 MKdgngnVALKdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkf 987
Cdd:cd14896 460 PQ-----LPLP----VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYG----------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 988 rghksallskkmtassiigenknylelskllkkkgtstflqrLERGDPvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPN 1067
Cdd:cd14896 520 ------------------------------------------LGQGKP-TLASRFQQSLGDLTARLGRSHVYFIHCLNPN 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1068 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADtflREKKEQSAAERCRLVLQQckLQG--- 1144
Cdd:cd14896 557 PGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS---ERQEALSDRERCGAILSQ--VLGaes 631
|
730
....*....|...
gi 312147315 1145 --WQMGVRKVFLK 1155
Cdd:cd14896 632 plYHLGATKVLLK 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
438-1155 |
2.94e-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: 2.94e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLcsSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14903 2 AILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKE--ELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 597
Cdd:cd14903 80 SGESGAGKTETTKILMNHLATIAGGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF-DKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 598 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAH--RYLNQTIQDDAstgerslNREKLAVLKRALNVVG 675
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYtgANKTIKIEGMS-------DRKHFARTKEALSLIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 676 FSSLEVENLFVILAAILHLGDIRFTA--LNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQ 753
Cdd:cd14903 232 VSEEKQEVLFEVLAGILHLGQLQIQSkpNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 754 IAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 833
Cdd:cd14903 312 QAEDCRDALAKAIYSNVFDWLVATINASL----GNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 834 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKpSGFLTLLDEESQMIWSVESNFPKKLQSLLEsSNTNAVYSPmkdgng 913
Cdd:cd14903 388 KTVQIEYEEEGIRWAHIDFADNQD-VLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHK-DEQDVIEFP------ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 914 nvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKSA 993
Cdd:cd14903 459 ----RTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 994 LLSKkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPD 1073
Cdd:cd14903 535 LTTT---------------------------------------TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPT 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1074 TFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYkplaDTFLREKKE--QSAAERCRLVLQQCKLQG---WQMG 1148
Cdd:cd14903 576 ELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKF----WLFLPEGRNtdVPVAERCEALMKKLKLESpeqYQMG 651
|
....*..
gi 312147315 1149 VRKVFLK 1155
Cdd:cd14903 652 LTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
437-1114 |
1.81e-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: 364.26 E-value: 1.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCF 515
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSY---QGKSLGTLPPHVFAIADKAYRDMKVLKQSQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 516 ILSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 595
Cdd:cd01382 78 IVSGESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHF-NEKSSVVGGFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 596 YTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLhlnnlcahryLNQTIQDDAstgerslnrEKLAVLKRALNVVG 675
Cdd:cd01382 157 SHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------LKDPLLDDV---------GDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 676 FSSLEVENLFVILAAILHLGDIRFTALNEGNSA----FVSDLQLLEQVAGMLQVSTDELASALTTDIQY-----FKGDMI 746
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgcnvKPKSEQSLEYAAELLGLDQDELRVSLTTRVMQttrggAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 747 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQdeqKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 826
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE---TSSYF--IGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 827 YINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFpkklqsllessnTNAVYS 906
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEYVDNQD-CIDLIEAKLVGILDLLDEESKLPKPSDQHF------------TSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 907 PMKDgNGNVA------LKDHGT-----AFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 975
Cdd:cd01382 440 KHKN-HFRLSiprkskLKIHRNlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNN 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 976 GSLVSAypsfkfrghksallSKKMTASSIigenknylelskllkkkgTSTFlqrlergdpvtiASQLrKSLMDiigKLQK 1055
Cdd:cd01382 519 KDSKQK--------------AGKLSFISV------------------GNKF------------KTQL-NLLMD---KLRS 550
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 312147315 1056 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYK 1114
Cdd:cd01382 551 TGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYK 609
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
438-1155 |
1.94e-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: 1.94e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvsQLY----FSSSGKLCSSLPPHLFSCVERAFHQLFRE---- 509
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYdlhkYREEMPGWTALPPHVFSIAEGAYRSLRRRlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 510 ---QRPQCFILSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVC---------ILEAFGHAKTTLNDLSSCFIK 577
Cdd:cd14895 75 gasKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISgsellsanpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 578 Y----FELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAH--RYLNQTIQDD 651
Cdd:cd14895 155 FvrmfFEGHELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQefQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 652 ASTGERslNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGN---------------SAFVSDL--- 713
Cdd:cd14895 235 RNDGVR--DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLtvq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 714 QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL----HSQDEQK 789
Cdd:cd14895 313 QHLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqFALNPNK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 790 SMQ---TLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNqNGVLDFFFQ 865
Cdd:cd14895 393 AANkdtTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLqYQFIQDIL-LTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 866 KPSGFLTLLDEESQMIWSVESNFPKKL-QSLLESSNTNAVYSPMKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKN 944
Cdd:cd14895 471 RPSGIFSLLDEECVVPKGSDAGFARKLyQRLQEHSNFSASRTDQAD-----------VAFQIHHYAGAVRYQAEGFCEKN 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 945 KDSLSQNLLFVMKTSENVVINHLFQS-KLSQTGSLVSAYPsfKFRGHKSALLSkkmtassiigenknylelskllkkkgt 1023
Cdd:cd14895 540 KDQPNAELFSVLGKTSDAHLRELFEFfKASESAELSLGQP--KLRRRSSVLSS--------------------------- 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1024 stflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVR 1103
Cdd:cd14895 591 ------------VGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVR 658
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 312147315 1104 LSFSDFLSRYKPLADTflREKKEQSAAErcrlVLQQCKLQGWQMGVRKVFLK 1155
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 ... |
438-1154 |
2.66e-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: 358.33 E-value: 2.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGK---LCSSLPPHLFSCVERAFHQLFREQRP-- 512
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYEHGERraaGERKLPPHVYAVADKAFRAMLFASRGqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 513 --QCFILSGERGSGKSEASKQIIRHLTC--------RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQ 582
Cdd:cd14901 82 cdQSILVSGESGAGKTETTKIIMNYLASvssatthgQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 583 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGerSLNRE 662
Cdd:cd14901 162 F-ASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDG--VDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 663 KLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAF-VSDLQLLEQVAGMLQVSTDELASALTTDIQYF 741
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFsMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 742 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTN 821
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASRF--IGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 822 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLeSSNT 901
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDA-CVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLL-AKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 902 NAVYSPMKDGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvvinhlfqsklsqtgSLVSA 981
Cdd:cd14901 475 SFSVSKLQQGKRQ---------FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSN---------------AFLSS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 982 YPSFKFRGHKSALLskkmtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrkslmdiiGKLQKCTPHFI 1061
Cdd:cd14901 531 TVVAKFKVQLSSLL-------------------------------------------------------EVLNATEPHFI 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1062 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTfLREKKEQ--SAAERCRLVLQQ 1139
Cdd:cd14901 556 RCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPD-GASDTWKvnELAERLMSQLQH 634
|
730 740
....*....|....*....|
gi 312147315 1140 CKLQG-----WQMGVRKVFL 1154
Cdd:cd14901 635 SELNIehlppFQVGKTKVFL 654
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
438-1113 |
4.48e-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: 351.94 E-value: 4.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRD---KLQPHVYATSTAAYKHMLTNEMNQSIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 596
Cdd:cd14904 79 VSGESGAGKTETTKIVMNHLASVAGGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQF-DGRGKLIGAKCE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 597 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIqddASTGERSLNREKL-AVLKRALNVVG 675
Cdd:cd14904 158 TYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSL---AQMQIPGLDDAKLfASTQKSLSLIG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 676 FSSLEVENLFVILAAILHLGDIRFTALNEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 755
Cdd:cd14904 235 LDNDAQRTLFKILSGVLHLGEVMFDKSDENGSR-ISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 756 EFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLH 835
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQ---IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 836 EQVECVQEGVTMETAYSPGNQnGVLDFFFQKpSGFLTLLDEESQMIWSVESNFPKKLQSLLESsntnavyspmKDGNGNV 915
Cdd:cd14904 391 VEEEYIREGLQWDHIEYQDNQ-GIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQT----------KKDNESI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 916 AL-KDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvSAYPSfkfrghksal 994
Cdd:cd14904 459 DFpKVKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---------SEAPS---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 995 lSKKMTASsiiGENKNylelskllkkkgtstflqrlergDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDT 1074
Cdd:cd14904 520 -ETKEGKS---GKGTK-----------------------APKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTE 572
|
650 660 670
....*....|....*....|....*....|....*....
gi 312147315 1075 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1113
Cdd:cd14904 573 FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY 611
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
434-1158 |
4.24e-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: 334.52 E-value: 4.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 434 LNDGSLLYEIQKRFGNNQIYTFIGD-ILLLVNPYKELPIYS--SM---VSQLYFSSSGKLcSSLPPHLFSCVERAFHQLF 507
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSdaSLgeyGSEYYDTTSGSK-EPLPPHAYDLAARAYLRMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 508 REQRPQCFILSGERGSGKSEASKQIIRHLTCRAGAS-RAT-LDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCE 585
Cdd:cd14879 80 RRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 586 RKQqLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNN-----LCAHRYLNQTI----QDDAstge 656
Cdd:cd14879 160 RGR-LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDpsdyaLLASYGCHPLPlgpgSDDA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 657 rslnrEKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGN--SAFVSDLQLLEQVAGMLQVSTDELASAL 734
Cdd:cd14879 235 -----EGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGeeSAVVKNTDVLDIVAAFLGVSPEDLETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 735 TTDIQYFKGDmiirRHTI----QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQtldIGILDIFGFEEF--- 807
Cdd:cd14879 310 TYKTKLVRKE----LCTVfldpEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATF---ISLLDFPGFQNRsst 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 808 QKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTM-ETAYsPGNQnGVLDFFFQKPSGFLTLLDEESqmiwsveS 886
Cdd:cd14879 383 GGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVpATSY-FDNS-DCVRLLRGKPGGLLGILDDQT-------R 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 887 NFPKKL-QSLLES-SNTNAVYSPMKDGNGNVALKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktsenvvi 964
Cdd:cd14879 454 RMPKKTdEQMLEAlRKRFGNHSSFIAVGNFATRSGSAS-FTVNHYAGEVTYSVEGFLERNGDVLS--------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 965 nhlfqsklsqtGSLVSAypsfkFRGhksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRK 1044
Cdd:cd14879 518 -----------PDFVNL-----LRG-------------------------------------------------ATQLNA 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1045 SLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREK 1124
Cdd:cd14879 533 ALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKST----LRGS 608
|
730 740 750
....*....|....*....|....*....|....*.
gi 312147315 1125 KEQSAAERCRLVLQQCKLQGWqMGVRKVFLKY--WH 1158
Cdd:cd14879 609 AAERIRQCARANGWWEGRDYV-LGNTKVFLSYaaWR 643
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
438-1123 |
2.04e-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: 334.64 E-value: 2.04e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVsqLYFSSSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLI--LNEYKDINQNKSPIPHIYAVALRAYQSMVSEKKNQSII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGASRATL-------DSRFKHVVC---ILEAFGHAKTTLNDLSSCFIKYFELQFCER 586
Cdd:cd14906 80 ISGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnNSIEKDILTsnpILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 587 KQQLTGARIYTYLLEKSRLVSQP-LGQSNFLIFYLLMDGLSAEE--KYGLHlNNLCAHRYLN------QTIQDDASTGER 657
Cdd:cd14906 160 DGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDErsKWGLN-NDPSKYRYLDarddviSSFKSQSSNKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 658 SLNR-----EKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNS-AFVSD--LQLLEQVAGMLQVSTDE 729
Cdd:cd14906 239 NHNNktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKyAYQKDkvTASLESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 730 LASALTTdiQYFK----GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQ-------TLDIGI 798
Cdd:cd14906 319 FKQALLN--RNLKaggrGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAggsnkknNLFIGV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 799 LDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEES 878
Cdd:cd14906 397 LDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKE-CIELIEKKSDGILSLLDDEC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 879 QMiwsvesnfPK-KLQSLLES-----SNTNAVYspmkdgngnVALKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNL 952
Cdd:cd14906 476 IM--------PKgSEQSLLEKynkqyHNTNQYY---------QRTLAKGT-LGIKHFAGDVTYQTDGWLEKNRDSLYSDV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 953 LFVMKTSENVVINHLFQSKLSQTGSlvsaypsfkfrghksalLSKKMTASsiigenknylelskllkkkgtstflqrler 1032
Cdd:cd14906 538 EDLLLASSNFLKKSLFQQQITSTTN-----------------TTKKQTQS------------------------------ 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1033 gdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSR 1112
Cdd:cd14906 571 ---NTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSR 647
|
730
....*....|.
gi 312147315 1113 YKPLADTFLRE 1123
Cdd:cd14906 648 YKCIVDMYNRK 658
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
438-1142 |
2.49e-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: 2.49e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-----FSSSGKLCSSLPPHLFSCVERAFHQLFREQR 511
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtSTSPVSQLSELPPHVFAIGGKAFGGLLKPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 512 P-QCFILSGERGSGKSEASKQIIRHLTC---------RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFEL 581
Cdd:cd14902 82 RnQSILVSGESGSGKTESTKFLMQFLTSvgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 582 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG----------LSAEEKYGLHLNNLCAHRYLNQTIQDD 651
Cdd:cd14902 162 QF-GANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGadktlldllgLQKGGKYELLNSYGPSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 652 AStgerslnREKLAVlkRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAF-VSDLQL--LEQVAGMLQVSTD 728
Cdd:cd14902 241 AQ-------LYVETV--RAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATaVTAASRfhLAKCAELMGVDVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 729 ELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLD-----IGILDIFG 803
Cdd:cd14902 312 KLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSISDEDeelatIGILDIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 804 FEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiws 883
Cdd:cd14902 392 FESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAA-CLALFDDKSNGLFSLLDQECLM--- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 884 vesnfPKKLQsllESSNTNAVYSPMKDGNgnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVV 963
Cdd:cd14902 468 -----PKGSN---QALSTKFYRYHGGLGQ-----------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 964 InhlfqsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKnylelskllkkkgtstflQRLERGDPVTIAS--- 1040
Cdd:cd14902 529 V---------------------------VAIGADENRDSPGADNGA------------------AGRRRYSMLRAPSvsa 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1041 QLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdTF 1120
Cdd:cd14902 564 QFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFK-CF 642
|
730 740
....*....|....*....|..
