|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
415-1133 |
0e+00 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 1359.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGARIY 574
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKHLTGARIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 575 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLAVLKQALNVVGF 654
Cdd:cd14878 161 TYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREDVSTAERSLNREKLAVLKQALNVVGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 655 SNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 734
Cdd:cd14878 241 SSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 735 FFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHE 814
Cdd:cd14878 321 FYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 815 QVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTNAVYSPLKDGNGNVA 894
Cdd:cd14878 401 QTECVQEGVTMETAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAVYSPMKDGNGNVA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 895 LKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLsqtgslvsaypsfkfrghksalls 974
Cdd:cd14878 481 LKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKL------------------------ 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 975 kkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFD 1054
Cdd:cd14878 537 ---------------------------------------VTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFD 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884524 1055 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCKLQGWQMGVRKVFLK 1133
Cdd:cd14878 578 NFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
416-1133 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 668.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRS--ADLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAAS-------SRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQL 568
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALSGSgssksssSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQF-DPTGRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 569 TGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ-TMQDDVSTGERSLNREKLAVLKQ 647
Cdd:cd00124 159 VGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDyLNSSGCDRIDGVDDAEEFQELLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 648 ALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 725
Cdd:cd00124 239 ALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 726 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSmqTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd00124 319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAES--TSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTNAvysp 885
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDFPDNQD-CLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF---- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 886 lkdgngnVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSenvvinhlfqsklsqtgslvsaypsfkf 965
Cdd:cd00124 472 -------SKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG---------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 966 rghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLTDIIGKLQKCTPHFIHCIRPN 1045
Cdd:cd00124 517 ----------------------------------------------------SQFRSQLDALMDTLNSTQPHFVRCIKPN 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFL-REKKEHLAAERCRLVLQQCKLQGWQ 1124
Cdd:cd00124 545 DEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATeKASDSKKAAVLALLLLLKLDSSGYQ 624
|
....*....
gi 1622884524 1125 MGVRKVFLK 1133
Cdd:cd00124 625 LGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
404-1143 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 611.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 404 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 483
Cdd:smart00242 9 EDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKY---RGKSRGELPPHVFAIADNAYRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 484 LFQEQRPQCFILSGERGSGKSEASKQIIRHLTcrAASSRAMLDSRFKHVM----CILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:smart00242 86 MLNDKENQSIIISGESGAGKTENTKKIMQYLA--SVSGSNTEVGSVEDQIlesnPILEAFGNAKTLRNNNSSRFGKFIEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 560 QFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ------TMQDDVstg 633
Cdd:smart00242 164 HFDA-KGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQggcltvDGIDDA--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 634 erslnrEKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSA-FVSDLQLLEQVAGMLQVSTDELASAL 712
Cdd:smart00242 240 ------EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 713 TTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQ 792
Cdd:smart00242 314 TKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYF----IGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 793 LCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFpkkLQS 872
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDW-TFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTF---LEK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 873 LLESSNTNAVYSPLKdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQ 952
Cdd:smart00242 466 LNQHHKKHPHFSKPK--------KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 953 TGslvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGKLQ 1032
Cdd:smart00242 538 AG-------------------SKKR-----------------------------------FQTVGSQFKEQLNELMDTLN 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1033 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCR 1112
Cdd:smart00242 564 STNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTW-PPWGGDAKKACE 642
|
730 740 750
....*....|....*....|....*....|...
gi 1622884524 1113 LVLQQCKL--QGWQMGVRKVFLKYWHADQLNDL 1143
Cdd:smart00242 643 ALLQSLGLdeDEYQLGKTKVFLRPGQLAELEEL 675
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
416-1133 |
8.16e-176 |
|
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: 546.87 E-value: 8.16e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLY---RGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCeRKQQLTGARIYT 575
Cdd:cd01379 79 SGESGAGKTESANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT-STGAVTGARISE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 576 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEK-HGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLAVLKQALNVVGF 654
Cdd:cd01379 158 YLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 655 SNLEVENLFVILAAILHLGDIRFTALTEG----NSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 730
Cdd:cd01379 238 TKEEVDSVYSILAAILHIGDIEFTEVESNhqtdKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 731 QIAEFFRDLLAKSLYSRLFSFLVNTMNScLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 810
Cdd:cd01379 318 EEATDARDAMAKALYGRLFSWIVNRINS-LLKPDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 811 FLHEQVECVQEGVTMET-AYSpgNQNGVLDFFFQKPSGFLTLLDEESQmiwsmesnFPKKL-QSLLESSNTNavyspLKD 888
Cdd:cd01379 397 FAWEQQEYLNEGIDVDLiEYE--DNRPLLDMFLQKPMGLLALLDEESR--------FPKATdQTLVEKFHNN-----IKS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 889 GNgNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfkfrgh 968
Cdd:cd01379 462 KY-YWRPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 969 ksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSK 1048
Cdd:cd01379 517 ----------------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSR 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1049 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtFLREKKEHLAAERCRLVLQQCKLQGWQMGVR 1128
Cdd:cd01379 551 QAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLA--FKWNEEVVANRENCRLILERLKLDNWALGKT 628
|
....*
gi 1622884524 1129 KVFLK 1133
Cdd:cd01379 629 KVFLK 633
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
404-1133 |
9.68e-166 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 521.46 E-value: 9.68e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 404 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQ 483
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAY---RGKRRGELPPHIFAIADEAYRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 484 LFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMC----ILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:pfam00063 79 MLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRLEEQILqsnpILEAFGNAKTVRNNNSSRFGKYIEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 560 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSlnr 639
Cdd:pfam00063 159 QF-DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDS--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 640 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 719
Cdd:pfam00063 235 EEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 720 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTN 799
Cdd:pfam00063 315 GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSL---DVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 800 EKMHHYINEVLFLHEQVECVQEGVTmetaYSP---GNQNGVLDFFFQKPSGFLTLLDEesqmiwsmESNFPKK-----LQ 871
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIE----WTFidfGDNQPCIDLIEKKPLGILSLLDE--------ECLFPKAtdqtfLD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 872 SLLESSNTNAVY-SPLKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSkl 950
Cdd:pfam00063 460 KLYSTFSKHPHFqKPRLQGE---------THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPD-- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 951 sqtGSLVSAYPSFKFRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGK 1030