gi 312147315 1121 LREKKEQSAAERCRLVLQQCKL 1142
Cdd:cd14902 643 LSTRDRAAKMNNHDLAQALVTV 664
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
439-1117 |
2.49e-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: 2.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 439 LLYEIQKRFG--NNQIYTFIGDILLLVNPYKELPiySSMVSqLYFSSSGKLCsslPPHLFSCVERAFHQLfREQRP---- 512
Cdd:cd14891 3 ILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP--EPDKS-DYINTPLDPC---PPHPYAIAEMAYQQM-CLGSGrmqn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 513 QCFILSGERGSGKSEASKQIIRHLTCRA------------------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSC 574
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkrKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 575 FIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiqdDAST 654
Cdd:cd14891 156 FGKFMKLQFTKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQS---GCVS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 655 GERSLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRF----TALNEGNSAFVSDLQLLEQVAGMLQVSTDEL 730
Cdd:cd14891 233 DDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 731 ASALTT-DIQYFKGDMIIRRhTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQ- 808
Cdd:cd14891 313 EKVITQrEIVTRGETFTIKR-NAREAVYSRDAIAKSIYERLFLWIVQQINTSL----GHDPDPLPYIGVLDIFGFESFEt 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 809 KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsvesnf 888
Cdd:cd14891 388 KNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRE-CLDLIASKPNGILPLLDNEARN-------- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 889 PK----KLQSLLESSNTNAVYSPMKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLlfvmktsENVVi 964
Cdd:cd14891 459 PNpsdaKLNETLHKTHKRHPCFPRPHP------KDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDF-------EDLL- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 965 nhlfqsklsqtgslvsaypsfkfrgHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrK 1044
Cdd:cd14891 525 -------------------------ASSAKFSDQM--------------------------------------------Q 535
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312147315 1045 SLMDiigKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1117
Cdd:cd14891 536 ELVD---TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVL 605
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
438-1128 |
2.70e-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: 2.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFS---------SSGKlcsSLPPHLFSCVERAFHQLFR 508
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQegllrsqgiESPQ---ALGPHVFAIADRSYRQMMS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 509 EQRP-QCFILSGERGSGKSEASKQIIRHLTCRAGAS-----------RATLDSRFKHVVCILEAFGHAKTTLNDLSSCFI 576
Cdd:cd14908 79 EIRAsQSILISGESGAGKTESTKIVMLYLTTLGNGEegapnegeelgKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 577 KYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE--KYGLH---LNNLCAHRYLNQTIQDD 651
Cdd:cd14908 159 KFIELGF-NRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEheKYEFHdgiTGGLQLPNEFHYTGQGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 652 ASTGERSLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAF---VSDLQLLEQVAGMLQVSTD 728
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEiaeEGNEKCLARVAKLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 729 ELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLH--SQDEQKSmqtlDIGILDIFGFEE 806
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRS----SVGVLDIFGFEC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 807 FQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQM-IWSVE 885
Cdd:cd14908 394 FAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQD-CLDTIQAKKKGILTMLDDECRLgIRGSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 886 SNFPKKLqsllessntNAVYSPMKDGNGNVALKDHGTA-------FTIMHYAGRVMYDV-VGAIEKNKDSLSqnllfvmK 957
Cdd:cd14908 473 ANYASRL---------YETYLPEKNQTHSENTRFEATSiqktkliFAVRHFAGQVQYTVeTTFCEKNKDEIP-------L 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 958 TSENvvinhLFQSklsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvt 1037
Cdd:cd14908 537 TADS-----LFES------------------------------------------------------------------- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1038 iASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1117
Cdd:cd14908 545 -GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLL 623
|
730
....*....|.
gi 312147315 1118 DTFLREKKEQS 1128
Cdd:cd14908 624 PLIPEVVLSWS 634
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
438-1155 |
1.26e-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: 1.26e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14929 2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY---KGKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASRA-----TLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLTG 592
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESkkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM-LSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 593 ARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG--------LSAEEKYGLHLnnlCAHRYLNQTIQDDAstgerslnrEKL 664
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGkkelrdllLVSANPSDFHF---CSCGAVAVESLDDA---------EEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 665 AVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 744
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 745 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKM 824
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVL---DAKLSRQFF-IGILDITGFEILDYNSLEQLCINFTNEKL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 825 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSVESNFPKKLqslLESSNTNAV 904
Cdd:cd14929 382 QQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKL---FDNHFGKSV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 905 Y--SPMKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqTGSlvsay 982
Cdd:cd14929 458 HfqKPKPDK------KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIS-TDS----- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 983 psfkfrghksallskkmtaSSIIGENKNylelskllkKKGTSTFLqrlergdpvtIASQLRKSLMDIIGKLQKCTPHFIH 1062
Cdd:cd14929 526 -------------------AIQFGEKKR---------KKGASFQT----------VASLHKENLNKLMTNLKSTAPHFVR 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1063 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKL 1142
Cdd:cd14929 568 CINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEELLGSLEI 647
|
730
....*....|....*
gi 312147315 1143 QG--WQMGVRKVFLK 1155
Cdd:cd14929 648 DHtqYRFGITKVFFK 662
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
426-1193 |
3.18e-94 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 325.45 E-value: 3.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 426 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQ 505
Cdd:PTZ00014 99 GDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDS--DKLPPHVFTTARRALEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 506 LFREQRPQCFILSGERGSGKSEASKQIIRHLtcrAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFEL 581
Cdd:PTZ00014 177 LHGVKKSQTIIVSGESGAGKTEATKQIMRYF---ASSKSGNMDLKIQNAIMaanpVLEAFGNAKTIRNNNSSRFGRFMQL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 582 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ------TIqDDASTG 655
Cdd:PTZ00014 254 QL-GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPkcldvpGI-DDVKDF 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 656 ERSLNreklavlkrALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEG---NSAFVSD--LQLLEQVAGMLQVSTDEL 730
Cdd:PTZ00014 332 EEVME---------SFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltDAAAISDesLEVFNEACELLFLDYESL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 731 ASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKN 810
Cdd:PTZ00014 403 KKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVF----IGMLDIFGFEVFKNN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 811 EFEQLCVNMTNEKMH-HYINeVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVESNFP 889
Cdd:PTZ00014 479 SLEQLFINITNEMLQkNFVD-IVFERESKLYKDEGISTEELEYTSNES-VIDLLCGKGKSVLSILEDQCLAPGGTDEKFV 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 890 KKLQSLLESsntNAVYSPMK-DGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLF 968
Cdd:PTZ00014 557 SSCNTNLKN---NPKYKPAKvDSNKN---------FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 969 QSKLSQTGslvsaypsfkfrghksallskKMTASSIIGenknylelskllkkkgtSTFLQRLergdpvtiasqlrKSLMD 1048
Cdd:PTZ00014 625 EGVEVEKG---------------------KLAKGQLIG-----------------SQFLNQL-------------DSLMS 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1049 IIgklQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEQS 1128
Cdd:PTZ00014 654 LI---NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL-DLAVSNDSSLD 729
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147315 1129 AAERCRLVLQQCKL--QGWQMGVRKVFLKYWHADQLNdlclQLQRKIITCQK--------VIRGFLARQHLLQRI 1193
Cdd:PTZ00014 730 PKEKAEKLLERSGLpkDSYAIGKTMVFLKKDAAKELT----QIQREKLAAWEplvsvleaLILKIKKKRKVRKNI 800
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
438-1124 |
7.53e-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: 7.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS--------LPPHLFSCVERAFHQLFR 508
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYLLSFEARSSStrnkgsdpMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 509 ----EQRPQCFILSGERGSGKSEASKQIIRHLTcRAGASRA-----------TLDSRFKHVVCILEAFGHAKTTLNDLSS 573
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLA-QAGDNNLaasvsmgkstsGIAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 574 CFIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEkyglhlnnlcahrylnqtiqddas 653
Cdd:cd14900 161 RFGKFIKLHF-TSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAA------------------------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 654 tgersLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGN--SAFVSDL-----QLLEQVAGMLQVS 726
Cdd:cd14900 216 -----RKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrlGQLKSDLapssiWSRDAAATLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 727 TDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLD-IGILDIFGFE 805
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHfIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 806 EFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSVE 885
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQD-CVNLISQRPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 886 SNFPKKLQSLLEsSNTNAVYSPMKDGNGnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvin 965
Cdd:cd14900 450 TTLASKLYRACG-SHPRFSASRIQRARG---------LFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------ 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 966 HLFQSKLsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiasQLRKS 1045
Cdd:cd14900 508 DLFVYGL--------------------------------------------------------------------QFKEQ 519
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312147315 1046 LMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREK 1124
Cdd:cd14900 520 LTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRLL 598
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
446-1155 |
8.86e-91 |
|
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: 310.38 E-value: 8.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 446 RFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklCSSLPPHLFSCVERAFHQLFREQRPQCFILSGERGSGK 525
Cdd:cd14876 10 RYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPD--LTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 526 SEASKQIIRHLtcrAGASRATLDSRFKHVVC----ILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGArIYTYLLE 601
Cdd:cd14876 88 TEATKQIMRYF---ASAKSGNMDLRIQTAIMaanpVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS-VVAFLLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 602 KSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREklavLKRALNVVGFSSLEV 681
Cdd:cd14876 164 KSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEE----VLESLKSMGLTEEQI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 682 ENLFVILAAILHLGDIRFTALNEG---NSAFVS--DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 756
Cdd:cd14876 240 DTVFSIVSGVLLLGNVKITGKTEQgvdDAAAISneSLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 757 FFRDLLAKSLYSRLFSFLVNTMNSCLHSQDeqkSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINeVLFLH 835
Cdd:cd14876 320 MLKLSLAKAMYDKLFLWIIRNLNSTIEPPG---GFKNF-MGMLDIFGFEVFKNNSLEQLFINITNEMLQkNFID-IVFER 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 836 EQVECVQEGV-TMETAYSPGNQngVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESsntNAVYSPMK-DGNG 913
Cdd:cd14876 395 ESKLYKDEGIpTAELEYTSNAE--VIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKS---NGKFKPAKvDSNI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 914 NvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkfrghksa 993
Cdd:cd14876 470 N---------FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 994 llskKMTASSIIGenknylelskllkkkgtSTFLQRLErgdpvtiasqlrkSLMDIIGKLQkctPHFIHCIRPNNSKLPD 1073
Cdd:cd14876 524 ----KIAKGSLIG-----------------SQFLKQLE-------------SLMGLINSTE---PHFIRCIKPNETKKPL 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1074 TFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEQSAAERCRLVLQQCKL--QGWQMGVRK 1151
Cdd:cd14876 567 EWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL-DLGIANDKSLDPKVAALKLLESSGLseDEYAIGKTM 645
|
....
gi 312147315 1152 VFLK 1155
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 ... |
438-1155 |
6.35e-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: 6.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14909 2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMY---RGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHL--------TCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQ 589
Cdd:cd14909 79 TGESGAGKTENTKKVIAYFatvgaskkTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP-TGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 590 LTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG-LSAEEKYGLHLNNLCAHRYLNQ---TIQ--DDAstgerslnrEK 663
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGsVPGVKEMCLLSDNIYDYYIVSQgkvTVPnvDDG---------EE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 664 LAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 743
Cdd:cd14909 229 FSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 744 DMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQdeQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEK 823
Cdd:cd14909 309 EFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQ--QKRQHF--IGVLDIAGFEIFEYNGFEQLCINFTNEK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 824 MHHYINEVLFLHEQVECVQEGVtmETAYspgnqngvLDF---------FFQKPSGFLTLLDEESQMIWSVESNFPKKLQS 894
Cdd:cd14909 385 LQQFFNHHMFVLEQEEYKREGI--DWAF--------IDFgmdllacidLIEKPMGILSILEEESMFPKATDQTFSEKLTN 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 895 L-LESSNTNAVYSPMKDGNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLS 973
Cdd:cd14909 455 ThLGKSAPFQKPKPPKPGQ-------QAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 974 QTGSLVSAYPSfkfRGHKSALLSkkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKL 1053
Cdd:cd14909 528 QSGGGEQAKGG---RGKKGGGFA----------------------------------------TVSSAYKEQLNSLMTTL 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1054 QKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR-EKKEQSAAER 1132
Cdd:cd14909 565 RSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQgEEDPKKAAEI 644
|
730 740
....*....|....*....|....*
gi 312147315 1133 CrlvLQQCKL--QGWQMGVRKVFLK 1155
Cdd:cd14909 645 I---LESIALdpDQYRLGHTKVFFR 666
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
438-1155 |
1.61e-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: 1.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY---KGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLT--------------CRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQF 583
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 584 CErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQ--TIQDDASTGErsln 660
Cdd:cd14927 159 GP-TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQgvTTVDNMDDGE---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 661 reKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 740
Cdd:cd14927 234 --ELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 741 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMT 820
Cdd:cd14927 312 VGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFF----IGVLDIAGFEIFEFNSFEQLCINFT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 821 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLES 898
Cdd:cd14927 388 NEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACID-LIEKPLGILSILEEECMFPKASDASFKAKLydNHLGKS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 899 SNTNavySPMKDGNgnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTgsl 978
Cdd:cd14927 467 PNFQ---KPRPDKK-----RKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSD--- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 979 vSAYPsfkfrgHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpvTIASQLRK-SLMDIIGKLQKCT 1057
Cdd:cd14927 536 -STED------PKSGVKEKRKKAASF--------------------------------QTVSQLHKeNLNKLMTNLRATQ 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1058 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL------ADTFLREKKeqsAAE 1131
Cdd:cd14927 577 PHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILnpsaipDDKFVDSRK---ATE 653
|
730 740
....*....|....*....|....
gi 312147315 1132 RCRLVLQQCKLQgWQMGVRKVFLK 1155
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 ... |
438-1155 |
4.04e-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: 4.04e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY---KGIKRHEVPPHVFAITDSAYRNMLGDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVC-----------------ILEAFGHAKTTLNDLSSCFIKYFE 580
Cdd:cd14911 79 TGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVNpavligeleqqllqanpILEAFGNAKTVKNDNSSRFGKFIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 581 LQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQ-----DDASTG 655
Cdd:cd14911 159 INF-DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLpvpgvDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 656 ERSLNreklavlkrALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALT 735
Cdd:cd14911 238 QATVK---------SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 736 TDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQL 815
Cdd:cd14911 309 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL---DRTKRQGASFIGILDMAGFEIFELNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 816 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSl 895
Cdd:cd14911 386 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDKLVS- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 896 leSSNTNAVYspMKDGNGNVAlkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqt 975
Cdd:cd14911 464 --AHSMHPKF--MKTDFRGVA------DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD----- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 976 gslvsaypsfkfrghksallskkmtaSSIIGenknylelsKLLKKKGTSTFLQRLERGDPVTIASQLRKSLMDIIGKLQK 1055
Cdd:cd14911 529 --------------------------AEIVG---------MAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRN 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1056 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRL 1135
Cdd:cd14911 574 TNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVI-PKGFMDGKKACEK 652
|
730 740
....*....|....*....|..
gi 312147315 1136 VLQQCKLQG--WQMGVRKVFLK 1155
Cdd:cd14911 653 MIQALELDSnlYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
438-1155 |
6.39e-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: 6.39e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY---RGKKRHEMPPHIYAISESAYRCMLQDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRA--------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQ 589
Cdd:cd14920 79 TGESGAGKTENTKKVIQYLAHVAsshkgrkdHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 590 LTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL-NQTIqddASTGERslNREKLAVLK 668
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsNGYI---PIPGQQ--DKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 669 RALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 748
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 749 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 828
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 829 NEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSVESNFPKKLQSllESSNTNAVYS 906
Cdd:cd14920 390 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHSKFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 907 PMKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTG-SLVSAYPSF 985
Cdd:cd14920 468 PRQ-------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGlDQVTGMTET 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 986 KFrghKSALLSKKmtassiigenknylelskllkkkgtstflqrlerGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIR 1065
Cdd:cd14920 540 AF---GSAYKTKK----------------------------------GMFRTVGQLYKESLTKLMATLRNTNPNFVRCII 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1066 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQQCKLQG- 1144
Cdd:cd14920 583 PNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACERMIRALELDPn 661
|
730
....*....|..
gi 312147315 1145 -WQMGVRKVFLK 1155
Cdd:cd14920 662 lYRIGQSKIFFR 673
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
438-1155 |
7.62e-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: 7.62e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLF-REQRPQCF 515
Cdd:cd14875 2 TLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDP--RLLPPHIWQVAHKAFNAIFvQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 516 ILSGERGSGKSEASKQIIRHL-----------TCRAGASRatLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFC 584
Cdd:cd14875 80 VISGESGSGKTENAKMLIAYLgqlsymhssntSQRSIADK--IDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 585 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGL-HLNNLCAHRYLN--QTIQDDASTGERSLNR 661
Cdd:cd14875 158 PTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNggNTFVRRGVDGKTLDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 662 EKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTAlNEGNSAFVSDLQLLEQVAGMLQVSTDELASALttdiqyf 741
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES-DQNDKAQIADETPFLTACRLLQLDPAKLRECF------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 742 kgdmIIRRHT--IQI------AEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTldIGILDIFGFEEFQKNEFE 813
Cdd:cd14875 310 ----LVKSKTslVTIlankteAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGCKY--IGLLDIFGFENFTRNSFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 814 QLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQMIWSVESNFPKKLQ 893
Cdd:cd14875 384 QLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECV-NMFDQKRTGIFSMLDEECNFKGGTTERFTTNLW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 894 SllESSNTNAVYSPMKDGNGNvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqskls 973
Cdd:cd14875 463 D--QWANKSPYFVLPKSTIPN--------QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIR-------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 974 qtgSLVSAYPSFKFRGHksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKL 1053
Cdd:cd14875 525 ---TLLSTEKGLARRKQ----------------------------------------------TVAIRFQRQLTDLRTEL 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1054 QKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFlSRY------KPLADTFLREKKEQ 1127
Cdd:cd14875 556 ESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF-CRYfylimpRSTASLFKQEKYSE 634
|
730 740 750
....*....|....*....|....*....|...
gi 312147315 1128 SAaerCRLVLQQCKLQGWQ-----MGVRKVFLK 1155
Cdd:cd14875 635 AA---KDFLAYYQRLYGWAkpnyaVGKTKVFLR 664
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
437-1155 |
1.29e-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: 298.85 E-value: 1.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGASRATLDS--------RFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 588
Cdd:cd14921 78 CTGESGAGKTENTKKVIQYLAVVASSHKGKKDTsitgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 589 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLavlk 668
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETL---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 669 RALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 748
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 749 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 828
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 829 NEVLFLHEQVECVQEGV-------------TMETAYSPGNqngvldfffqkPSGFLTLLDEESQMIWSVESNFPKKLQSl 895
Cdd:cd14921 390 NHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKSFVEKLCT- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 896 lESSNTNAVYSPMKdgngnvaLKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 975
Cdd:cd14921 458 -EQGNHPKFQKPKQ-------LKDK-TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 976 GSLVSAypsfkfrghksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQK 1055
Cdd:cd14921 529 GLDQMA----------------KMTESSLPSASKT--------------------KKGMFRTVGQLYKEQLGKLMTTLRN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1056 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRL 1135
Cdd:cd14921 573 TTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACIL 651
|
730 740
....*....|....*....|..
gi 312147315 1136 VLQQCKLQG--WQMGVRKVFLK 1155
Cdd:cd14921 652 MIKALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
437-1155 |
4.84e-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: 4.84e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMY---KGKKRTEMPPHLFSISDNAYHDMLMDRENQSML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGASR------ATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQL 590
Cdd:cd14934 78 ITGESGAGKTENTKKVIQYFANIGGTGKqssdgkGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT-TGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 591 TGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQ--TIQDDASTGErslnreKLAVL 667
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQgvTVVDNMDDGE------ELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 668 KRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 747
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 748 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 827
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTL----DTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 828 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtnavY 905
Cdd:cd14934 387 FNHHMFVLEQEEYKREGIEWVFIDFGLDLQACID-LLEKPMGIFSILEEQCVFPKATDATFKAALydNHLGKSSN----F 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 906 SPMKDGNGnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvsaypsf 985
Cdd:cd14934 462 LKPKGGKG----KGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGS-------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 986 kfrghksallSKKMTASSIIgenknylelskllkkkgtstflqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIR 1065
Cdd:cd14934 530 ----------KKQKRGSSFM-------------------------------TVSNFYREQLNKLMTTLHSTAPHFVRCIV 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1066 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-----ADTFLREKKeqsAAErcrLVLQQC 1140
Cdd:cd14934 569 PNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLnpnviPQGFVDNKK---ASE---LLLGSI 642
|
730
....*....|....*..
gi 312147315 1141 KLQ--GWQMGVRKVFLK 1155
Cdd:cd14934 643 DLDvnEYKIGHTKVFFR 659
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
437-1155 |
1.56e-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: 1.56e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGA------------SRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFc 584
Cdd:cd14932 78 CTGESGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 585 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLnqtiqddaSTGERSL----N 660
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFL--------SNGNVTIpgqqD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 661 REKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 740
Cdd:cd14932 229 KELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 741 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 820
Cdd:cd14932 309 VGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 821 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSVESNFPKKLQSllES 898
Cdd:cd14932 386 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQ--EQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 899 SNTNAVYSPMKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgsl 978
Cdd:cd14932 464 GNNPKFQKPKK-------LKDDAD-FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD-------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 979 vsaypsfkfrghksallskkmtASSIIGENKNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLMDIIGKLQKCTP 1058
Cdd:cd14932 528 ----------------------VDRIVGLDKVAGMGESLHGAFKTRKGMFR-------TVGQLYKEQLMNLMTTLRNTNP 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1059 HFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQ 1138
Cdd:cd14932 579 NFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMVK 657
|
730
....*....|....*....
gi 312147315 1139 QCKLQG--WQMGVRKVFLK 1155
Cdd:cd14932 658 ALELDPnlYRIGQSKVFFR 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
438-1155 |
1.91e-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: 1.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGAS----------RATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERK 587
Cdd:cd14913 79 TGESGAGKTVNTKRVIQYFATIAATGdlakkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 588 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQtiqddastGERSL----NRE 662
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELiELLLITTNPYDYPFISQ--------GEILVasidDAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 663 KLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 742
Cdd:cd14913 230 ELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 743 GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNE 822
Cdd:cd14913 310 NEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF----IGVLDIAGFEIFEYNSLEQLCINFTNE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 823 KMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSN 900
Cdd:cd14913 386 KLQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 901 tnavYSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvs 980
Cdd:cd14913 465 ----FQKPKVVKGRAE-----AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 981 aypsfkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHF 1060
Cdd:cd14913 526 ------FATADADSGKKKVAKKK-------------------GSSFQ---------TVSALFRENLNKLMSNLRTTHPHF 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1061 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQC 1140
Cdd:cd14913 572 VRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASI 651
|
730
....*....|....*..
gi 312147315 1141 KLQ--GWQMGVRKVFLK 1155
Cdd:cd14913 652 DIDhtQYKFGHTKVFFK 668
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
438-1155 |
5.04e-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: 290.10 E-value: 5.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklcSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSR---SDNAPHIFSVADSAYQDMLHHEEPQHIIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLtCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 597
Cdd:cd14882 79 SGESYSGKTTNARLLIKHL-CYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTF-GSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 598 YLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEK---YGLHLNNlcAHRYLnQTIQDDASTGERSL------NREKLAVLK 668
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlkeYNLKAGR--NYRYL-RIPPEVPPSKLKYRrddpegNVERYKEFE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 669 RALNVVGFSSLEVENLFVILAAILHLGDIRFTalnEGN-SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 747
Cdd:cd14882 234 EILKDLDFNEEQLETVRKVLAAILNLGEIRFR---QNGgYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 748 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 827
Cdd:cd14882 311 RKHTTEEARDARDVLASTLYSRLVDWIINRINMKM-SFPRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 828 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQmiwsvesnfpkklqsllESSNTNAVYSP 907
Cdd:cd14882 390 YNQRIFISEMLEMEEEDIPTINLRFYDNKTAV-DQLMTKPDGLFYIIDDASR-----------------SCQDQNYIMDR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 908 MKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLVSAYPSFKF 987
Cdd:cd14882 452 IKEKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--SQVRNMRTLAATFRA 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 988 rghkSALLSKKMTAssiIGENknylelskllkKKGTstflqrlergdpvtiasqlrkslmdiigklqkctpHFIHCIRPN 1067
Cdd:cd14882 530 ----TSLELLKMLS---IGAN-----------SGGT-----------------------------------HFVRCIRSD 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1068 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlrEKKEQSAAERCRLVLQQCKLQGWQM 1147
Cdd:cd14882 557 LEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDF--DETVEMTKDNCRLLLIRLKMEGWAI 634
|
....*...
gi 312147315 1148 GVRKVFLK 1155
Cdd:cd14882 635 GKTKVFLK 642
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
443-1154 |
1.19e-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: 1.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 443 IQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFREQRPQCFILSGERG 522
Cdd:cd14881 7 LQARFYAKEFFTNVGPILLSVNPYRDVG------NPLTLTSTRS--SPLAPQLLKVVQEAVRQQSETGYPQAIILSGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 523 SGKSEASKQIIRHLTCRAGASRATldSRFKHV---VCILEAFGHAKTTLNDLSSCFIKYFELQFCErkQQLTGARIYTYL 599
Cdd:cd14881 79 SGKTYASMLLLRQLFDVAGGGPET--DAFKHLaaaFTVLRSLGSAKTATNSESSRIGHFIEVQVTD--GALYRTKIHCYF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 600 LEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAH--RYLNQ--TIQDDASTGERslnrekLAVLKRALNVVG 675
Cdd:cd14881 155 LDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPAnlRYLSHgdTRQNEAEDAAR------FQAWKACLGILG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 676 FSSLEVENlfvILAAILHLGDIRFTALNEGNSAFVSDLQLlEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 755
Cdd:cd14881 229 IPFLDVVR---VLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 756 EFFRDLLAKSLYSRLFSFLVNTMNSC--LHSQdeqKSMQTLD--IGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 831
Cdd:cd14881 305 NMTRDALAKALYCRTVATIVRRANSLkrLGST---LGTHATDgfIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTH 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 832 LFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESnFPKKLQslLESSNTNAVYSPmkdg 911
Cdd:cd14881 382 IFKSSIESCRDEGIQCEVEVDYVDNVPCIDLISSLRTGLLSMLDVECSPRGTAES-YVAKIK--VQHRQNPRLFEA---- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 912 ngnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtsenvvinhlfqsklSQTGslvsaypSFKFRGHk 991
Cdd:cd14881 455 -----KPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY---------------KQNC-------NFGFATH- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 992 sallskkmtassiigenknylelskllkkkgTSTFLQRLErgdpvtiasQLRKSLMdiigklqKCTPHFIHCIRPNNSKL 1071
Cdd:cd14881 507 -------------------------------TQDFHTRLD---------NLLRTLV-------HARPHFVRCIRSNTTET 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1072 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKLQ-------- 1143
Cdd:cd14881 540 PNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILQFLEAQppsklssv 619
|
730
....*....|...
gi 312147315 1144 --GWQMGVRKVFL 1154
Cdd:cd14881 620 stSWALGKRHIFL 632
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
437-1155 |
6.42e-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: 285.06 E-value: 6.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGASRAT-----LDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLT 591
Cdd:cd14919 78 CTGESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 592 GARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLavlkRAL 671
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETM----EAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 672 NVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 751
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 752 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 831
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 832 LFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSVESNFPKKlqsLLESSNTNAVYSPMK 909
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEK---VVQEQGTHPKFQKPK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 910 DgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfrg 989
Cdd:cd14919 467 Q------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVA-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 990 hksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNS 1069
Cdd:cd14919 532 --------GMSETALPGAFKT--------------------RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHE 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1070 KLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQQCKLQG--WQM 1147
Cdd:cd14919 584 KKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRI 662
|
....*...
gi 312147315 1148 GVRKVFLK 1155
Cdd:cd14919 663 GQSKVFFR 670
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
437-1114 |
2.35e-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: 2.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-------FSSSGKLCSSLPPHLFSCVERAFHQLFR 508
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqFGDRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 509 EQRPQCFILSGERGSGKSEASKQIIRHLTCRAG-----------------ASRATLDSRFKHVVCILEAFGHAKTTLNDL 571
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppasPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 572 SSCFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDG----LSAEEKYGLHLN-NLCAHRYLNQ 646
Cdd:cd14899 161 SSRFGKFIELRFRDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSgGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 647 TIQDDASTGERslNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEG--NSAFVSDLQLLEQVAG--- 721
Cdd:cd14899 241 SLCSKRRDGVK--DGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKgdDTVFADEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 722 -------MLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQ--------- 785
Cdd:cd14899 319 hftkaaeLLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 786 ----DEQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQnGVLD 861
Cdd:cd14899 399 sdvdDEEDATDF--IGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNR-ACLE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 862 FFFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTNAVYSpmkdgngNVALKDHGTAFTIMHYAGRVMYDVVGAI 941
Cdd:cd14899 476 LFEHRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFR-------SAPLIQRTTQFVVAHYAGCVTYTIDGFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 942 EKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKSAllsKKMTASsiigenknylelskllkkk 1021
Cdd:cd14899 549 AKNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRA---KSAIAA------------------- 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1022 gtstflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYP 1101
Cdd:cd14899 607 --------------VSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFP 672
|
730
....*....|...