Cdd:pfam00063 529 ---YETAESAAANESGKSTPKRTKKKR-----------------------------------FITVGSQFKESLGELMKT 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1031 LQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHlAAER 1110
Cdd:pfam00063 571 LNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGD-AKKG 649
|
730 740
....*....|....*....|....*
gi 1622884524 1111 CRLVLQQCKLQG--WQMGVRKVFLK 1133
Cdd:pfam00063 650 CEAILQSLNLDKeeYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
403-1235 |
2.38e-148 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 497.29 E-value: 2.38e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 403 NDDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFH 482
Cdd:COG5022 68 VDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSY---SGKNRLELEPHVFAIAEEAYR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 483 QLFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:COG5022 145 NLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEKQILAtnpILEAFGNAKTVRNDNSSRFGKYIKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 560 QFCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNR 639
Cdd:COG5022 225 EFDE-NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEF 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 640 EKLAvlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFvSDLQLLEQVAGMLQVSTDELASALTTDIQYF 719
Cdd:COG5022 304 KITL---DALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNGAAIF-SDNSVLDKACYLLGIDPSLFVKWLVKRQIKT 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 720 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTN 799
Cdd:COG5022 380 GGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNF----IGVLDIYGFEIFEKNSFEQLCINYTN 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 800 EKMHHYINEVLFLHEQVECVQEGVtmetAYSP----GNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLe 875
Cdd:COG5022 456 EKLQQFFNQHMFKLEQEEYVKEGI----EWSFidyfDNQPCIDLIEKKNPLGILSLLDEECVMPHATDESFTSKLAQRL- 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 876 SSNTNAVYSPLKDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsqtgs 955
Cdd:COG5022 531 NKNSNPKFKKSRFRD---------NKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE------ 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 956 lvsaypsfkfrghksallskkmtassiigENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCT 1035
Cdd:COG5022 596 -----------------------------ENIE--------------------SKGRFPTLGSRFKESLNSLMSTLNSTQ 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1036 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR---EKKEHLAAERCR 1112
Cdd:COG5022 627 PHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWtgeYTWKEDTKNAVK 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1113 LVLQQCKL--QGWQMGVRKVFLKywhADQLNDLCLQ----LQRKIITCQKVIRGFLARQHLLQKISiRQQEVTS-INSFL 1185
Cdd:COG5022 707 SILEELVIdsSKYQIGNTKVFFK---AGVLAALEDMrdakLDNIATRIQRAIRGRYLRRRYLQALK-RIKKIQViQHGFR 782
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884524 1186 QNTE-DMGLKTYDALVIQNASDIA--RENDRLRSEMNAPYHKE---KLEVRNTQEE 1235
Cdd:COG5022 783 LRRLvDYELKWRLFIKLQPLLSLLgsRKEYRSYLACIIKLQKTikrEKKLRETEEV 838
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
416-1133 |
5.34e-148 |
|
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: 471.48 E-value: 5.34e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVR--SQRPPHLFWIADQAYRRLLETGRNQCILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQLTGARIYT 575
Cdd:cd14897 80 SGESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTE-NGQLLGAKIDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 576 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYL-NQTMQDDV--STGERSLNREKLAVLKQALNVV 652
Cdd:cd14897 159 YLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILrDDNRNRPVfnDSEELEYYRQMFHDLTNIMKLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 653 GFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQI 732
Cdd:cd14897 239 GFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 733 AEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTL-DIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 811
Cdd:cd14897 319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGpSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 812 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTnavYSPLKDGNg 891
Cdd:cd14897 399 PRERSEYEIEGIEWRDIEYHDNDD-VLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPR---YVASPGNR- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 892 nvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsaypsfkfrghksa 971
Cdd:cd14897 474 --------VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF------------------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 972 llskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPD 1051
Cdd:cd14897 521 ---------------------------------------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPN 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1052 TFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlrEKKEHLAAERCRLVLQQCKLQGWQMGVRKVF 1131
Cdd:cd14897 556 KFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS--NKVRSDDLGKCQKILKTAGIKGYQFGKTKVF 633
|
..
gi 1622884524 1132 LK 1133
Cdd:cd14897 634 LK 635
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
416-1133 |
5.62e-148 |
|
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: 472.12 E-value: 5.62e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLY---RNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTcrAASS------RAMLDSRfkhvmCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLT 569
Cdd:cd01381 79 SGESGAGKTESTKLILQYLA--AISGqhswieQQILEAN-----PILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV-IE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 570 GARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLnqtMQDDVSTGERSLNREKLAVLKQAL 649
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYL---TQGNCLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 650 NVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 727
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNldASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 728 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSmQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 807
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDS-SRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 808 EVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQmiwsmesnFPKKL-QSLLESSN----TNAV 882
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEFVDNQD-VLDLIALKPMNIMSLIDEESK--------FPKGTdQTMLEKLHsthgNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 883 YSPLKdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsayps 962
Cdd:cd01381 458 YLKPK--------SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 963 fkfrghksallskkmtassiigenknylelskllkkkGTSTflqrleRGDPVTIASQLRKSLTDIIGKLQKCTPHFIHCI 1042
Cdd:cd01381 520 -------------------------------------GSET------RKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCI 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1043 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKE---HLAAERCRLVLQQCK 1119
Cdd:cd01381 557 KPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTdcrAATRKICCAVLGGDA 636
|
730
....*....|....
gi 1622884524 1120 LqgWQMGVRKVFLK 1133
Cdd:cd01381 637 D--YQLGKTKIFLK 648
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
417-1133 |
6.35e-146 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 467.08 E-value: 6.35e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLF----QEQRPQC 492
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKS---SLPPHIFAVADRAYQSMLgrlaRGPKNQC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 493 FILSGERGSGKSEASKQIIRHLT--CRAASSramLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTG 570
Cdd:cd14889 80 IVISGESGAGKTESTKLLLRQIMelCRGNSQ---LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF--RNGHVKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 571 ARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTM--QDDVSTGerslnREKLAVLKQA 648
Cdd:cd14889 155 AKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAgcKREVQYW-----KKKYDEVCNA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 649 LNVVGFSNLEVENLFVILAAILHLGDIRFTaLTEGNSAFVSDLQ--LLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 726
Cdd:cd14889 230 MDMVGFTEQEEVDMFTILAGILSLGNITFE-MDDDEALKVENDSngWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNScLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 806
Cdd:cd14889 309 HHTKQQAEDARDSIAKVAYGRVFGWIVSKINQ-LLAPKDDSSVELREIGILDIFGFENFAVNRFEQACINLANEQLQYFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 807 NEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntNAVYSpl 886
Cdd:cd14889 388 NHHIFLMEQKEYKKEGIDWKEITYKDNKP-ILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG---NSYYG-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 887 KDGNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfr 966
Cdd:cd14889 462 KSRS-------KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPR------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 967 ghksallSKKMTASSiigenknylelskllkKKGTSTFLQrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNN 1046
Cdd:cd14889 528 -------AKLPQAGS----------------DNFNSTRKQ--------SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNH 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1047 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREKKEHLAAERCRLVLQQCKLQGWQMG 1126
Cdd:cd14889 577 VKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKLVGWKCG 652
|
....*..