gi 312147315 1102 VRLSFSDFLSRYK 1114
Cdd:cd14899 673 VRLTHKQFLGRYR 685
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
437-1155 |
2.80e-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: 283.11 E-value: 2.80e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGA------------SRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFc 584
Cdd:cd15896 78 CTGESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 585 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKL 664
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 665 avlkRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 744
Cdd:cd15896 237 ----EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 745 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 824
Cdd:cd15896 313 YVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 825 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSVESNFPKKLqsLLESSNTN 902
Cdd:cd15896 390 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKV--LQEQGTHP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 903 AVYSPMKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsay 982
Cdd:cd15896 468 KFFKPKK-------LKDEAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVG------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 983 psfkfrghksalLSKKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLMDIIGKLQKCTPHFIH 1062
Cdd:cd15896 534 ------------LDKVSGMSEMPGAFKT--------------------RKGMFRTVGQLYKEQLSKLMATLRNTNPNFVR 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1063 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQQCKL 1142
Cdd:cd15896 582 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMIKSLEL 660
|
730
....*....|....*
gi 312147315 1143 QG--WQMGVRKVFLK 1155
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 ... |
438-1155 |
3.14e-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: 282.76 E-value: 3.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAG----------ASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCErK 587
Cdd:cd14917 79 TGESGAGKTVNTKRVIQYFAVIAAigdrskkdqtPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA-T 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 588 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTIQDDASTGERslnrEKLAV 666
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDA----EELMA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 667 LKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 746
Cdd:cd14917 234 TDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 747 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 826
Cdd:cd14917 314 TKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 827 YINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNTNav 904
Cdd:cd14917 390 FFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLfdNHLGKSNNFQ-- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 905 yspmKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvsayps 984
Cdd:cd14917 467 ----KPRNIKGKPEAH---FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN-------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 985 fkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHCI 1064
Cdd:cd14917 526 --YAGADAPIEKGKGKAKK-------------------GSSFQ---------TVSALHRENLNKLMTNLRSTHPHFVRCI 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1065 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKL-- 1142
Cdd:cd14917 576 IPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIdh 655
|
730
....*....|...
gi 312147315 1143 QGWQMGVRKVFLK 1155
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 ... |
437-1155 |
3.78e-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: 279.67 E-value: 3.78e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 437 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY---RGKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGASRA--------TLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 588
Cdd:cd14930 78 CTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 589 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLnqTIQDDASTG-ERSLNREKLavl 667
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGqERELFQETL--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 668 kRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 747
Cdd:cd14930 232 -ESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 748 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 827
Cdd:cd14930 311 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASF---LGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 828 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSVESNFPKKLQSllESSNTNAVY 905
Cdd:cd14930 388 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQ--EQGGHPKFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 906 SPMKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS-----KLSQTGSLVS 980
Cdd:cd14930 466 RPRH-------LRDQAD-FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGD 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 981 AYPSFKFRghksallskkmtassiigenknylelskllkkkgtstflqrleRGDPVTIASQLRKSLMDIIGKLQKCTPHF 1060
Cdd:cd14930 538 GPPGGRPR-------------------------------------------RGMFRTVGQLYKESLSRLMATLSNTNPSF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1061 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEQSAAERCRLVLQQC 1140
Cdd:cd14930 575 VRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQAL 653
|
730
....*....|....*..
gi 312147315 1141 KLQG--WQMGVRKVFLK 1155
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 ... |
438-1155 |
3.49e-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: 277.00 E-value: 3.49e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRA------------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcE 585
Cdd:cd14910 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeatsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 586 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMdglSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLA 665
Cdd:cd14910 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIM---SNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 666 VLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 745
Cdd:cd14910 235 ATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 746 IIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 825
Cdd:cd14910 315 VTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 826 HYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtna 903
Cdd:cd14910 391 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSNN--- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 904 vYSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYP 983
Cdd:cd14910 467 -FQKPKPAKGKVE-----AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 984 SFKFRGhksallskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHC 1063
Cdd:cd14910 541 GGKKKG----------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPHFVRC 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1064 IRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRLVLQQC 1140
Cdd:cd14910 578 IIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQfidSKKASEKLLGSIDID 657
|
730
....*....|....*
gi 312147315 1141 KLQgWQMGVRKVFLK 1155
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 ... |
438-1155 |
1.17e-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: 275.40 E-value: 1.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTC-----------RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 586
Cdd:cd14916 79 TGESGAGKTVNTKRVIQYFASiaaigdrskkeNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 587 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQTIQDDASTGERslnrEKLA 665
Cdd:cd14916 158 TGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELlDMLLVTNNPYDYAFVSQGEVSVASIDDS----EELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 666 VLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 745
Cdd:cd14916 234 ATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 746 IIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 825
Cdd:cd14916 314 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 826 HYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNTNa 903
Cdd:cd14916 390 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLydNHLGKSNNFQ- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 904 vyspmKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqtgslVSAYP 983
Cdd:cd14916 468 -----KPRNVKGKQEAH---FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS-----ADTGD 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 984 SFKFRGHKSAllskkmtassiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIHC 1063
Cdd:cd14916 535 SGKGKGGKKK-----------------------------GSSFQ---------TVSALHRENLNKLMTNLKTTHPHFVRC 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1064 IRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEQSAAERCRLVLQQCKL- 1142
Cdd:cd14916 577 IIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDId 656
|
730
....*....|....
gi 312147315 1143 -QGWQMGVRKVFLK 1155
Cdd:cd14916 657 hNQYKFGHTKVFFK 670
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
438-1155 |
4.71e-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: 273.53 E-value: 4.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRA------------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCE 585
Cdd:cd14915 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 586 rKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQtiqddastGERSL----N 660
Cdd:cd14915 159 -TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELiEMLLITTNPYDFAFVSQ--------GEITVpsidD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 661 REKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 740
Cdd:cd14915 230 QEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 741 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMT 820
Cdd:cd14915 310 VGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 821 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLES 898
Cdd:cd14915 386 NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 899 SNtnavYSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvinHLFQSKLSQTgsl 978
Cdd:cd14915 465 NN----FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVV------------GLYQKSGMKT--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 979 vsayPSFKFRGHKSAllSKKMTASSIIGENKNylelskllkkkgtSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTP 1058
Cdd:cd14915 521 ----LAFLFSGGQTA--EAEGGGGKKGGKKKG-------------SSFQ---------TVSALFRENLNKLMTNLRSTHP 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1059 HFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRL 1135
Cdd:cd14915 573 HFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQfidSKKASEKLLG 652
|
730 740
....*....|....*....|
gi 312147315 1136 VLQQCKLQgWQMGVRKVFLK 1155
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 ... |
438-1155 |
5.01e-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: 273.53 E-value: 5.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRA------------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcE 585
Cdd:cd14912 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeitsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 586 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQTIQDDASTGERslnrEKL 664
Cdd:cd14912 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELiEMLLITTNPYDYPFVSQGEISVASIDDQ----EEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 665 AVLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 744
Cdd:cd14912 234 MATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 745 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKM 824
Cdd:cd14912 314 YVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 825 HHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtn 902
Cdd:cd14912 390 QQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSAN-- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 903 avYSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLVSAY 982
Cdd:cd14912 467 --FQKPKVVKGKAE-----AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSG--AQTAEGASAG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 983 PSFKFRGHKSAllskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLMDIIGKLQKCTPHFIH 1062
Cdd:cd14912 538 GGAKKGGKKKG------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPHFVR 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1063 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRLVLQQ 1139
Cdd:cd14912 579 CIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQfidSKKASEKLLASIDI 658
|
730
....*....|....*.
gi 312147315 1140 CKLQgWQMGVRKVFLK 1155
Cdd:cd14912 659 DHTQ-YKFGHTKVFFK 673
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
439-1155 |
5.86e-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: 270.45 E-value: 5.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 439 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILS 518
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 519 GERGSGKSEASKQIIRHLTC----------RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 588
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATiavtgekkkeESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 589 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMdglSAEEKYGLHLNNLCAHRYLNQTIQDDASTGERSLNREKLAVLK 668
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIT---SNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 669 RALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 748
Cdd:cd14918 236 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 749 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 828
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 829 NEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtnavYS 906
Cdd:cd14918 392 NHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLydQHLGKSAN----FQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 907 PMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktseNVVINHLFQSKLSQTGSLVSAYPSFK 986
Cdd:cd14918 467 KPKVVKGKAE-----AHFSLIHYAGTVDYNITGWLDKNKDPLN-----------DTVVGLYQKSAMKTLASLFSTYASAE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 987 frGHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRP 1066
Cdd:cd14918 531 --ADSGAKKGAKKKGSSF-------------------------------QTVSALFRENLNKLMTNLRSTHPHFVRCIIP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1067 NNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRLVLQQCKLQ 1143
Cdd:cd14918 578 NETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQfidSKKASEKLLASIDIDHTQ 657
|
730
....*....|..
gi 312147315 1144 gWQMGVRKVFLK 1155
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 ... |
443-1155 |
3.36e-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: 3.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 443 IQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLC--SSLPPHLFSCVERAFHQLFREQRPQCFILSG 519
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSRGfpSDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 520 ERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIYTYL 599
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL-LVGPDGGLKGGKITSYM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 600 LEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTIQDDASTGErslNREKLAVLKRALNVVgFSSL 679
Cdd:cd14886 166 LELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGID---DQKEFAPVRSQLEKL-FSKN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 680 EVENLFVILAAILHLGDIRF---TALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 756
Cdd:cd14886 242 EIDSFYKCISGILLAGNIEFseeGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 757 FFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVlFLH 835
Cdd:cd14886 322 VNIRAVAKDLYGALFELCVDTLNEIIQFDADARPW----IGILDIYGFEFFERNTYEQLLINYANERLQqYFINQV-FKS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 836 EQVECVQEGVTMETAYSPGNQNGVLdfFFQKPS-GFLTLLDEESQmiwsVESNFPKKLQSLLESSNTNAVYSPMKDGNGN 914
Cdd:cd14886 397 EIQEYEIEGIDHSMITFTDNSNVLA--VFDKPNlSIFSFLEEQCL----IQTGSSEKFTSSCKSKIKNNSFIPGKGSQCN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 915 valkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgslvsaypsfkfrghksal 994
Cdd:cd14886 471 ---------FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN----------------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 995 lskkMTASSIIGENKNYLelskllkkkgtSTFLqrlergdpvtiASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDT 1074
Cdd:cd14886 513 ----KAFSDIPNEDGNMK-----------GKFL-----------GSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1075 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL---ADTFLREKKEQSAAERCRLVLQQCKLQGWQMGVRK 1151
Cdd:cd14886 567 YETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTK 646
|
....
gi 312147315 1152 VFLK 1155
Cdd:cd14886 647 VFLR 650
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
438-1155 |
3.41e-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: 265.39 E-value: 3.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRA-----------GASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 586
Cdd:cd14923 79 TGESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 587 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEkygLHLNNLCAHRYLNQTIQDDASTGERSLNREKLAV 666
Cdd:cd14923 158 TGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL---IDLLLISTNPFDFPFVSQGEVTVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 667 LKRALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 746
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 747 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 826
Cdd:cd14923 315 TKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF----IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 827 YINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSVESNFPKKL--QSLLESSNtnav 904
Cdd:cd14923 391 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN---- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 905 YSPMKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvSAYps 984
Cdd:cd14923 466 FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-----------SNY-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 985 fkfrghksallskkmtASSIIGENknylelskllkkkGTSTFLQRLERGDPVTIASQLRKSLMDIIGKLQKCTPHFIHCI 1064
Cdd:cd14923 528 ----------------AGAEAGDS-------------GGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCL 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1065 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKK---EQSAAERCRLVLQQCK 1141
Cdd:cd14923 579 IPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQfidSKNASEKLLNSIDVDR 658
|
730
....*....|....
gi 312147315 1142 LQgWQMGVRKVFLK 1155
Cdd:cd14923 659 EQ-YRFGHTKVFFK 671
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
438-1117 |
1.15e-74 |
|
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: 263.25 E-value: 1.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFREQRP--QC 514
Cdd:cd14880 2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQP--QKLKPHIFTVGEQTYRNVKSLIEPvnQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 515 FILSGERGSGKSEASKQIIRHLTCRAgASRAT---------LDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcE 585
Cdd:cd14880 80 IVVSGESGAGKTWTSRCLMKFYAVVA-ASPTSweshkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL-N 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 586 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTiqddastgERSLNREKLA 665
Cdd:cd14880 158 RAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP--------ERNLEEDCFE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 666 VLKRALNVVGFSSLEVENLFVILAAILHLGDIRFTalNEGNSAFVSDLQLLEQV-----AGMLQVSTDELASALTT-DIQ 739
Cdd:cd14880 230 VTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFA--DSEDEAQPCQPMDDTKEsvrtsALLLKLPEDHLLETLQIrTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 740 YFKGDMIIRRHTIQI-AEFFRDLLAKSLYSRLFSFLVNTMNSCLHSqdEQKSMQTLdIGILDIFGFEEFQKNEFEQLCVN 818
Cdd:cd14880 308 AGKQQQVFKKPCSRAeCDTRRDCLAKLIYARLFDWLVSVINSSICA--DTDSWTTF-IGLLDVYGFESFPENSLEQLCIN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 819 MTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsVESNFPKKLQSLLE 897
Cdd:cd14880 385 YANEKLqQHFVAHYL-RAQQEEYAVEGLEWSFINYQDNQT-CLDLIEGSPISICSLINEECRL---NRPSSAAQLQTRIE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 898 SsntnAVYSPMKDGNGNVALKdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsqtgs 977
Cdd:cd14880 460 S----ALAGNPCLGHNKLSRE---PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 978 lvsaypsfkfrghksallSKKMTASSIIGENknylelskllkkkgtstflqrleRGDPVTIASQLRKSLMDIIGKLQKCT 1057
Cdd:cd14880 527 ------------------PEEKTQEEPSGQS-----------------------RAPVLTVVSKFKASLEQLLQVLHSTT 565
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1058 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1117
Cdd:cd14880 566 PHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLR 625
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
450-1155 |
1.65e-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: 1.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 450 NQIYTFIGDILLLVNPYKELPIYS-SMVSQLYFSSSgklcSSLPPHLFSCVERAFHQLFREQRPQCFILSGERGSGKSEA 528
Cdd:cd14887 22 NCIYTYTGTLLIAVNPYRFFNLYDrQWISRFDTEAN----SRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTET 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 529 SKQIIRHLTC----RAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKqQLTGARIYTYLLEKSR 604
Cdd:cd14887 98 SKHVLTYLAAvsdrRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG-KLTRASVATYLLANER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 605 LVSQPLGQSNFLIFYllmdglsaeekyglhlnNLCAHRYLNQTiqDDASTGERSLNREKLAVLKRALNVVGFSSLEVENL 684
Cdd:cd14887 177 VVRIPSDEFSFHIFY-----------------ALCNAAVAAAT--QKSSAGEGDPESTDLRRITAAMKTVGIGGGEQADI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 685 FVILAAILHLGDIRFTALNE--------------GNSAFVSDL-QLLE--------QVAGMLQVSTDELASALTTDIQYF 741
Cdd:cd14887 238 FKLLAAILHLGNVEFTTDQEpetskkrkltsvsvGCEETAADRsHSSEvkclssglKVTEASRKHLKTVARLLGLPPGVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 742 KGDMI-----IRR-------HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLH----------SQDEQKSMQTLDIGIL 799
Cdd:cd14887 318 GEEMLrlalvSRSvretrsfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQrsakpsesdsDEDTPSTTGTQTIGIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 800 DIFGFEEFQ---KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVL-DFFFQKPSGFLTLLD 875
Cdd:cd14887 398 DLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSFPLaSTLTSSPSSTSPFSP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 876 EESQMIWSVESNFPKKLQSLLESSNTNAVYSPMKDGNGNV----------------------ALKDHGTAFTIMHYAGRV 933
Cdd:cd14887 478 TPSFRSSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSdlfyeklnkniinsakyknitpALSRENLEFTVSHFACDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 934 MYDVVGAIEKNKDSLSQNLlfvmktsenvvinhlfqsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKNyle 1013
Cdd:cd14887 558 TYDARDFCRANREATSDEL---------------------------------------ERLFLACSTYTRLVGSKKN--- 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1014 lskllkkKGTSTFLQRLErgdpvTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMV 1093
Cdd:cd14887 596 -------SGVRAISSRRS-----TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLL 663
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312147315 1094 KIFRYGYPVRLSFSDFLSRYkplaDTFLREKKEQSAAER--CRLVLQQCKLQ--GWQMGVRKVFLK 1155
Cdd:cd14887 664 RVMADGFPCRLPYVELWRRY----ETKLPMALREALTPKmfCKIVLMFLEINsnSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
438-1119 |
3.15e-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: 247.89 E-value: 3.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsslpPHLFSCVERAFHQLFREQRpQCFIL 517
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE------PHVYDVAEASVQDLLVHGN-QTIVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAgASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcerKQQLTGARIYT 597
Cdd:cd14898 75 SGESGSGKTENAKLVIKYLVERT-ASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF---DGKITGAKFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 598 YLLEKSRLVSQPLGQSNFLIFYLLmdglsaeekyglhlnnlCAHRYLNqtIQDD-------ASTGERSLN-REKLAVLKR 669
Cdd:cd14898 151 YLLEKSRVTHHEKGERNFHIFYQF-----------------CASKRLN--IKNDfidtsstAGNKESIVQlSEKYKMTCS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 670 ALNVVGFSSL-EVENLfviLAAILHLGDIRFTalNEGNSAFVSDlQLLEQVAGMLQVSTDELASALTT-DIQYfKGDMII 747
Cdd:cd14898 212 AMKSLGIANFkSIEDC---LLGILYLGSIQFV--NDGILKLQRN-ESFTEFCKLHNIQEEDFEESLVKfSIQV-KGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 748 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEqksmqtLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 827
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGE------RSISVLDIFGFEIFESNGLDQLCINWTNEKIQND 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 828 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDffFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLessntnavysp 907
Cdd:cd14898 359 FIKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRD--FEKPCGLMDLISEESFNAWGNVKNLLVKIKKYL----------- 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 908 mkdgNGNVALKdHGTAFTIMHYAGRVMYDVVGAIEKNKDSlsqnllfvmktsenvvinhlfqsklsqtGSLvsaypsfkf 987
Cdd:cd14898 426 ----NGFINTK-ARDKIKVSHYAGDVEYDLRDFLDKNREK----------------------------GQL--------- 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 988 RGHKSALLSKKMTASSIIGENKNylelskllkkkgtstflqrlergdpvtiasqlrkSLMDIIGKLQKCTPHFIHCIRPN 1067
Cdd:cd14898 464 LIFKNLLINDEGSKEDLVKYFKD----------------------------------SMNKLLNSINETQAKYIKCIRPN 509
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 312147315 1068 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT 1119
Cdd:cd14898 510 EECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
439-1155 |
3.20e-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: 3.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 439 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgklcsslppHLFSCVERAFHQLFR-EQRPQCFIL 517
Cdd:cd14874 3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC-------------HISGVAENALDRIKSmSSNAESIVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGASRATLDSrfKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARI-Y 596
Cdd:cd14874 70 GGESGSGKSYNAFQVFKYLTSQPKSKVTTKHS--SAIESVFKSFGCAKTLKNDEATRFGCSIDLLY--KRNVLTGLNLkY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 597 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQtiqdDASTGERSLNREKLAVLKRALNVVGF 676
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQ----GNSTENIQSDVNHFKHLEDALHVLGF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 677 SSLEVENLFVILAAILHLGDIRFTAL----NEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQyfKGDMIirrhTI 752
Cdd:cd14874 222 SDDHCISIYKIISTILHIGNIYFRTKrnpnVEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSE--DGTTI----DL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 753 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 832
Cdd:cd14874 296 NAALDNRDSFAMLIYEELFKWVLNRIGLHL-----KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 833 FLHEQVECVQEGVTMETAYSPGNQNG-VLDFFFQKPSGFLTLLDEESQmiwsvesnFPK-KLQSLLESSNTNAVyspMKD 910
Cdd:cd14874 371 FHDQLVDYAKDGISVDYKVPNSIENGkTVELLFKKPYGLLPLLTDECK--------FPKgSHESYLEHCNLNHT---DRS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 911 GNGNVALKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVsaypsfkfrgh 990
Cdd:cd14874 440 SYGKARNKER-LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMI----------- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 991 ksallskkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSK 1070
Cdd:cd14874 508 ---------------------------------------------VSQAQFILRGAQEIADKINGSHAHFVRCIKSNNER 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1071 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL--ADTflreKKEQSAAERCRLVLQQcklQG---- 1144
Cdd:cd14874 543 QPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLlpGDI----AMCQNEKEIIQDILQG---QGvkye 615
|
730
....*....|...
gi 312147315 1145 --WQMGVRKVFLK 1155
Cdd:cd14874 616 ndFKIGTEYVFLR 628
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
438-1113 |
1.23e-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: 1.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcssLPPHLFSCVERAFHQLFREQRPQCFI 516
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRG-----LPPHLFALAAKAISDMQDFRRDQLIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 517 LSGERGSGKSEASKQIIRHLTCRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIY 596
Cdd:cd14905 77 IGGESGSGKSENTKIIIQYLLTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEM-FYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 597 TYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQ--TIQDDASTGERSLNReklavLKRALNVV 674
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQggSISVESIDDNRVFDR-----LKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 675 GFSSLEVENLFVILAAILHLGDIRFtaLNEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDiqyfkgdmiiRRHTIQI 754
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTF--FQKNGKTEVKDRTLIESLSHNITFDSTKLENILISD----------RSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 755 AEFFRDLLAKSLYSRLFSFLVNTMNSCLhsqdeQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 834
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKL-----KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 835 HEQVECVQEGVTMETAYS-PGNQNGVldfffQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLESSNTNAvYSPMKdgng 913
Cdd:cd14905 374 QEQREYQTERIPWMTPISfKDNEESV-----EMMEKIINLLDQESKNINSSDQIFLEKLQNFLSRHHLFG-KKPNK---- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 914 nvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtseNVVINHLFQS----KLSQTGSLVSAYPSFKFRG 989
Cdd:cd14905 444 ----------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHK---NSITKYLFSRdgvfNINATVAELNQMFDAKNTA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 990 HKSALLSKK--MTASSIIGENKNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLMDiigklQKCTPHFIHCIRPN 1067
Cdd:cd14905 511 KKSPLSIVKvlLSCGSNNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINN-----SNCDFHFIRCIKPN 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 312147315 1068 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1113
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 ... |
438-1114 |
9.99e-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: 9.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS----LPPHLFSCVERAFHQLFREQRP 512
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAASaapfPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 513 QCFILSGERGSGKSEASKQIIRHLT-CRAGASRATLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQ-- 589
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHyIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENTqk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 590 ------LTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL--------NQTIQDDASTG 655
Cdd:cd14884 162 nmfngcFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLlnpdeshqKRSVKGTLRLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 656 ERSLNREKLAVLK---------RALNVVGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAgMLQVS 726
Cdd:cd14884 242 SDSLDPSEEEKAKdeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKAAAECLQIEEEDLENVIKYK-NIRVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 727 TDelasalttdiqyfkgdmIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMQTLD--------IG 797
Cdd:cd14884 321 HE-----------------VIRTErRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDiysineaiIS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 798 ILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVLFlHEQVECVQEGVTMETAYSPgNQNGVLDFffqkPSGFLTLLDE 876
Cdd:cd14884 384 ILDIYGFEELSGNDFDQLCINLANEKLNnYYINNEIE-KEKRIYARENIICCSDVAP-SYSDTLIF----IAKIFRRLDD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 877 ESQM-----------IWSVESNFPKKLQslLESSNTNAVYSPMKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNK 945
Cdd:cd14884 458 ITKLknqgqkktddhFFRYLLNNERQQQ--LEGKVSYGFVLNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 946 DSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfkfrghksallskkmtasSIIGENKNYLelskllkkkgtst 1025
Cdd:cd14884 536 DKIETSIETLISCSSNRFLRE------------------------------------ANNGGNKGNF------------- 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1026 flqrlergdpVTIASQLRKSLMDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLS 1105
Cdd:cd14884 567 ----------LSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
....*....
gi 312147315 1106 FSDFLSRYK 1114
Cdd:cd14884 637 KKETAAALK 645
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
438-1155 |
2.61e-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: 2.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFIL 517
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMF---KGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 518 SGERGSGKSEASKQIIRHLTCRAGAS--RATLDsRFKHVVCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 595
Cdd:cd01386 79 LGRSGSGKTTNCRHILEYLVTAAGSVggVLSVE-KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDF-DQAGQLASASI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 596 YTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLC--AHRYLNQTIQDDastgERSLNREKLAVLKRALNV 673
Cdd:cd01386 157 QTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAesNSFGIVPLQKPE----DKQKAAAAFSKLQAAMKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 674 VGFSSLEVENLFVILAAILHLGDIRFTALNEGNSAFVSDLQLLEQVAGMLQVSTDELASAL------------TTDIQYF 741
Cdd:cd01386 233 LGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 742 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQdeQKSMQTldIGILDIFGFE--EFQKNE----FEQL 815
Cdd:cd01386 313 SPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSS--HHSTSS--ITIVDTPGFQnpAHSGSQrgatFEDL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 816 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPS--------------GFLTLLDEESQMI 881
Cdd:cd01386 389 CHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedrrGLLWLLDEEALYP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 882 WSVESNFPKKLQSllessntnaVYSPMKDGNGNVALK--DHGTAFTIMHYAGR--VMYDVVGaieknkdslsqnllFVMK 957
Cdd:cd01386 469 GSSDDTFLERLFS---------HYGDKEGGKGHSLLRrsEGPLQFVLGHLLGTnpVEYDVSG--------------WLKA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 958 TSENVvinhlfqSKLSQTGSLVSAYPSFKFRGHKSALLSKKMTassiigenknylelskllkkkgtstflqrlergdpvt 1037
Cdd:cd01386 526 AKENP-------SAQNATQLLQESQKETAAVKRKSPCLQIKFQ------------------------------------- 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1038 iasqlrkslMD-IIGKLQKCTPHFIHCIRPN------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRL 1104
Cdd:cd01386 562 ---------VDaLIDTLRRTGLHFVHCLLPQhnagkderstssPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHM 632
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 312147315 1105 SFSDFLSRYKPLADTFLREKKEQS--AAERcRLV---LQQCKLQ--GWQMGVRKVFLK 1155
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 ... |
446-1155 |
1.67e-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: 1.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 446 RFGNNQIYTFIGDILLLVNPYKELPIYSSmvsqlyfSSSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILSGERGSGK 525
Cdd:cd14937 10 RYKKNYIYTIAEPMLISINPYQVIDVDIN-------EYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGSGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 526 SEASKQIIRHLTCRAGA----SRATLDSRFkhvvcILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGARIYTYLLE 601
Cdd:cd14937 83 TEASKLVIKYYLSGVKEdneiSNTLWDSNF-----ILEAFGNAKTLKNNNSSRYGKYIKIELDEY-QNIVSSSIEIFLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 602 KSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL-NQTIQ----DDASTGER---SLNREKLAVLKralnv 673
Cdd:cd14937 157 NIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIvNKNVVipeiDDAKDFGNlmiSFDKMNMHDMK----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 674 vgfsslevENLFVILAAILHLGDIRFTALNEGNSAFVSDL-----QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 748
Cdd:cd14937 232 --------DDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELdknnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 749 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLHSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 828
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNY----IGILDIFGFEIFSKNSLEQLLINIANEEIHSIY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 829 NEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfffqkpsgfltLLDEESQMIWSVESNF--PKKLQSLLESSNTNAVys 906
Cdd:cd14937 380 LYIVYEKETELYKAEDILIESVKYTTNES-IID-----------LLRGKTSIISILEDSClgPVKNDESIVSVYTNKF-- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 907 pMKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSkLSQTGSLvsaypsfk 986
Cdd:cd14937 446 -SKHEKYASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-VEVSESL-------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 987 frGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrKSLMDIIGKLQKCTPHFIHCIRP 1066
Cdd:cd14937 516 --GRKNLITFKYL--------------------------------------------KNLNNIISYLKSTNIYFIKCIKP 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1067 NNSKLPDTFDNFYVSAQLQYIGVLEMVKI---FRYGYpvrlSFSDFLSRYKPL-----ADTFLREKKEQSaaercRLVLQ 1138
Cdd:cd14937 550 NENKEKNNFNQKKVFPQLFSLSIIETLNIsffFQYKY----TFDVFLSYFEYLdystsKDSSLTDKEKVS-----MILQN 620
|
730
....*....|....*..
gi 312147315 1139 QCKLQGWQMGVRKVFLK 1155
Cdd:cd14937 621 TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
439-1114 |
2.20e-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: 2.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 439 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKL-------CSSLPPHLFSCVERAFHQLFREQR 511
Cdd:cd14893 3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQTplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 512 PQCFILSGERGSGKSEASKQIIRHLtCRAGASRA-------------TLDSRFKHVVCILEAFGHAKTTLNDLSSCFIKY 578
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYL-CEIGDETEprpdsegasgvlhPIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 579 FELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEE--KYGLHLNNlCAHRYlNQTIQDDASTGE 656
Cdd:cd14893 162 ISVEF-SKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNK-CVNEF-VMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 657 RSLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDIRF-------TALNEGNSAFVSDLQ--------LLEQVAG 721
Cdd:cd14893 239 FALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQscalkdpaQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 722 MLQVSTDELASALTTDiQYFKGD-----MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL-----HSQDEQKSM 791
Cdd:cd14893 319 LLEVEPVVLDNYFRTR-QFFSKDgnktvSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdRYEKSNIVI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 792 QTLDIGILDIFGFEEF--QKNEFEQLCVNMTNEKMHH-YINEVL-----FLHEQVECVQEGVTMETAYS-PGNQNGVLDF 862
Cdd:cd14893 398 NSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHfYVQNTLainfsFLEDESQQVENRLTVNSNVDiTSEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 863 FFQKPSGFLTLLDEESQMIWSVESNFPKKLQSLLE-----------SSNTNAVYSPMKDGNgnvalkdhgTAFTIMHYAG 931
Cdd:cd14893 478 FEDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEavgglsrpnmgADTTNEYLAPSKDWR---------LLFIVQHHCG 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 932 RVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAyPSFKFRGHKSALLSKKMTASSiigENKNy 1011
Cdd:cd14893 549 KVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAA-KQTEERGSTSSKFRKSASSAR---ESKN- 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1012 lelskllkkKGTSTFLQRLERGDPVTIAsqlrkslMDIIGKlqkctpHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLE 1091
Cdd:cd14893 624 ---------ITDSAATDVYNQADALLHA-------LNHTGK------NFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVE 681
|
730 740
....*....|....*....|...