gi 1622884524 1127 VRKVFLK 1133
Cdd:cd14889 653 KTRLFFK 659
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
1221-1566 |
2.64e-141 |
|
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: 443.06 E-value: 2.64e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1221 PYHKEKLEVRNTQEEGSKRTEDK---------SGPRHFHPSSMSVCMAVDGLG-QCLAGPSIWSPSLHSVFSMDDNSSLP 1290
Cdd:pfam15439 1 LYRKEKLEKRRRQEEGIKRSGEEvagkvrdisSEGRHFRMGFMTMPASQDRLPhPCAAGMSIRSQSLHSVGSGDEDGSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1291 SPRKQPPPKPKRDPNTRLSASYEAVSACLS-AAREAA--NEALARPRPHSDDYStmKKIPPRKPKRSPNTKLSGSYEEIS 1367
Cdd:pfam15439 81 SSRKQPPPKPKRDPSTKLSMSSEAVSAGLSaGAKETPseTEALSKPRPHSDEYS--RKIPPPKPKRSPNTQLSGSFDEIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1368 GSRPgdaRPPGAPGTAArvlTPGTPQCAlppatpPGDEDDGEPVYIEMLGHPAR-------PDSPDPGESVYEEMKCCLP 1440
Cdd:pfam15439 159 APYI---RPHGLLQRAS---SSDGPSPA------PLPDEEEEPVYIEMVGNVLRdfspttpDDDPDQSEAVYEEMKYPLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1441 DDGGPGAGSFLRASPPLL-----HGAPEDE--------AAGPPGDMCDIPPPFPNLLPHRPPLLVFPPTPVTCSPASDES 1507
Cdd:pfam15439 227 EDSGAANGPPPLASSPLLadphsPISPESDsalpssqcATPTKKDLCDIPAPFPNLLPHRPPLLVFPPAPVTCSPASDES 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884524 1508 PLTPLEVKKLPVLEtNLKYPVQSEgSSPLSPQYSKSQKGDGDRPASPGLALFNGSGRAS 1566
Cdd:pfam15439 307 PLTPLEVKKLPVLE-NVSYSKQPA-SSPLSPQESKHQREDKDRPSSPGLAVLTPSGRAR 363
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
421-1133 |
5.98e-141 |
|
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: 452.77 E-value: 5.98e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 421 IQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERG 500
Cdd:cd01378 7 LKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESY---RGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 501 SGKSEASKQIIRHLTcrAASSRAMLD-SRFKHVM----CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 575
Cdd:cd01378 84 AGKTEASKRIMQYIA--AVSGGSESEvERVKDMLlasnPLLEAFGNAKTLRNDNSSRFGKYMEIQF-DFKGEPVGGHITN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 576 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVStgerSLNREK-LAVLKQALNVVGF 654
Cdd:cd01378 161 YLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVD----GIDDAAdFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 655 SNLEVENLFVILAAILHLGDIRFTALTEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM---IIRRHTIQ 731
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEEGNAA-ISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 732 IAEFFRDLLAKSLYSRLFSFLVNTMNSCLLS-QDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 810
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAkSGGKKKV----IGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 811 FLHEQVECVQEGVTMETayspgnqngvLDFFF---------QKPSGFLTLLDEESqmiwsmesNFPKK------LQSLLE 875
Cdd:cd01378 392 LKAEQEEYVREGIEWTP----------IKYFNnkiicdlieEKPPGIFAILDDAC--------LTAGDatdqtfLQKLNQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 876 SSNTNAVYSPLKDgngnvALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTgs 955
Cdd:cd01378 454 LFSNHPHFECPSG-----HFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 956 lvsaypsfkfrghksallSKKMtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGKLQKCT 1035
Cdd:cd01378 527 ------------------SKKR-----------------------------------PPTAGTKFKNSANALVETLMKKQ 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1036 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAD-TFLRekKEHLAAERCRLV 1114
Cdd:cd01378 554 PSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPkTWPA--WDGTWQGGVESI 631
|
730 740
....*....|....*....|.
gi 1622884524 1115 LQQCKLQG--WQMGVRKVFLK 1133
Cdd:cd01378 632 LKDLNIPPeeYQMGKTKIFIR 652
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
415-1133 |
6.94e-137 |
|
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: 442.97 E-value: 6.94e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSsgKLcSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNR--RL-GKLPPHIFAIADVAYHAMLRKKKNQCIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTcrAASSRAMLDSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQLTGA 571
Cdd:cd01385 78 ISGESGSGKTESTNFLLHHLT--ALSQKGYGSGVEQTILGagpVLEAFGNAKTAHNNNSSRFGKFIQVNYRE-NGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 572 RIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqdDVSTGERSLNREKLAVLKQALNV 651
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQS---DCYTLEGEDEKYEFERLKQAMEM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 652 VGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 729
Cdd:cd01385 232 VGFLPETQRQIFSVLSAVLHLGNIEYKKKAYHRdeSVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 730 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 809
Cdd:cd01385 312 LPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 810 LFLHEQVECVQEGVTMETAYSPGNqNGVLDFFFQKPSGFLTLLDEesqmiwsmESNFPKKL-QSLLE------SSNTNAV 882
Cdd:cd01385 392 IFKLEQEEYKKEGISWHNIEYTDN-TGCLQLISKKPTGLLCLLDE--------ESNFPGATnQTLLAkfkqqhKDNKYYE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 883 YSPLKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgSLVSAYPS 962
Cdd:cd01385 463 KPQVME-----------PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVR-----------ELIGIDPV 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 963 FKFRghkSALLS---KKMTASSIIGEN--KNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLTDIIGKLQKCTPH 1037
Cdd:cd01385 521 AVFR---WAVLRaffRAMAAFREAGRRraQRTAGHSLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPF 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1038 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQ 1117
Cdd:cd01385 598 FIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDR 677
|
730
....*....|....*.
gi 1622884524 1118 CKlqgWQMGVRKVFLK 1133
Cdd:cd01385 678 DN---YQIGKTKVFLK 690
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
416-1133 |
1.26e-136 |
|
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: 441.38 E-value: 1.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFsssGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYF---GKRMGALPPHIFALAEAAYTNMQEDGKNQSVII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLtCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 575
Cdd:cd14883 79 SGESGAGKTETTKLILQYL-CAVTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCF-DASGHIKGAIIQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 576 YLLEKSRLVSQPLGQSNFLIFSLLMDG--LSAEEKHGLHLNNLCAHRYLNQtmqDDVSTGERSLNREKLAVLKQALNVVG 653
Cdd:cd14883 157 YLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQ---SGCIRIDNINDKKDFDHLRLAMNVLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 654 FSNLEVENLFVILAAILHLGDIRFTALtEGNSA--FVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQ 731
Cdd:cd14883 234 IPEEMQEGIFSVLSAILHLGNLTFEDI-DGETGalTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 732 IAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLF 811
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRF----IGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 812 LHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntNAVY-SPLKdgn 890
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVFTDNQE-CLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEK---HPYYeKPDR--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 891 gnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsAYPSfkfrghks 970
Cdd:cd14883 462 -----RRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELF------------TYPD-------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 971 alLSKKMTASSIIGENKNylelskllkKKGTStflqrleRGDPvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLP 1050
Cdd:cd14883 517 --LLALTGLSISLGGDTT---------SRGTS-------KGKP-TVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1051 DTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEHLAAERCRLVLQQCKLQG--WQMGVR 1128
Cdd:cd14883 578 NVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCL-DPRARSADHKETCGAVRALMGLGGLPEdeWQVGKT 656
|
....*
gi 1622884524 1129 KVFLK 1133
Cdd:cd14883 657 KVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
418-1133 |
3.44e-133 |
|
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: 431.33 E-value: 3.44e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 418 LYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILS 496
Cdd:cd01384 4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQY---KGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 497 GERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVM---CILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 573
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLesnPLLEAFGNAKTVRNNNSSRFGKFVEIQF-DDAGRISGAAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 574 YTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ---DDVSTGErslnrEKLAVLKqALN 650
Cdd:cd01384 160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCfelDGVDDAE-----EYRATRR-AMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 651 VVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSD---LQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 727
Cdd:cd01384 234 VVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 728 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 807
Cdd:cd01384 314 LDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRL----IGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 808 EVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLqsllessntnavYSPLK 887
Cdd:cd01384 390 QHVFKMEQEEYTKEEIDWSYIEFVDNQD-VLDLIEKKPGGIIALLDEACMFPRSTHETFAQKL------------YQTLK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 888 DGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKD---SLSQNLLfvmKTSENVVINHLFQSKLSQTGSlvsayPSFK 964
Cdd:cd01384 457 DHKRFSKPKLSRTDFTIDHYAGDVTYQTDLFLDKNKDyvvAEHQALL---NASKCPFVAGLFPPLPREGTS-----SSSK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 965 FrghksallskkmtaSSiigenknylelskllkkkgtstflqrlergdpvtIASQLRKSLTDIIGKLQKCTPHFIHCIRP 1044
Cdd:cd01384 529 F--------------SS----------------------------------IGSRFKQQLQELMETLNTTEPHYIRCIKP 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1045 NNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLreKKEHLAAERCRLVLQQCKLQGWQ 1124
Cdd:cd01384 561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL--KGSDDEKAACKKILEKAGLKGYQ 638
|
....*....
gi 1622884524 1125 MGVRKVFLK 1133
Cdd:cd01384 639 IGKTKVFLR 647
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
416-1133 |
1.51e-132 |
|
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: 429.94 E-value: 1.51e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQY---SGRALGELPPHLFAIANLAFAKMLDAKQNQCVVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARIYT 575
Cdd:cd01387 79 SGESGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF--EGGVIVGAITSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 576 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVStGERSlnREKLAVLKQALNVVGFS 655
Cdd:cd01387 157 YLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIA-GKSD--ADDFRRLLAAMQVLGFS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 656 NLEVENLFVILAAILHLGDIRF-----TALTEGNSaFVSDLQlLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 730
Cdd:cd01387 234 SEEQDSIFRILASVLHLGNVYFhkrqlRHGQEGVS-VGSDAE-IQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 731 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEqrsmQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 810
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQ----DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 811 FLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEesqmiwsmESNFPKKLQ-SLLESSNTNAVYSPLKDg 889
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAFADNQP-VINLISKKPVGILHILDD--------ECNFPQATDhSFLEKCHYHHALNELYS- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 890 ngnvALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQtgslvsaypsfkfrgHK 969
Cdd:cd01387 458 ----KPRMPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQ---------------TD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 970 SALLSKkmtassiigenknylelskllkkkGTSTFLQRLERGDpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKL 1049
Cdd:cd01387 519 KAPPRL------------------------GKGRFVTMKPRTP--TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKE 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1050 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCKLQG-WQMGVR 1128
Cdd:cd01387 573 PMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPKDmYRLGAT 652
|
....*
gi 1622884524 1129 KVFLK 1133
Cdd:cd01387 653 KVFLR 657
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
416-1133 |
3.21e-127 |
|
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: 414.41 E-value: 3.21e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLcsSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY---RQKL--LDSPHVYAVADTAYREMMRDEINQSIII 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRAmLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 575
Cdd:cd01383 77 SGESGAGKTETAKIAMQYLAALGGGSSG-IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHF-DAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 576 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqdDVSTGERSLNREKLAVLKQALNVVGFS 655
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQS---NCLTIDGVDDAKKFHELKEALDTVGIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 656 NLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEF 735
Cdd:cd01383 232 KEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAID 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 736 FRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQ--RSmqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLH 813
Cdd:cd01383 312 ARDALAKAIYASLFDWLVEQINKSLEVGKRRtgRS-----ISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 814 EQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEesqmiwsmESNFPK--------KLQSLLessNTNAVYSp 885
Cdd:cd01383 387 EQEEYELDGIDWTKVDFEDNQE-CLDLIEKKPLGLISLLDE--------ESNFPKatdltfanKLKQHL---KSNSCFK- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 886 lkdgngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSEnvviNHLFQsklsqtgslvsaypsfkf 965
Cdd:cd01383 454 ----------GERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCS----CQLPQ------------------ 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 966 rghksaLLSKKMTassiigenkNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPN 1045
Cdd:cd01383 502 ------LFASKML---------DASRKALPLTKASGSDSQKQ-------SVATKFKGQLFKLMQRLENTTPHFIRCIKPN 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAerCRLVLQQCKLQG--W 1123
Cdd:cd01383 560 NKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLST--SVAILQQFNILPemY 637
|
730
....*....|
gi 1622884524 1124 QMGVRKVFLK 1133
Cdd:cd01383 638 QVGYTKLFFR 647
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
416-1133 |
6.12e-127 |
|
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: 413.09 E-value: 6.12e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd01380 2 AVLHNLKVRFCQrNAIYTYCGIVLVAINPYEDLPIYGEDIIQAY---SGQNMGELDPHIFAIAEEAYRQMARDEKNQSII 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASSRAMlDSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGA 571
Cdd:cd01380 79 VSGESGAGKTVSAKYAMRYFATVGGSSSGE-TQVEEKVLAsnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKN-YRIIGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 572 RIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ---TMQDDVStgerslNREKLAVLKQA 648
Cdd:cd01380 157 NMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQggsPVIDGVD------DAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 649 LNVVGFSNLEVENLFVILAAILHLGDIRFTAlTEGNSAFVS-DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRR 727
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKA-TRNDSASISpDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 728 HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYIN 807
Cdd:cd01380 310 LTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQHSF--IGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 808 EVLFLHEQVECVQEGVTMETAYSPGNQnGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL-QSLLESSntNAVYSPL 886
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDFYDNQ-PCID-LIEGKLGILDLLDEECRLPKGSDENWAQKLyNQHLKKP--NKHFKKP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 887 KDGNgnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvvinhlfqsklsqtgslvsaypsfkfr 966
Cdd:cd01380 464 RFSN---------TAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN--------------------------- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 967 gHKSallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNN 1046
Cdd:cd01380 508 -RKK--------------------------------------------TVGSQFRDSLILLMETLNSTTPHYVRCIKPND 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1047 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA---DTFLREKKEHLAAERCRLVLQQCKlqgW 1123
Cdd:cd01380 543 EKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLpskEWLRDDKKKTCENILENLILDPDK---Y 619
|
730
....*....|
gi 1622884524 1124 QMGVRKVFLK 1133
Cdd:cd01380 620 QFGKTKIFFR 629
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
415-1126 |
9.27e-124 |
|
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: 404.54 E-value: 9.27e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPK---EMPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASSRAmLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 574
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAGSTNG-VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF-DNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 575 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLhlNNLCAHRYLNQTMQDDVSTGERSLNREKLavlKQALNVVGF 654
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW--GSSAAYGYLSLSGCIEVEGVDDVADFEEV---VLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 655 SNLEVENLFVILAAILHLGDIRFTALTEGNSAF---VSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG--DMIIRRHT 729
Cdd:cd14872 231 DDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGcdPTRIPLTP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 730 IQiAEFFRDLLAKSLYSRLFSFLVNTMNsclLSQDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 809
Cdd:cd14872 311 AQ-ATDACDALAKAAYSRLFDWLVKKIN---ESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 810 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQsllessNTNAVYSPLKDG 889
Cdd:cd14872 387 TFKLEEALYQSEGVKFEHIDFIDNQP-VLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAAN------QTHAAKSTFVYA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 890 NgnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvsayPSFKFRghk 969
Cdd:cd14872 460 E----VRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--------------PPSEGD--- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 970 sallskkmtassiigenknylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKL 1049
Cdd:cd14872 519 ---------------------------------------QKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1050 PDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-ADTFLREKKehLAAERCRLVLQ---QCKlQGWQM 1125
Cdd:cd14872 560 ARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLvKTIAKRVGP--DDRQRCDLLLKslkQDF-SKVQV 636
|
.
gi 1622884524 1126 G 1126
Cdd:cd14872 637 G 637
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
415-1133 |
1.66e-123 |
|
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: 404.18 E-value: 1.66e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCF 493
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQY---SRRHLGELPPHIFAIANECYRCLWKRHDNQCI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 494 ILSGERGSGKSEASKQIIRHLT----------CRAASSR---AMLDSRfkhvmCILEAFGHAKTTLNDLSSCFIKYFELQ 560
Cdd:cd14873 78 LISGESGAGKTESTKLILKFLSvisqqslelsLKEKTSCveqAILESS-----PIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 561 FCErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQT--MQDDVSTGERSLN 638
Cdd:cd14873 153 ICQ-KGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSgcVEDKTISDQESFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 639 ReklaVLKqALNVVGFSNLEVENLFVILAAILHLGDIRFtaLTEGnSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 718
Cdd:cd14873 232 E----VIT-AMEVMQFSKEEVREVSRLLAGILHLGNIEF--ITAG-GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 719 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSmqtldIGILDIFGFEEFQKNEFEQLCVNMT 798
Cdd:cd14873 304 LRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKS-----IGILDIFGFENFEVNHFEQFNINYA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 799 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSlleSSN 878
Cdd:cd14873 379 NEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGE-CLD-LIEKKLGLLALINEESHFPQATDSTLLEKLHS---QHA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 879 TNAVYSPLKDGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvs 958
Cdd:cd14873 454 NNHFYVKPRVAVNN---------FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQ--- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 959 aypsfkfrghksallSKKMTASsiigenknylelskllkkkgtstflqrlERGDPvTIASQLRKSLTDIIGKLQKCTPHF 1038
Cdd:cd14873 522 ---------------DTLKCGS----------------------------KHRRP-TVSSQFKDSLHSLMATLSSSNPFF 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1039 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-----ADTFLREKkehlaaerCRL 1113
Cdd:cd14873 558 VRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmrnlaLPEDVRGK--------CTS 629
|
730 740
....*....|....*....|..