gi 312147315 1092 MVKIFRYGYPVRLSFSDFLSRYK 1114
Cdd:cd14893 682 LMQASRSIFTVHLTYGHFFRRYK 704
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
67-347 |
1.53e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 166.67 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 67 LKRLKHAKNPKVHFNLTDMLQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDE 146
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 147 DFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyldENGVDLtslrqmklqrpmsmltd 226
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA-------------NGNLEI----------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 227 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLV 306
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 312147315 307 NCNEEKASDIAASEFIEEMLLKAEIAWEEKMKEPLSASTLA 347
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
66-359 |
6.03e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 159.35 E-value: 6.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 66 FLKRLKHAKNPKVHFNLTDMLQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQD 145
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 146 EDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyldENGVDLtslrqmklqrpmsmlt 225
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY-------------NGNLEI---------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 226 dVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHL 305
Cdd:COG0666 136 -VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 312147315 306 VNCNEEKASDIAASEF---IEEMLLKAEIAWEEKMKEPLSASTLAQEEPYEEIIHDL 359
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 ... |
438-1154 |
2.83e-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: 161.16 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 438 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgkLCSSLPPHL----FSCVERAFHQLFREQRPQ 513
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKY------KCIDCIEDLslneYHVVHNALKNLNELKRNQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 514 CFILSGERGSGKSEASKQIIRHLTCRAGASRATLDSR-----------------------FKHVVCILEAFGHAKTTLND 570
Cdd:cd14938 76 SIIISGESGSGKSEIAKNIINFIAYQVKGSRRLPTNLndqeednihneentdyqfnmsemLKHVNVVMEAFGNAKTVKNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 571 LSSCFIKYFELQFceRKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNqtiqD 650
Cdd:cd14938 156 NSSRFSKFCTIHI--ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLN----N 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 651 DASTGERSLNREKLAVLKRALNVVGFSSLEVENLFVILAAILHLGDI---------------RFTALNEGNSAFVSDLQL 715
Cdd:cd14938 230 EKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkafrkksllmgkNQCGQNINYETILSELEN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 716 LEQVAGMLQVSTDELASAL-----TTDIQYFKGDMI------IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNsCLHS 784
Cdd:cd14938 310 SEDIGLDENVKNLLLACKLlsfdiETFVKYFTTNYIfndsilIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN-EKCT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 785 QDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFF 864
Cdd:cd14938 389 QLQNININTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 865 QKPSGFL-TLLDEESQMIWSVESNFPkklQSLLESSNTNAVYSPMKDGNGNvalkdhGTAFTIMHYAGRVMYDVVGAIEK 943
Cdd:cd14938 469 GPTEGSLfSLLENVSTKTIFDKSNLH---SSIIRKFSRNSKYIKKDDITGN------KKTFVITHSCGDIIYNAENFVEK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 944 NKDSLSQNLLFVMKTSENVVINHLFQsklsqtgslvsaypSFKFRghksallskkmTASSIIGENKNYLELSKLlkkkgt 1023
Cdd:cd14938 540 NIDILTNRFIDMVKQSENEYMRQFCM--------------FYNYD-----------NSGNIVEEKRRYSIQSAL------ 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1024 STFLQRLERGDPVTIaSQLRKSLMDIIGKLQKCTPHFIHCIRPNNSK-LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPV 1102
Cdd:cd14938 589 KLFKRRYDTKNQMAV-SLLRNNLTELEKLQETTFCHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPH 667
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 312147315 1103 RLSFSDFLSRYKpladtflreKKEQSAAERCRLVLQQCKL--QGWQMGVRKVFL 1154
Cdd:cd14938 668 KFTLNEFLSIFD---------IKNEDLKEKVEALIKSYQIsnYEWMIGNNMIFL 712
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
557-1123 |
6.30e-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: 110.22 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 557 ILEAFGHAKTTLNDLSSCFIKYFELQFC----ERKQQLTGARIYTYLLEKSRLVSQPLGQS------NFLIFYLLMDGLS 626
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVAfglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 627 AEE-----KYGLHLNNL--CAHRYLNQTIQDDA------STGERSLNREKLAVlkRALNVVGFSSLEVENLFVILAAILH 693
Cdd:cd14894 335 AFPfmrllAKELHLDGIdcSALTYLGRSDHKLAgfvskeDTWKKDVERWQQVI--DGLDELNVSPDEQKTIFKVLSAVLW 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 694 LGDIRFTALNEGNSAFVSD---LQLLEQVAGMLQV-STDELASALTTDIQYFKGDMIIRRHTIQIAEF--FRDLLAKSLY 767
Cdd:cd14894 413 LGNIELDYREVSGKLVMSStgaLNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVnhVRDTLARLLY 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 768 SRLFSFLVNTMN-----SCLHSQDEQKSMQTLD--------IGILDIFGFEEFQKNEFEQLCVNMTNEKMhhYINEvlfl 834
Cdd:cd14894 493 QLAFNYVVFVMNeatkmSALSTDGNKHQMDSNAsapeavslLKIVDVFGFEDLTHNSLDQLCINYLSEKL--YARE---- 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 835 hEQVecvqegvtMETAYSP-------GNQNGVLdFFFQKPSGF------LTLLDEESQMIWSVESNFPKKLQSLLESSNT 901
Cdd:cd14894 567 -EQV--------IAVAYSSrphltarDSEKDVL-FIYEHPLGVfasleeLTILHQSENMNAQQEEKRNKLFVRNIYDRNS 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 902 NAVYSP---MKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvviNHLfqSKLSQTGSL 978
Cdd:cd14894 637 SRLPEPprvLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNS---SHF--CRMLNESSQ 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 979 VSAYPSfkfrghksallskkmTASSIIGENKNylelskllKKKGTSTFLqrlergdpvtiaSQLRKSLMDIIGKLQKCTP 1058
Cdd:cd14894 712 LGWSPN---------------TNRSMLGSAES--------RLSGTKSFV------------GQFRSHVNVLTSQDDKNMP 756
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312147315 1059 HFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG----YPVRLSFSDFLSRYKPLadtfLRE 1123
Cdd:cd14894 757 FYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSsssySAIDISKSTLLTRYGSL----LRE 821
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
89-302 |
7.45e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 103.59 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 89 AIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARY-----DNAFIAEILIDRGVNVNHQDEDFWTPMHIA-CACDN-P 161
Cdd:PHA03100 42 AKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAiSKKSNsY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 162 DIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLrqmklqrpmsmlTDVKHFLSSGGNVNEKN 241
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLIDKGVDINAK------------NRVNYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312147315 242 DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQAN 302
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
94-326 |
4.89e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 98.20 E-value: 4.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 94 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACAC-----DNPDIVLLLV 168
Cdd:PHA03100 14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 169 LAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLR-------QMKLQRPMSMLTDVKHFLSSGGNVNEKN 241
Cdd:PHA03100 94 EYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNsdgenllHLYLESNKIDLKILKLLIDKGVDINAKN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 242 degvtllhmacasgykeVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLVNCNEEKASDIAASEF 321
Cdd:PHA03100 174 -----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
|
....*
gi 312147315 322 IEEML 326
Cdd:PHA03100 237 NKEIF 241
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
463-581 |
3.83e-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: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 463 VNPYKELPIYSSmvSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFREQRPQCFILSGERGSGKSEASKQIIRHLTCRAGA 542
Cdd:cd01363 5 VNPFKELPIYRD--SKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFN 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 312147315 543 SRATLDSRF-----KHVVC----------ILEAFGHAKTTLNDLSSCFIKYFEL 581
Cdd:cd01363 83 GINKGETEGwvyltEITVTledqilqanpILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
81-301 |
1.34e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 92.43 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 81 NLTDMLQDAIIHHNDKE------VLRLLKEGADPHTLVSSGGSLLHLCAR--YDNAFIaEILIDRGVNVNHQDEDFWTPM 152
Cdd:PHA02876 267 NSIDDCKNTPLHHASQApslsrlVPKLLERGADVNAKNIKGETPLYLMAKngYDTENI-RTLIMLGADVNAADRLYITPL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 153 HIACACD-NPDIVLLLVLAGANVLLQDVNGNIPLDYAveGTESSSILLTYLDENGVDLTSLRQmKLQRPMSM-------L 224
Cdd:PHA02876 346 HQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYA--AVRNNVVIINTLLDYGADIEALSQ-KIGTALHFalcgtnpY 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312147315 225 TDVKHFLSSGGNVNEKNDEGVTLLHMACASGYK-EVVSLILEHGGDLNIVDDQYWTPLHLAAKYgqTNLVKLLLMHQA 301
Cdd:PHA02876 423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGA 498
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
227-307 |
8.06e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 227 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHgGDLNIVDDQyWTPLHLAAKYGQTNLVKLLLMHQANPHLV 306
Cdd:pfam12796 13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVK 90
|
.
gi 312147315 307 N 307
Cdd:pfam12796 91 D 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
86-178 |
6.87e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 86 LQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRgVNVNHQDEDfWTPMHIACACDNPDIVL 165
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 312147315 166 LLVLAGANVLLQD 178
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
97-306 |
5.90e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.60 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 97 EVLRLL-KEGADPHTLVSSGGSLLHLCARYDN--AFIAEILIDRGVNVNHQDEDFWTPMHI-----ACacdNPDIVLLLV 168
Cdd:PHA03095 98 DVIKLLiKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVllksrNA---NVELLRLLI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 169 LAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLRQMKLQRPMSMLT-------DVKHFLSSGGNVNEKN 241
Cdd:PHA03095 175 DAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgssckrsLVLPLLIAGISINARN 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147315 242 DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLV 306
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
126-311 |
7.98e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.77 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 126 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVllQDVNGNIPLDYAVEGTESSSILLTYLDEN 205
Cdd:PHA02874 13 DIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADI--NHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 206 GVDLTSLRQMKLQRPMsmltdVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAA 285
Cdd:PHA02874 91 GVDTSILPIPCIEKDM-----IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
|
170 180
....*....|....*....|....*.
gi 312147315 286 KYGQTNLVKLLLMHQANPHLVNCNEE 311
Cdd:PHA02874 166 KHNFFDIIKLLLEKGAYANVKDNNGE 191
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
124-309 |
2.49e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 74.23 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 124 RYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLqdvngnIPLDyAVEGTESSSILLTYLD 203
Cdd:PHA02874 44 RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIP-CIEKDMIKTILDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 204 ENGVDLTSLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHL 283
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180
....*....|....*....|....*.
gi 312147315 284 AAKYGQTNLVKLLLMHQANPhLVNCN 309
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHI-MNKCK 221
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
107-307 |
2.50e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 74.68 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 107 DPHTLVSSGGSLLHLCARYDNAFIAEI--LIDRGVNVNHQDEDFWTPMH--IACACDN-PDIVLLLVLAGANVLLQDVNG 181
Cdd:PHA03095 4 DESVDIIMEAALYDYLLNASNVTVEEVrrLLAAGADVNFRGEYGKTPLHlyLHYSSEKvKDIVRLLLEAGADVNAPERCG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 182 NIPLDYavegtesssilltYLdENGvdlTSLRQMKLqrpmsmltdvkhFLSSGGNVNEKNDEGVTLLHmACASGY---KE 258
Cdd:PHA03095 84 FTPLHL-------------YL-YNA---TTLDVIKL------------LIKAGADVNAKDKVGRTPLH-VYLSGFninPK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 312147315 259 VVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTN--LVKLLLMHQANPHLVN 307
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVD 184
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
96-311 |
5.44e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.52 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 96 KEVLRLLKEGADP-----------HTLVSSGGSL-------------------------LHLCARYDN-AFIAEILIDRG 138
Cdd:PHA03095 28 EEVRRLLAAGADVnfrgeygktplHLYLHYSSEKvkdivrllleagadvnapercgftpLHLYLYNATtLDVIKLLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 139 VNVNHQDEDFWTPMHIACA--CDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDL------- 209
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVyavddrf 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 210 -TSLRQMKL-----QRPMSMLTDvkhflsSGGNVNEKNDEGVTLLH-MACASGYKE-VVSLILEHGGDLNIVDDQYWTPL 281
Cdd:PHA03095 188 rSLLHHHLQsfkprARIVRELIR------AGCDPAATDMLGNTPLHsMATGSSCKRsLVLPLLIAGISINARNRYGQTPL 261
|
250 260 270
....*....|....*....|....*....|
gi 312147315 282 HLAAKYGQTNLVKLLLMHQANPHLVNCNEE 311
Cdd:PHA03095 262 HYAAVFNNPRACRRLIALGADINAVSSDGN 291
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
95-325 |
6.63e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 73.38 E-value: 6.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 95 DKEVLRLLKE-GADPHTLV-SSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGA 172
Cdd:PHA02878 146 EAEITKLLLSyGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 173 NVLLQDVNGNIPLDYAVEGTESSSILltyldengvdltslrqmklqrpmsmltdvKHFLSSGGNVNEKND-EGVTLLHMA 251
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDIL-----------------------------KLLLEHGVDVNAKSYiLGLTALHSS 276
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312147315 252 CASgyKEVVSLILEHGGDLNIVDDQYWTPLHLAAK-YGQTNLVKLLLMHqanphlVNCNEEKASDIAASE-FIEEM 325
Cdd:PHA02878 277 IKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILISN------ICLLKRIKPDIKNSEgFIDNM 344
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
248-299 |
1.59e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.14 E-value: 1.59e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 312147315 248 LHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMH 299
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
119-274 |
3.18e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.98 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 119 LHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLlvlaganvLLQDVNGNIpldyavegtesssil 198
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL--------LLEHADVNL--------------- 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312147315 199 ltyldengvdltslrqmklqrpmsmltdvkhflssggnvnekNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVD 274
Cdd:pfam12796 58 ------------------------------------------KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
244-297 |
1.22e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.14 E-value: 1.22e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 312147315 244 GVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLL 297
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
81-302 |
3.05e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.55 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 81 NLTDMLQDAIIHH-----NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDedfwtpMHIA 155
Cdd:PHA02876 172 NAKDIYCITPIHYaaergNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND------LSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 156 CACDNPDI--VLLLVLAGANVLLQDVNGNIPLDYAVEgTESSSILLTYLDENGVDLTSlRQMKLQRPMSMLT-------D 226
Cdd:PHA02876 246 KAIRNEDLetSLLLYDAGFSVNSIDDCKNTPLHHASQ-APSLSRLVPKLLERGADVNA-KNIKGETPLYLMAkngydteN 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312147315 227 VKHFLSSGGNVNEKNDEGVTLLHMACA-SGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQAN 302
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
94-332 |
5.87e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 66.91 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 94 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGAN 173
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 174 VLLQDVNGNIPLDYAVEgtesssilltYLDengvdltslrqmklqrpmsmLTDVKHFLSSGGNVNEKNDEGVTLLHMACA 253
Cdd:PHA02874 183 ANVKDNNGESPLHNAAE----------YGD--------------------YACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 254 sgYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYG-QTNLVKLLLMHQANPHLVNCNEEKASDIAASEFIEEMLLKAEIA 332
Cdd:PHA02874 233 --HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIA 310
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
126-302 |
3.50e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.08 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 126 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDEN 205
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 206 GVDLTSLRQMKLQRPMSMLTDVKHFlSSGGNVNEKNDEGVTLLHMAC-ASGYKEVVSLILEHGGDLNIVDDQYWTPLHLA 284
Cdd:PHA02876 236 NINKNDLSLLKAIRNEDLETSLLLY-DAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
|
170
....*....|....*....