gi 1622884524 1114 VLQQCKLQG--WQMGVRKVFLK 1133
Cdd:cd14873 630 LLQLYDASNseWQLGKTKVFLR 651
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
416-1133 |
3.84e-122 |
|
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: 400.69 E-value: 3.84e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKY---KGKRREEMPPHIFAIADNAYRNMLQDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKH-------VMC--ILEAFGHAKTTLNDLSSCFIKYFELQFCErKQ 566
Cdd:cd01377 79 TGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledqiLQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGS-TG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 567 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ------TMQDDVstgerslnrE 640
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgeltiDGVDDA---------E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 641 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIqyFK 720
Cdd:cd01377 229 EFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPR--IK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 721 -GDMIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMT 798
Cdd:cd01377 307 vGREWVTKGqNKEQVVFSVGALAKALYERLFLWLVKRINKTL---DTKSKRQYF-IGVLDIAGFEIFEFNSFEQLCINYT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 799 NEKMHHYINEVLFLHEQVECVQEGVTMEtayspgnqngVLDF---------FFQKPS-GFLTLLDEESQMIWSMESNFPK 868
Cdd:cd01377 383 NEKLQQFFNHHMFVLEQEEYKKEGIEWT----------FIDFgldlqptidLIEKPNmGILSILDEECVFPKATDKTFVE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 869 KLQSLLESSNTN-AVYSPLKDGNGnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ 947
Cdd:cd01377 453 KLYSNHLGKSKNfKKPKPKKSEAH----------FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 948 SKLSQTGSlvsaypSFKFRGHKSALLskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDI 1027
Cdd:cd01377 523 DYEESGGG------GGKKKKKGGSFR-----------------------------------------TVSQLHKEQLNKL 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1028 IGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLA 1107
Cdd:cd01377 556 MTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGK 635
|
730 740
....*....|....*....|....*...
gi 1622884524 1108 AErCRLVLQQCKL--QGWQMGVRKVFLK 1133
Cdd:cd01377 636 AA-CEKILKALQLdpELYRIGNTKVFFK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
416-1133 |
7.24e-120 |
|
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: 394.44 E-value: 7.24e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcsSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSI----SKSPHVFSTASSAYQGMCNNKKSQTIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASS---RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQ----- 566
Cdd:cd14888 78 ISGESGAGKTESTKYVMKFLACAGSEDikkRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKSkrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 567 ---QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHL--NNLCAHR-YLNQTMQDDVSTGERSLNRE 640
Cdd:cd14888 158 drgRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYeeNDEKLAKgADAKPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 641 KLAV-----------LKQ------ALNVVGFSNLEVENLFVILAAILHLGDIRFT---ALTEGNSAFVSDLQLLEQVAGM 700
Cdd:cd14888 238 YLTKsschelpdvddLEEfestlyAMQTVGISPEEQNQIFSIVAAILYLGNILFEnneACSEGAVVSASCTDDLEKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 701 LQVSTDELASALTTDiqyfkgdMIIRRH-------TIQIAEFFRDLLAKSLYSRLFSFLVNTMNScllSQDEQRSMQTLD 773
Cdd:cd14888 318 LGVDAEDLLNALCYR-------TIKTAHefytkplRVDEAEDVRDALARALYSCLFDKVVERTNE---SIGYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 774 IGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLD 853
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCV-DLLQEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 854 EESQmiwsmesnFPK-KLQSLlessnTNAVYSPLKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLF 932
Cdd:cd14888 467 EECF--------VPGgKDQGL-----CNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 933 VMKTSENVVINHLFQSKLSqtgslvsaypsfkfRGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergd 1012
Cdd:cd14888 534 VIKNSKNPFISNLFSAYLR--------------RGTDGNTKKKKF----------------------------------- 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1013 pVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYK 1092
Cdd:cd14888 565 -VTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYR 643
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1622884524 1093 PLADTFLREkkehlaaercrlvlqqcKLQGWQMGVRKVFLK 1133
Cdd:cd14888 644 ILLNGEGKK-----------------QLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
417-1091 |
3.71e-119 |
|
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: 392.47 E-value: 3.71e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFS-----SSGKLCSSLPPHLFSCVERAFHQLFQEQRP 490
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiiqnGEYFDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 491 QCFILSGERGSGKSEASKQIIRHLT-------------CRAASSRAMLDSRF----KHVMC--ILEAFGHAKTTLNDLSS 551
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTqlsqqeqnseevlTLTSSIRATSKSTKsieqKILSCnpILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 552 CFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCA---HRYLNQTMQD 628
Cdd:cd14907 163 RFGKYVSILVDKKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSgdrYDYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 629 DVSTgersLNREKL-AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRF--TALTEGNSAFVSDLQLLEQVAGMLQVST 705
Cdd:cd14907 243 EVDT----INDEKLfKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFddSTLDDNSPCCVKNKETLQIIAKLLGIDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 706 DELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLL--SQDEQRSMQ--TLDIGILDIFG 781
Cdd:cd14907 319 EELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMpkDEKDQQLFQnkYLSIGLLDIFG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 782 FEEFQKNEFEQLCVNMTNEKMHH-YINEVlFLHEQVECVQEGVT---METAYsPGNQNgVLDFFFQKPSGFLTLLDEESQ 857
Cdd:cd14907 399 FEVFQNNSFEQLCINYTNEKLQQlYISYV-FKAEEQEFKEEGLEdylNQLSY-TDNQD-VIDLLDKPPIGIFNLLDDSCK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 858 MIWSMESNFPKKLQSLLESSNTNAVYSPLKDgngnvalkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTS 937
Cdd:cd14907 476 LATGTDEKLLNKIKKQHKNNSKLIFPNKINK-----------DTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 938 ENVVINHLF----QSKLSQTGSLVSAYPSFKFRGHKsallskkmtassiigenknylelskllkkkgtstflqrlergdp 1013
Cdd:cd14907 545 KNRIISSIFsgedGSQQQNQSKQKKSQKKDKFLGSK-------------------------------------------- 580
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884524 1014 vtiasqLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1091
Cdd:cd14907 581 ------FRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQY 652
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
416-1133 |
2.70e-115 |
|
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: 380.66 E-value: 2.70e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14896 2 SVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASY---HPRKALNTTPHIFAIAASAYRLSQSTGQDQCILL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELqfCERKQQLTGARIYT 575
Cdd:cd14896 79 SGHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRL--HLQHGVIVGASVSH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 576 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSlnrEKLAVLKQALNVVGFS 655
Cdd:cd14896 157 YLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDA---QDFEGLLKALQGLGLC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 656 NLEVENLFVILAAILHLGDIRFTAlTEGNS---AFVSDLQLLEQVAGMLQVSTDELASALT---TDIQYfkgDMIIRRHT 729
Cdd:cd14896 234 AEELTAIWAVLAAILQLGNICFSS-SERESqevAAVSSWAEIHTAARLLQVPPERLEGAVThrvTETPY---GRVSRPLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 730 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 809
Cdd:cd14896 310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDAT--IGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 810 LFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFpkkLQSLLESSNTNAVYS----P 885
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIPQPPRES-CLDLLVDQPHSLLSILDDQTWLSQATDHTF---LQKCHYHHGDHPSYAkpqlP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 886 LKdgngnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkf 965
Cdd:cd14896 464 LP-------------VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYG----------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 966 rghksallskkmtassiigenknylelskllkkkgtstflqrLERGDPvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPN 1045
Cdd:cd14896 520 ------------------------------------------LGQGKP-TLASRFQQSLGDLTARLGRSHVYFIHCLNPN 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADtflREKKEHLAAERCRLVLQQckLQG--- 1122
Cdd:cd14896 557 PGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS---ERQEALSDRERCGAILSQ--VLGaes 631
|
730
....*....|...
gi 1622884524 1123 --WQMGVRKVFLK 1133
Cdd:cd14896 632 plYHLGATKVLLK 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
416-1133 |
7.70e-115 |
|
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: 380.28 E-value: 7.70e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRP---- 490
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLY---HGTTAGELPPHVFAIADHAYTQLIQSGVLdpsn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 491 QCFILSGERGSGKSEASKQIIRHLTcRAASSRA-------------------MLDSRFKHVMCILEAFGHAKTTLNDLSS 551
Cdd:cd14890 79 QSIIISGESGAGKTEATKIIMQYLA-RITSGFAqgasgegeaaseaieqtlgSLEDRVLSSNPLLESFGNAKTLRNDNSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 552 CFIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQtmQDDVS 631
Cdd:cd14890 158 RFGKFIEIQF-DHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRG--ECSSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 632 TGERslNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG-NSAFVSDLQLLEQVAGMLQVSTDELAS 710
Cdd:cd14890 235 PSCD--DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTtVLEDATTLQSLKLAAELLGVNEDALEK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 711 ALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEF 790
Cdd:cd14890 313 ALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGF----IGVLDIYGFEKFEWNTF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 791 EQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQN-GVLDFFFQKPSG----FLTLLDeesqmIWSMESN 865
Cdd:cd14890 389 EQLCINYANEKLQRHFNQHMFEVEQVEYSNEGI--DWQYITFNDNqACLELIEGKVNGkpgiFITLDD-----CWRFKGE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 866 FP-KKLQSLLESSntnavYSPLKDGNGNVALK-----------DHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFV 933
Cdd:cd14890 462 EAnKKFVSQLHAS-----FGRKSGSGGTRRGSsqhphfvhpkfDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKEL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 934 MKTSEnvvinhlfqsklsqtgslvsaypsfkfrghksallskkmtaSSIigenknylelskllkkkgtstflqrleRGdp 1013
Cdd:cd14890 537 IKQSR-----------------------------------------RSI---------------------------RE-- 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1014 VTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKP 1093
Cdd:cd14890 547 VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQV 626
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1622884524 1094 LADTflREKKEHLAAERCRLvLQQCKLQgWQMGVRKVFLK 1133
Cdd:cd14890 627 LLPT--AENIEQLVAVLSKM-LGLGKAD-WQIGSSKIFLK 662
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
417-1133 |
1.24e-113 |
|
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: 376.41 E-value: 1.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFQ----EQRPQC 492
Cdd:cd14892 3 LLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATASSPPPHVFSIAERAYRAMKGvgkgQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 493 FILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVM------C------ILEAFGHAKTTLNDLSSCFIKYFELQ 560
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAhesieeCvllsnlILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 561 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVStgERSLNRE 640
Cdd:cd14892 163 Y-NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVD--GVDDATE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 641 kLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALT--EGNSAFVSDLQLLEQVAGMLQVSTDELASALTTD-IQ 717
Cdd:cd14892 240 -FKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENAddEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQtTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 718 YFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSC---LLSQDEQRSM---QTLDIGILDIFGFEEFQKNEFE 791
Cdd:cd14892 319 TARGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAChkqQTSGVTGGAAsptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 792 QLCVNMTNEKMHHYINEVLFLHEQVECVQEGVtmETAYSPGNQNG-VLDFFFQKPSGFLTLLDEesQMIWSMESNfPKKL 870
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGI--DVSAIEFQDNQdCLDLIQKKPLGLLPLLEE--QMLLKRKTT-DKQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 871 QSLLESSN--TNAVYSPLKDGNgnvalkDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSenvvinhlfqs 948
Cdd:cd14892 474 LTIYHQTHldKHPHYAKPRFEC------DE---FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS----------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 949 klsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLTDII 1028
Cdd:cd14892 534 ---------------------------------------------------------------------SKFRTQLAELM 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1029 GKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA------DTFLREK 1102
Cdd:cd14892 545 EVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvAASPDAC 624
|
730 740 750
....*....|....*....|....*....|..
gi 1622884524 1103 KEHLAAERCR-LVLQQCKLQGWQMGVRKVFLK 1133
Cdd:cd14892 625 DATTARKKCEeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
416-1133 |
4.47e-110 |
|
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: 366.41 E-value: 4.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKLcsSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14903 2 AILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKE--ELPPHVYATSVAAYNHMKRSGRNQSILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLtcrAASSRAMLDSRFK---HVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGAR 572
Cdd:cd14903 80 SGESGAGKTETTKILMNHL---ATIAGGLNDSTIKkiiEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF-DKNGTLVGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 573 IYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHrylnqTMQDDVSTGERSLNREKLAVLKQALNVV 652
Cdd:cd14903 156 CRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAY-----TGANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 653 GFSNLEVENLFVILAAILHLGDIRFTALT--EGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 730
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPndDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 731 QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVL 810
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASL--GNDAKMANH--IGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 811 FLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKpSGFLTLLDEESQMIWSMESNFPKKLQSLLEsSNTNAVYSPlkdgn 890
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDFADNQD-VLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHK-DEQDVIEFP----- 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 891 gnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKS 970
Cdd:cd14903 459 -----RTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 971 ALLSKkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLP 1050
Cdd:cd14903 534 ALTTT---------------------------------------TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSP 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1051 DTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYkplaDTFLREKKEHL--AAERCRLVLQQCKLQG---WQM 1125
Cdd:cd14903 575 TELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKF----WLFLPEGRNTDvpVAERCEALMKKLKLESpeqYQM 650
|
....*...
gi 1622884524 1126 GVRKVFLK 1133
Cdd:cd14903 651 GLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
415-1133 |
1.90e-107 |
|
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: 358.48 E-value: 1.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCF 493
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSY---QGKSLGTLPPHVFAIADKAYRDMKVLKQSQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 494 ILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARI 573
Cdd:cd01382 78 IVSGESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHF-NEKSSVVGGFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 574 YTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLhlnnlcahryLNQTMQDDVstgerslnrEKLAVLKQALNVVG 653
Cdd:cd01382 157 SHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL----------LKDPLLDDV---------GDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 654 FSNLEVENLFVILAAILHLGDIRFTALTEGNSA----FVSDLQLLEQVAGMLQVSTDELASALTTDIQY-----FKGDMI 724
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgcnvKPKSEQSLEYAAELLGLDQDELRVSLTTRVMQttrggAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 725 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQdeqRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 804
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE---TSSYF--IGVLDIAGFEYFEVNSFEQFCINYCNEKLQQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 805 YINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFpkklqsllessnTNAVYS 884
Cdd:cd01382 373 FFNERILKEEQELYEKEGLGVKEVEYVDNQD-CIDLIEAKLVGILDLLDEESKLPKPSDQHF------------TSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 885 PLKDgNGNVA------LKDHGT-----AFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 953
Cdd:cd01382 440 KHKN-HFRLSiprkskLKIHRNlrddeGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNN 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 954 GSLVSAypsfkfrghksallSKKMTASSiigenknylelskllkkkgtstflqrlergdpvtIASQLRKSLTDIIGKLQK 1033
Cdd:cd01382 519 KDSKQK--------------AGKLSFIS----------------------------------VGNKFKTQLNLLMDKLRS 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1034 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKpladTFLREKKEHLAAER-CR 1112
Cdd:cd01382 551 TGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYK----KYLPPKLARLDPRLfCK 626
|
730 740
....*....|....*....|...