gi 312147315 285 AKYG-QTNLVKLLLMHQAN 302
Cdd:PHA02876 315 AKNGyDTENIRTLIMLGAD 333
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
36-283 |
5.78e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.42 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 36 GQRQRLVKRMRCEQI----KAYYEREKAFQKQEGFLKRL--------KHAKNPKVHFNLTdMLQDAIIHH---NDKEVLR 100
Cdd:PLN03192 433 GEKERVVGTLGCGDIfgevGALCCRPQSFTFRTKTLSQLlrlktstlIEAMQTRQEDNVV-ILKNFLQHHkelHDLNVGD 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 101 LLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILiDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVN 180
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 181 GNIPLDYAVEGTESSSILLTYL------DENGVDLTSLRQMKlqrpmSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACAS 254
Cdd:PLN03192 591 GNTALWNAISAKHHKIFRILYHfasisdPHAAGDLLCTAAKR-----NDLTAMKELLKQGLNVDSEDHQGATALQVAMAE 665
|
250 260 270
....*....|....*....|....*....|
gi 312147315 255 GYKEVVSLILEHGGDLNIVD-DQYWTPLHL 283
Cdd:PLN03192 666 DHVDMVRLLIMNGADVDKANtDDDFSPTEL 695
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
86-309 |
6.16e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.39 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 86 LQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIacACDNPDIVL 165
Cdd:PHA02875 6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHD--AVEEGDVKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 166 LLVLAGANVLLQDV---NGNIPLDYAVEgtesssilltyldengvdLTSLRQMKLqrpmsmltdvkhFLSSGGNVNEKND 242
Cdd:PHA02875 84 VEELLDLGKFADDVfykDGMTPLHLATI------------------LKKLDIMKL------------LIARGADPDIPNT 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312147315 243 EGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLVNCN 309
Cdd:PHA02875 134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
134-188 |
1.59e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 52.35 E-value: 1.59e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 312147315 134 LIDRG-VNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYA 188
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
119-311 |
2.08e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 59.12 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 119 LHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIAC-----------------------------ACDNPD------- 162
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdAFNNRNveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 163 ----------------------------IVLLLVLAGANVLLQDVN-GNIPLDYAVEG--TESSSILLTYLDE-NGVDLT 210
Cdd:PHA02878 121 ltnrykniqtidlvyidkkskddiieaeITKLLLSYGADINMKDRHkGNTALHYATENkdQRLTELLLSYGANvNIPDKT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 211 SLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMacASGY---KEVVSLILEHGGDLNIVDD-QYWTPLHLAAK 286
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI--SVGYckdYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
|
250 260
....*....|....*....|....*
gi 312147315 287 YGQTnlVKLLLMHQANPHLVNCNEE 311
Cdd:PHA02878 279 SERK--LKLLLEYGADINSLNSYKL 301
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
227-304 |
2.08e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 2.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312147315 227 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPH 304
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1412-1672 |
4.22e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.80 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1412 GTPQCALPPAAPPGDEDDSEPvyiemlghaarPDSPDPGESvyeemkcclpddgGPGAGSFLLHGASPPLLH--RAPEDE 1489
Cdd:PHA03247 2549 GDPPPPLPPAAPPAAPDRSVP-----------PPRPAPRPS-------------EPAVTSRARRPDAPPQSArpRAPVDD 2604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1490 AAGPPGDACDIPPPfPNllPHRPPllvfPPTPvtcSPASDESPLTPLEVKKLPVLETNLKYPVQPEGSSP-------LSP 1562
Cdd:PHA03247 2605 RGDPRGPAPPSPLP-PD--THAPD----PPPP---SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrlgRAA 2674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1563 QYSKSQKGDGDRPASPGLALFNGSGRASPPSTPPP---PPPPPGPPPAPYRPCAHLAFPPEPA-----PVNAGKAGPSAE 1634
Cdd:PHA03247 2675 QASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEpapHALVSATPLPPGPAAARQASPALPAapappAVPAGPATPGGP 2754
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 312147315 1635 APKVHPK-----PNSAPVAGPCSSFPKIPYSPVKATRADARKA 1672
Cdd:PHA03247 2755 ARPARPPttagpPAPAPPAAPAAGPPRRLTRPAVASLSESRES 2797
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
86-273 |
5.04e-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: 57.48 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 86 LQDAIIHHNDKEvLRLLKEGADPHTLVSSGGSLLHL-----CARYDN---AFIAEILI--DRGVNVNHQDED--FWTPMH 153
Cdd:pfam15439 6 KLEKRRRQEEGI-KRSGEEVAGKVRDISSEGRHFRMgfmtmPASQDRlphPCAAGMSIrsQSLHSVGSGDEDgsLPSSRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 154 IACACDNPDIVLLLVLAGANVLLQDVNGNIpldyaVEGTESSSILLTYLDENgVDLTSLRQMKLQR-PMSMLT------- 225
Cdd:pfam15439 85 QPPPKPKRDPSTKLSMSSEAVSAGLSAGAK-----ETPSETEALSKPRPHSD-EYSRKIPPPKPKRsPNTQLSgsfdeip 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312147315 226 -------DVKHFLSSGG---NVNEKNDE---------GVTLLHMACA----------SGYKEVVSLILEHGGDLNIV 273
Cdd:pfam15439 159 apyirphGLLQRASSSDgpsPAPLPDEEeepvyiemvGNVLRDFSPTtpdddpdqseAVYEEMKYPLPEDSGAANGP 235
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
114-384 |
9.96e-08 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 57.23 E-value: 9.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 114 SGGSLLH--LCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDN--PDIVLLLVLAGANVLLQDVNGNIP-LDYA 188
Cdd:PHA02716 176 TGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPiMTYI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 189 VE----GTESSSILLTYLDENGVD-----LTSLRQMKLQRPMSMltdVKHFLSSGGNVNEKNDEGVTLLHMACASGY--K 257
Cdd:PHA02716 256 INidniNPEITNIYIESLDGNKVKnipmiLHSYITLARNIDISV---VYSFLQPGVKLHYKDSAGRTCLHQYILRHNisT 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 258 EVVSLILEHGGDLNIVDDQYWTPLHlaakygqTNLVKLLLMHQANPH--------LVNCNEEKASDIAASEFIEEMLLKA 329
Cdd:PHA02716 333 DIIKLLHEYGNDLNEPDNIGNTVLH-------TYLSMLSVVNILDPEtdndirldVIQCLISLGADITAVNCLGYTPLTS 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 312147315 330 EIAweekmkeplsastLAQEEPYEEIIHDLpvLSSKLSPLVLPIAKQDSLLEKDI 384
Cdd:PHA02716 406 YIC-------------TAQNYMYYDIIDCL--ISDKVLNMVKHRILQDLLIRVDD 445
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
115-168 |
3.08e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 3.08e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 312147315 115 GGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLV 168
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
236-284 |
3.62e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.50 E-value: 3.62e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147315 236 NVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLA 284
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
152-308 |
7.06e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.84 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 152 MHIACACD-----NPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILL-----TYLDENGVDLTSLRQMKLQRpm 221
Cdd:PHA02875 1 MDQVALCDailfgELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLlmkhgAIPDVKYPDIESELHDAVEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 222 SMLTDVKHFLSSGGNVNEK-NDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQ 300
Cdd:PHA02875 79 GDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
....*...
gi 312147315 301 ANPHLVNC 308
Cdd:PHA02875 159 ACLDIEDC 166
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
159-312 |
1.02e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.69 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 159 DNP--DIVLLLVLAGANVLLQDVNGNIPLdyavegtesSSILLTYLDENgvdltslrqmklqrpmSMLTDVKHFLSSGGN 236
Cdd:PHA02798 47 DSPstDIVKLFINLGANVNGLDNEYSTPL---------CTILSNIKDYK----------------HMLDIVKILIENGAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 237 VNEKNDEGVTLLHMACASGY---KEVVSLILEHGGDLNIVDDQYWTPLHLAAKYG---QTNLVKLLLMHQANPHLVNcNE 310
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHN-NK 180
|
..
gi 312147315 311 EK 312
Cdd:PHA02798 181 EK 182
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1355-1671 |
5.07e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1355 PRPHSDDYStmkkIPPRKPKRSPNTKLSGSYEeisgSRPGdaRPAGAPGAAARVLTPGTPQCALPPAAPPGDEDDSEPvy 1434
Cdd:PHA03247 2559 APPAAPDRS----VPPPRPAPRPSEPAVTSRA----RRPD--APPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDP-- 2626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1435 iEMLGHAARPDSPDPGESVYEEMKCCLPDDGGPG---------AGSFLLHGASPPLLHRAPEDEAA-GPPGDACDIPPPF 1504
Cdd:PHA03247 2627 -PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGrvsrprrarRLGRAAQASSPPQRPRRRAARPTvGSLTSLADPPPPP 2705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1505 PNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETnlkyPVQPEG----SSPLSPQYSKSQKGDGDRPASP-- 1578
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG----PATPGGparpARPPTTAGPPAPAPPAAPAAGPpr 2781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1579 -----GLALFNGSGRASPPSTPPPPPPPPGPPPAPYRPCAHLAFPPEPAPVNAGKAGPS-AEAPKVHPKPNSAPVA---- 1648
Cdd:PHA03247 2782 rltrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPpPPGPPPPSLPLGGSVApggd 2861
|
330 340
....*....|....*....|....*..
gi 312147315 1649 ----GPCSSFPKIPYSPvkaTRADARK 1671
Cdd:PHA03247 2862 vrrrPPSRSPAAKPAAP---ARPPVRR 2885
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
59-190 |
6.57e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.05 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 59 AFQKQEGFLKRLKHAKNPK-VHFNLTDMLQDAIIHHNDK-EVLRLLKEGAD--PHTLVSSGG-----------SLLHLCA 123
Cdd:PTZ00322 12 AFAAQLFFGTEGSRKRRAKpISFERMAAIQEEIARIDTHlEALEATENKDAtpDHNLTTEEVidpvvahmltvELCQLAA 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312147315 124 RYDnAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVE 190
Cdd:PTZ00322 92 SGD-AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
263-317 |
1.32e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 1.32e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 312147315 263 ILEHGG-DLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLVNCNEEKASDIA 317
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
70-287 |
2.61e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 48.83 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 70 LKHAKNPKVHF-NLTDMLQDAIIHHNDKEVLRLLKEGADPHTLV-SSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDED 147
Cdd:PHA02875 55 MKHGAIPDVKYpDIESELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 148 FWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSilltyldengvdltslrqmklqrpmsmltdV 227
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI------------------------------C 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312147315 228 KHFLSSGGNVNEKNDEG-VTLLHMACASGYKEVVSLILEHGGDLNI---VDDQYWTPLHLAAKY 287
Cdd:PHA02875 185 KMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNImfmIEGEECTILDMICNM 248
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
278-307 |
3.17e-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: 3.17e-05
10 20 30
....*....|....*....|....*....|.
gi 312147315 278 WTPLHLAA-KYGQTNLVKLLLMHQANPHLVN 307
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
130-297 |
6.44e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 47.52 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 130 IAEILIDRGVNVNHQDEDFWTPM-----HIACACDNPDIVLLLVLAGANVLLQDVNGNIPLdYAV--EGTESSSILLTYL 202
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL-YCLlsNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 203 DENGVDLTSLRQMKlqrpmsmLTDVKHFLSSGGNVNekndegvtllhmacasgyKEVVSLILEHGGDLNIVDDQY-WTPL 281
Cdd:PHA02798 132 IENGADTTLLDKDG-------FTMLQVYLQSNHHID------------------IEIIKLLLEKGVDINTHNNKEkYDTL 186
|
170 180
....*....|....*....|
gi 312147315 282 HLAAKYG----QTNLVKLLL 297
Cdd:PHA02798 187 HCYFKYNidriDADILKLFV 206
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
243-272 |
1.18e-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: 40.65 E-value: 1.18e-04
10 20 30
....*....|....*....|....*....|
gi 312147315 243 EGVTLLHMACASGYKEVVSLILEHGGDLNI 272
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
95-189 |
1.80e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.17 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 95 DKEVLR-LLKEGADPHTLVSSGGSLLHLCARYDNAFIAEI--LIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAG 171
Cdd:PHA03095 201 RARIVReLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
|
90
....*....|....*...
gi 312147315 172 ANVLLQDVNGNIPLDYAV 189
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMV 298
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
276-305 |
2.08e-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: 2.08e-04
10 20 30
....*....|....*....|....*....|
gi 312147315 276 QYWTPLHLAAKYGQTNLVKLLLMHQANPHL 305
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
243-275 |
2.33e-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: 2.33e-04
10 20 30
....*....|....*....|....*....|....
gi 312147315 243 EGVTLLHMACAS-GYKEVVSLILEHGGDLNIVDD 275
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
95-217 |
2.60e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.42 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 95 DKEVLRLL-KEGAD-PHTLVSSGGSLLHLCARYD---NAFIAEILIDRGVNVNHQDEDFWTPMHI-ACACD-NPDIVLLL 167
Cdd:PHA02859 65 NVEILKFLiENGADvNFKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLL 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 312147315 168 VLAGANVLLQDVNGNIPLdYAVEGTESSSILLTYLDENGVDLTSLRQMKL 217
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNIL-YSYILFHSDKKIFDFLTSLGIDINETNKSGY 193
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
243-272 |
2.93e-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: 39.55 E-value: 2.93e-04
10 20 30
....*....|....*....|....*....|
gi 312147315 243 EGVTLLHMACASGYKEVVSLILEHGGDLNI 272
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1347-1672 |
4.13e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.55 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1347 AANEALARPRPHSDDYSTMKKIPPRKPKRSPntklsgsyeeiSGSRPGDARPAGAPGAAARVLTPGTPQCALPPAAPPGD 1426
Cdd:PHA03307 133 DLSEMLRPVGSPGPPPAASPPAAGASPAAVA-----------SDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1427 EDDSEPVYIEMLGHAARPDSPDPGESvyeemkcclpDDGGPGAGSFLLHGASPPLLHRAPEDEAAGPPGDACDIPPPFPN 1506
Cdd:PHA03307 202 ASPRPPRRSSPISASASSPAPAPGRS----------AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1507 LLPHRPPllvfPPTPVTCSPASDESPLTPlevkklpvletnlkyPVQP--EGSSPLSPQYSKSQKGDGDRPASPGLALFN 1584
Cdd:PHA03307 272 ASGWNGP----SSRPGPASSSSSPRERSP---------------SPSPssPGSGPAPSSPRASSSSSSSRESSSSSTSSS 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1585 GSGRASPPSTpPppppppgpppapyrpcahlafPPEPAPVNAGKAGPSAEAPkvhPKPNSAPVAGPCSSFPKIpySPVKA 1664
Cdd:PHA03307 333 SESSRGAAVS-P---------------------GPSPSRSPSPSRPPPPADP---SSPRKRPRPSRAPSSPAA--SAGRP 385
|
....*...