gi 1622884524 1113 LVLQQCKLQG--WQMGVRKVFLK 1133
Cdd:cd01382 627 ALFKALGLNEndFKFGLTKVFFR 649
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
416-1133 |
9.83e-107 |
|
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: 358.50 E-value: 9.83e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvsQLY----FSSSGKLCSSLPPHLFSCVERAF-------HQL 484
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYdlhkYREEMPGWTALPPHVFSIAEGAYrslrrrlHEP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 485 FQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMC---------ILEAFGHAKTTLNDLSSCFIK 555
Cdd:cd14895 75 GASKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISgsellsanpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 556 Y----FELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAH--RYLNQTM--- 626
Cdd:cd14895 155 FvrmfFEGHELDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQefQYISGGQcyq 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 627 -QDDVStgerslNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN---------------SAFVSD 690
Cdd:cd14895 235 rNDGVR------DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 691 L---QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlSQDEQR 767
Cdd:cd14895 309 LtvqQHLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS-PQRQFA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 768 SMQTLD--------IGILDIFGFEEFQKNEFEQLCVNMTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNqNGVL 838
Cdd:cd14895 388 LNPNKAankdttpcIAVLDIFGFEEFEVNQFEQFCINYANEKLqYQFIQDIL-LTEQQAHIEEGIKWNAVDYEDN-SVCL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 839 DFFFQKPSGFLTLLDEESQMIWSMESNFPKKL-QSLLESSNTNAVYSPLKDgngnvalkdhgTAFTIMHYAGRVMYDVVG 917
Cdd:cd14895 466 EMLEQRPSGIFSLLDEECVVPKGSDAGFARKLyQRLQEHSNFSASRTDQAD-----------VAFQIHHYAGAVRYQAEG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 918 AIEKNKDSLSQNLLFVMKTSENVVINHLFQS-KLSQTGSLVSAYPsfKFRGHKSALLSkkmtassiigenknylelskll 996
Cdd:cd14895 535 FCEKNKDQPNAELFSVLGKTSDAHLRELFEFfKASESAELSLGQP--KLRRRSSVLSS---------------------- 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 997 kkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRY 1076
Cdd:cd14895 591 -----------------VGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQ 653
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622884524 1077 GYPVRLSFSDFLSRYKPLADTflREKKEHLAAErcrlVLQQCKLQGWQMGVRKVFLK 1133
Cdd:cd14895 654 SYPVRMKHADFVKQYRLLVAA--KNASDATASA----LIETLKVDHAELGKTRVFLR 704
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
416-1132 |
1.63e-106 |
|
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: 356.02 E-value: 1.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGK---LCSSLPPHLFSCVERAFHQLFQEQRP-- 490
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYYEHGERraaGERKLPPHVYAVADKAFRAMLFASRGqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 491 --QCFILSGERGSGKSEASKQIIRHLTC--------RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQ 560
Cdd:cd14901 82 cdQSILVSGESGAGKTETTKIIMNYLASvssatthgQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 561 FcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGerSLNRE 640
Cdd:cd14901 162 F-ASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDG--VDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 641 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF-VSDLQLLEQVAGMLQVSTDELASALTTDIQYF 719
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFsMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 720 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTN 799
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASRF--IGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 800 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLeSSNT 879
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDA-CVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLL-AKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 880 NAVYSPLKDGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVInhlfqsklsqtgslvsa 959
Cdd:cd14901 475 SFSVSKLQQGKRQ---------FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL----------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 960 ypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdPVTIASQLRKSLTDIIGKLQKCTPHFI 1039
Cdd:cd14901 529 -----------------------------------------------------SSTVVAKFKVQLSSLLEVLNATEPHFI 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1040 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTfLREKKEHL--AAERCRLVLQQ 1117
Cdd:cd14901 556 RCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPD-GASDTWKVneLAERLMSQLQH 634
|
730 740
....*....|....*....|
gi 1622884524 1118 CKLQG-----WQMGVRKVFL 1132
Cdd:cd14901 635 SELNIehlppFQVGKTKVFL 654
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
416-1091 |
3.14e-104 |
|
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: 349.24 E-value: 3.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcsSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRD---KLQPHVYATSTAAYKHMLTNEMNQSIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIY 574
Cdd:cd14904 79 VSGESGAGKTETTKIVMNHLASVAGGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQF-DGRGKLIGAKCE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 575 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGersLNREKL-AVLKQALNVVG 653
Cdd:cd14904 158 TYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPG---LDDAKLfASTQKSLSLIG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 654 FSNLEVENLFVILAAILHLGDIRFTALTEGNSAfVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIA 733
Cdd:cd14904 235 LDNDAQRTLFKILSGVLHLGEVMFDKSDENGSR-ISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 734 EFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLH 813
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQ---IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 814 EQVECVQEGVTMETAYSPGNQnGVLDFFFQKpSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntnavysplKDGNGNV 893
Cdd:cd14904 391 VEEEYIREGLQWDHIEYQDNQ-GIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQT----------KKDNESI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 894 AL-KDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvSAYPSfkfrghksal 972
Cdd:cd14904 459 DFpKVKRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---------SEAPS---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 973 lSKKMTASsiiGENKNylelskllkkkgtstflqrlergDPVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDT 1052
Cdd:cd14904 520 -ETKEGKS---GKGTK-----------------------APKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTE 572
|
650 660 670
....*....|....*....|....*....|....*....
gi 1622884524 1053 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1091
Cdd:cd14904 573 FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY 611
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
416-1101 |
1.77e-99 |
|
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: 337.72 E-value: 1.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVsqLYFSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLI--LNEYKDINQNKSPIPHIYAVALRAYQSMVSEKKNQSII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASSRAML-------DSRFKHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCER 564
Cdd:cd14906 80 ISGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnNSIEKDILTsnpILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 565 KQQLTGARIYTYLLEKSRLVSQP-LGQSNFLIFSLLMDGLSAEEKHGLHL-NNLCAHRYLN-----------QTMQDDVS 631
Cdd:cd14906 160 DGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLDarddvissfksQSSNKNSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 632 TGERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNS-AFVSD--LQLLEQVAGMLQVSTDEL 708
Cdd:cd14906 240 HNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKyAYQKDkvTASLESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 709 ASALTTdiQYFK----GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQ-------TLDIGIL 777
Cdd:cd14906 320 KQALLN--RNLKaggrGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDLAggsnkknNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 778 DIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQ 857
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKE-CIELIEKKSDGILSLLDDECI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 858 MiwsmesnfPK-KLQSLLES-----SNTNAVYS-PLKDGngnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNL 930
Cdd:cd14906 477 M--------PKgSEQSLLEKynkqyHNTNQYYQrTLAKG-----------TLGIKHFAGDVTYQTDGWLEKNRDSLYSDV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 931 LFVMKTSENVVINHLFQSKLSQTGSlvsaypsfkfrghksalLSKKMTASsiigenknylelskllkkkgtstflqrler 1010
Cdd:cd14906 538 EDLLLASSNFLKKSLFQQQITSTTN-----------------TTKKQTQS------------------------------ 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1011 gdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSR 1090
Cdd:cd14906 571 ---NTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSR 647
|
730
....*....|.