gi 312147315 1665 TRADARKA 1672
Cdd:PHA03307 386 TRRRARAA 393
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
277-304 |
5.89e-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: 5.89e-04
10 20
....*....|....*....|....*...
gi 312147315 277 YWTPLHLAAKYGQTNLVKLLLMHQANPH 304
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1331-1548 |
5.99e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.87 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1331 SASYEAVSACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPAGAPGAAARVLT 1410
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPA 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1411 PgTPQCALPPAA----PPGDEDDSEPVYIEMLGHAAR-PDSPDPGESVYEEMKCCLPDDGGPGAGSFLLHGASPPLLHRA 1485
Cdd:PRK12323 456 A-APAAAARPAAagprPVAAAAAAAPARAAPAAAPAPaDDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADP 534
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312147315 1486 PEDEAAGPPGdacdiPPPFPNLLPHRPPLLVFPPTPvtcsPASDESPLTPLEVKKLPVLETNL 1548
Cdd:PRK12323 535 DDAFETLAPA-----PAAAPAPRAAAATEPVVAPRP----PRASASGLPDMFDGDWPALAARL 588
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1347-1578 |
7.74e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 44.68 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1347 AANEALARPRPHSDDYSTMKKIP-----PRKPKRSPNTKlsgsyEEISGSRPGdarpagapgaaarvlTPGTPQCALPPA 1421
Cdd:PTZ00449 602 SAQRPTRPKSPKLPELLDIPKSPkrpesPKSPKRPPPPQ-----RPSSPERPE---------------GPKIIKSPKPPK 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1422 AP--PGDEDDSEPVYIEMLGHAARPD----SPDPGESVYEEMKCCLPDDGGPgagSFLLHGASPPLLHRAPEDEAAgPPG 1495
Cdd:PTZ00449 662 SPkpPFDPKFKEKFYDDYLDAAAKSKetktTVVLDESFESILKETLPETPGT---PFTTPRPLPPKLPRDEEFPFE-PIG 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1496 DAcDIPPPFPNLLPHRPpllVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQPEgSSPLSPQySKSQKGDGDRP 1575
Cdd:PTZ00449 738 DP-DAEQPDDIEFFTPP---EEERTFFHETPADTPLPDILAEEFKEEDIHAETGEPDEAM-KRPDSPS-EHEDKPPGDHP 811
|
...
gi 312147315 1576 ASP 1578
Cdd:PTZ00449 812 SLP 814
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1411-1574 |
1.44e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.52 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1411 PGTPQCALPPAAPPGDEDDSEPVYIEMLGHAARPDSPDPGESVYEEMKcclPDDGGPGAgsfllhgASPPLLHRAPEDEA 1490
Cdd:PHA03378 698 PRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRAR---PPAAAPGR-------ARPPAAAPGRARPP 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1491 AGPPGDACDIPPP--------FPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETN-------LKYPVQPE 1555
Cdd:PHA03378 768 AAAPGAPTPQPPPqappapqqRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGvkrgrpsLKKPAALE 847
|
170
....*....|....*....
gi 312147315 1556 GSSPLSPQYSkSQKGDGDR 1574
Cdd:PHA03378 848 RQAAAGPTPS-PGSGTSDK 865
|
|
| NYAP_C |
pfam15452 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_C is a C-terminal ... |
1652-1880 |
1.87e-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: 42.26 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1652 SSFPKIPYSPVKATRADARKAGSSASPPAPYSPPSSRPLSSPL--DELASLFNSGRSVLRKSAAGRKIREAEGFETNMNI 1729
Cdd:pfam15452 1 RSSPSVPHSTVKNQVQEGAKGGNAASISCGSAIAGSRSRTPTSplEELTSLFGSGWSLQRKLSSGRKSKEPAEKTDEARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1730 SS----------RDD-----PSTSEITSETQDRN---ANNHGIQLSN----SLSSAITAENGNSISNGLPEEdGYSRlSI 1787
Cdd:pfam15452 81 WSgsteplprmeREErghhgAGASGIPVRAQGWDgvdGPPGFRALSRlglpSPCQTFPACHRNGEPKEVCRL-GRSA-ST 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1788 SGTGTSTFQRHRDSHT--TQVIHQLRLSENESV----ALQELLDWRRKLCEE------------GQDWQQIL----HHAE 1845
Cdd:pfam15452 159 SGVRQAGGDVPRQSSLplRQALSQSQVPPMQWVerdgKLLEVIERKRCLCKEikarrrpdkglcKQDSMPILpswrKNPE 238
|
250 260 270
....*....|....*....|....*....|....*
gi 312147315 1846 PRvpppppckkpsllkKPEGASCNRLPSELWDTTI 1880
Cdd:pfam15452 239 TR--------------KSGTPPCSRQQTVFWDTAI 259
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1411-1669 |
2.16e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1411 PGTPQCALPPaappgdeDDSEPvyiemlgHAARPdSPDPGESVYeemkcclPDDGGPGAGSFLlhgaSPPLLHRAPEDEA 1490
Cdd:PHA03247 2475 PGAPVYRRPA-------EARFP-------FAAGA-APDPGGGGP-------PDPDAPPAPSRL----APAILPDEPVGEP 2528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1491 AGP-------------PGDACDIPPPFPNLLPhrppllvfPPTPVTCSPASDESPlTPLEvkklPVLETNLKYP-VQPEG 1556
Cdd:PHA03247 2529 VHPrmltwirgleelaSDDAGDPPPPLPPAAP--------PAAPDRSVPPPRPAP-RPSE----PAVTSRARRPdAPPQS 2595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1557 SSPLSPqysksqKGDGDRPASPGlalfngsgrASPPSTPPPPPPPPGpppapyrpcahlAFPPEPAPVNAGKAGPSAEAP 1636
Cdd:PHA03247 2596 ARPRAP------VDDRGDPRGPA---------PPSPLPPDTHAPDPP------------PPSPSPAANEPDPHPPPTVPP 2648
|
250 260 270
....*....|....*....|....*....|...
gi 312147315 1637 KVHPKPNSAPvagPCSSFPKIPYSPVKATRADA 1669
Cdd:PHA03247 2649 PERPRDDPAP---GRVSRPRRARRLGRAAQASS 2678
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1330-1673 |
2.25e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1330 LSASYEAVSACLSAAREAANealaRPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDArpagapgaaarvl 1409
Cdd:PHA03307 44 VSDSAELAAVTVVAGAAACD----RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSP------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1410 TPGTPQCALPPAA---PPGDEDDSEPVYIEMLGHAARPDSPDPGESVyeemkcCLPDDGGPGAGsfllHGASPPLLHRA- 1485
Cdd:PHA03307 107 TPPGPSSPDPPPPtppPASPPPSPAPDLSEMLRPVGSPGPPPAASPP------AAGASPAAVAS----DAASSRQAALPl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1486 ---PEDEAAGPPGDACDIPPPFPNLLPHRPPllvfPPTPVTCSPASDESPLTP--LEVKKLPVLETNLKYPVQ-----PE 1555
Cdd:PHA03307 177 sspEETARAPSSPPAEPPPSTPPAAASPRPP----RRSSPISASASSPAPAPGrsAADDAGASSSDSSSSESSgcgwgPE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1556 GSSPLSPQYSKSQKGDGDRPASPGLALFN-GSGRASPPSTPPPPPPPPGPPPAPYRPCAH-------------LAFPPEP 1621
Cdd:PHA03307 253 NECPLPRPAPITLPTRIWEASGWNGPSSRpGPASSSSSPRERSPSPSPSSPGSGPAPSSPrasssssssressSSSTSSS 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 312147315 1622 APVNAGKAGPSAEAPKVHPKPNSAPVAGPCSSFPKIPySPVKATRADARKAG 1673
Cdd:PHA03307 333 SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP-RPSRAPSSPAASAG 383
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
1410-1673 |
2.90e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 42.74 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1410 TPGTPQCALP---PAAPPGDEDDSEPvyiemlGHAARPDSP-----DPGeSVYEE--MKCCLPDDGGPGagsfllhgasp 1479
Cdd:PHA03379 412 TYGTPRPPVEkprPEVPQSLETATSH------GSAQVPEPPpvhdlEPG-PLHDQhsMAPCPVAQLPPG----------- 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1480 PLLHRAPEDEAAGPPGDACDIPPPFPNLLPH--RP----PLLVFPPTPVTCSPasdesplTPLEVKKLPVLETNLKYPVQ 1553
Cdd:PHA03379 474 PLQDLEPGDQLPGVVQDGRPACAPVPAPAGPivRPweasLSQVPGVAFAPVMP-------QPMPVEPVPVPTVALERPVC 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1554 PegssplspqysksqkgdgdrpaSPGLALFNGSGRASPPSTPPPPPPPPGPPPAPYRpcahlafPPEPAPVNAGKAGPSA 1633
Cdd:PHA03379 547 P----------------------APPLIAMQGPGETSGIVRVRERWRPAPWTPNPPR-------SPSQMSVRDRLARLRA 597
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 312147315 1634 EA-PKVHP----------KPNSAPVAGPC----SSFPKIPYSPVkatrADARKAG 1673
Cdd:PHA03379 598 EAqPYQASvevqppqltqVSPQQPMEYPLepeqQMFPGSPFSQV----ADVMRAG 648
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
149-178 |
3.21e-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: 3.21e-03
10 20 30
....*....|....*....|....*....|.
gi 312147315 149 WTPMHIACA-CDNPDIVLLLVLAGANVLLQD 178
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
1343-1526 |
3.30e-03 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 42.25 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1343 AAREAANEAlarPRPHSDDYSTMKKIPPRKPKRSPNT----KLSGSYEEISGSRPGDARPAGAPGAAARVLTPGTPQCAL 1418
Cdd:PHA03321 486 AAPPPEPAA---APSPATYYTRMGGGPPRLPPRNRATetlrPDWGPPAAAPPEQMEDPYLEPDDDRFDRRDGAAAAATSH 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1419 PPAAPPGDE--------DDSEPVYIEMlghaarpdspdPGESVYEEMkccLPD-DGGPGAGSFLLHGASPPLLHRAP--- 1486
Cdd:PHA03321 563 PREAPAPDDdpiyegvsDSEEPVYEEI-----------PTPRVYQNP---LPRpMEGAGEPPDLDAPTSPWVEEENPiyg 628
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 312147315 1487 -EDEAAGPPGDACDIPPPFPNLLPHRPPLLVFPPTPVTCSP 1526
Cdd:PHA03321 629 wGDSPLFSPPPAARFPPPDPALSPEPPALPAHRPRPGALAP 669
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
79-283 |
3.44e-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: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 79 HFNLTDMLQDAiiHHNDKEVL-RLLK-EGADPHTLVSSGGSLLHLCARYDNAFIAEILID---RGVNVNHQDEDFW--TP 151
Cdd:cd22192 15 RISESPLLLAA--KENDVQAIkKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDLYQgeTA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 152 MHIACACDNPDIVLLLVLAGANVLLQDVNGnipldyavegtesssillTYLdengvdltslrqmkLQRPMSMLTDVKHFL 231
Cdd:cd22192 93 LHIAVVNQNLNLVRELIARGADVVSPRATG------------------TFF--------------RPGPKNLIYYGEHPL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 312147315 232 SsggnvnekndegvtllHMACAsGYKEVVSLILEHGGDLNIVDDQYWTPLHL 283
Cdd:cd22192 141 S----------------FAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
236-310 |
3.80e-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: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 236 NVNEKNDEGVTLLHMAcASGYKEVVSLILEH-------GGDLNIVDDQYW-------TPLHLAAKYGQTNLVKLLLMHQA 301
Cdd:TIGR00870 74 NLSCRGAVGDTLLHAI-SLEYVDAVEAILLHllaafrkSGPLELANDQYTseftpgiTALHLAAHRQNYEIVKLLLERGA 152
|
90
....*....|
gi 312147315 302 NPHL-VNCNE 310
Cdd:TIGR00870 153 SVPArACGDF 162
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
101-155 |
4.13e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 4.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 312147315 101 LLKEG-ADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIA 155
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
281-331 |
4.55e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.17 E-value: 4.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 312147315 281 LHLAAKYGQTNLVKLLLMHQANPHLVNCNEEKASDIAAS----EFIEEMLLKAEI 331
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKnghlEIVKLLLEHADV 55
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1343-1655 |
4.88e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1343 AAREAANE--ALARPRPHSddystmKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPAGAPGAAARVLTPGTPQcalPP 1420
Cdd:PHA03247 2687 AARPTVGSltSLADPPPPP------PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA---RP 2757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1421 AAPPGDEDDSEPVYIEMLGHAARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLLHGASPPLLHRAPEDEAAGPPGDACDI 1500
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPT 2837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 1501 PPPFPNLlPHRPPLL----VFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQPEGSSPLSPQysksqkgDGDRPA 1576
Cdd:PHA03247 2838 APPPPPG-PPPPSLPlggsVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPD-------QPERPP 2909
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312147315 1577 SPglalfngsgrASPPSTPPPPPPPPgpppapyrpcahlafPPEPAPVNAGKAGPSAEAPkvhPKPNSAPVAGPCSSFP 1655
Cdd:PHA03247 2910 QP----------QAPPPPQPQPQPPP---------------PPQPQPPPPPPPRPQPPLA---PTTDPAGAGEPSGAVP 2960
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
259-306 |
5.21e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.59 E-value: 5.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 312147315 259 VVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLV 306
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNII 207
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
147-174 |
5.53e-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: 5.53e-03
10 20
....*....|....*....|....*...
gi 312147315 147 DFWTPMHIACACDNPDIVLLLVLAGANV 174
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
149-174 |
6.06e-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: 6.06e-03
10 20
....*....|....*....|....*.
gi 312147315 149 WTPMHIACACDNPDIVLLLVLAGANV 174
Cdd:pfam13606 3 NTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
86-205 |
6.50e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.02 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147315 86 LQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHL----CARYDnafIAEILIDRGVNVNHQDEDF-WTPMHIacACDN 160
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIsvgyCKDYD---ILKLLLEHGVDVNAKSYILgLTALHS--SIKS 279
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 312147315 161 PDIVLLLVLAGANVLLQDVNGNIPLdyavegtesSSILLTYLDEN 205
Cdd:PHA02878 280 ERKLKLLLEYGADINSLNSYKLTPL---------SSAVKQYLCIN 315
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
245-317 |
7.23e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 7.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312147315 245 VTLLHMAcASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQTNLVKLLLMHQANPHLVNCNEEKASDIA 317
Cdd:PTZ00322 84 VELCQLA-ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
|
| |