gi 1622884524 1091 YKPLADTFLRE 1101
Cdd:cd14906 648 YKCIVDMYNRK 658
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
412-1136 |
8.70e-97 |
|
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: 327.58 E-value: 8.70e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 412 LNDGSLLYEIQKRFGNNQIYTFIGD-ILLLVNPYKELPIYS--SM---VSQLYFSSSGKLcSSLPPHLFSCVERAFHQLF 485
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSdaSLgeyGSEYYDTTSGSK-EPLPPHAYDLAARAYLRMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 486 QEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSR--AMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCE 563
Cdd:cd14879 80 RRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkgTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 564 RKQqLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLA 643
Cdd:cd14879 160 RGR-LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGCHPLPLGPGSDDAEGFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 644 VLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 721
Cdd:cd14879 239 ELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGeeSAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKLVRK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 722 DmiirRHTI----QIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQtldIGILDIFGFEEF---QKNEFEQLC 794
Cdd:cd14879 319 E----LCTVfldpEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATF---ISLLDFPGFQNRsstGGNSLDQFC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 795 VNMTNEKMHHYINEVLFLHEQVECVQEGVTM-ETAYsPGNQnGVLDFFFQKPSGFLTLLDEESqmiwsmeSNFPKKL-QS 872
Cdd:cd14879 392 VNFANERLHNYVLRSFFERKAEELEAEGVSVpATSY-FDNS-DCVRLLRGKPGGLLGILDDQT-------RRMPKKTdEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 873 LLES-SNTNAVYSPLKDGNGNVALKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktsenvvinhlfqskls 951
Cdd:cd14879 463 MLEAlRKRFGNHSSFIAVGNFATRSGSAS-FTVNHYAGEVTYSVEGFLERNGDVLS------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 952 qtGSLVSAypsfkFRGhksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiASQLRKSLTDIIGKL 1031
Cdd:cd14879 518 --PDFVNL-----LRG-------------------------------------------------ATQLNAALSELLDTL 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1032 QKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLadtfLREKKEHLAAERC 1111
Cdd:cd14879 542 DRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKST----LRGSAAERIRQCA 617
|
730 740
....*....|....*....|....*..
gi 1622884524 1112 RLVLQQCKLQGWqMGVRKVFLKY--WH 1136
Cdd:cd14879 618 RANGWWEGRDYV-LGNTKVFLSYaaWR 643
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
416-1115 |
9.76e-95 |
|
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: 323.77 E-value: 9.76e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-----FSSSGKLCSSLPPHLFSCVERAFHQLFQEQR 489
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtSTSPVSQLSELPPHVFAIGGKAFGGLLKPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 490 P-QCFILSGERGSGKSEASKQIIRHLTC---------RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:cd14902 82 RnQSILVSGESGSGKTESTKFLMQFLTSvgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 560 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ---TMQDDVSTGERS 636
Cdd:cd14902 162 QF-GANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 637 LNREKLAVlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF-VSDLQL--LEQVAGMLQVSTDELASALT 713
Cdd:cd14902 241 AQLYVETV--RAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATaVTAASRfhLAKCAELMGVDVDKLETLLS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 714 TDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLV----NTMN---SCLLSQDEQRSMQTldIGILDIFGFEEFQ 786
Cdd:cd14902 319 SREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVrrlsDEINyfdSAVSISDEDEELAT--IGILDIFGFESLN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 787 KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsmesnf 866
Cdd:cd14902 397 RNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAA-CLALFDDKSNGLFSLLDQECLM-------- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 867 PKKLQsllESSNTNAVYSPLKDGNgnvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVInhlf 946
Cdd:cd14902 468 PKGSN---QALSTKFYRYHGGLGQ-----------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVV---- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 947 qsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKnylelskllkkkgtstflQRLERGDPVTIAS---QLRKS 1023
Cdd:cd14902 530 -----------------------VAIGADENRDSPGADNGA------------------AGRRRYSMLRAPSvsaQFKSQ 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1024 LTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL------ADT 1097
Cdd:cd14902 569 LDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFkcflstRDR 648
|
730
....*....|....*...
gi 1622884524 1098 FLREKKEHLAAERCRLVL 1115
Cdd:cd14902 649 AAKMNNHDLAQALVTVLM 666
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
417-1095 |
2.22e-94 |
|
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: 320.45 E-value: 2.22e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 417 LLYEIQKRFG--NNQIYTFIGDILLLVNPYKELPiySSMVSqLYFSSSGKLCsslPPHLFSCVERAFHQLF---QEQRPQ 491
Cdd:cd14891 3 ILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP--EPDKS-DYINTPLDPC---PPHPYAIAEMAYQQMClgsGRMQNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 492 CFILSGERGSGKSEASKQIIRHLTCRAASSRAM------------------LDSRFKHVMCILEAFGHAKTTLNDLSSCF 553
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFLTTRAVGGKKAsgqdieqsskkrklsvtsLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 554 IKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqdDVSTG 633
Cdd:cd14891 157 GKFMKLQFTKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQS---GCVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 634 ERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRF----TALTEGNSAFVSDLQLLEQVAGMLQVSTDELA 709
Cdd:cd14891 234 DNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 710 SALTT-DIQYFKGDMIIRRhTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQ-K 787
Cdd:cd14891 314 KVITQrEIVTRGETFTIKR-NAREAVYSRDAIAKSIYERLFLWIVQQINTSL----GHDPDPLPYIGVLDIFGFESFEtK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 788 NEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwSMESNfp 867
Cdd:cd14891 389 NDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRE-CLDLIASKPNGILPLLDNEARN--PNPSD-- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 868 KKLQSLLESSNTNAVYSPLKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLlfvmktsENVVinhlfq 947
Cdd:cd14891 464 AKLNETLHKTHKRHPCFPRPHP------KDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDF-------EDLL------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 948 sklsqtgslvsaypsfkfrgHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrKSLTDi 1027
Cdd:cd14891 525 --------------------ASSAKFSDQM--------------------------------------------QELVD- 539
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884524 1028 igKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1095
Cdd:cd14891 540 --TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVL 605
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
416-1103 |
5.61e-94 |
|
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: 320.70 E-value: 5.61e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFS---------SSGKlcsSLPPHLFSCVERAFHQLFQ 486
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQegllrsqgiESPQ---ALGPHVFAIADRSYRQMMS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 487 EQRP-QCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDS-----------RFKHVMCILEAFGHAKTTLNDLSSCFI 554
Cdd:cd14908 79 EIRAsQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEgeelgklsimdRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 555 KYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAH-----RYLNQTMQDD 629
Cdd:cd14908 159 KFIELGF-NRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGglqlpNEFHYTGQGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 630 VSTGERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF---VSDLQLLEQVAGMLQVSTD 706
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEiaeEGNEKCLARVAKLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 707 ELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLL--SQDEQRSmqtlDIGILDIFGFEE 784
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRS----SVGVLDIFGFEC 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 785 FQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQM-IWSME 863
Cdd:cd14908 394 FAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQD-CLDTIQAKKKGILTMLDDECRLgIRGSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 864 SNFPKKLqsllessntNAVYSPLKDGNGNVALKDHGTA-------FTIMHYAGRVMYDV-VGAIEKNKDSLSqnllfvmK 935
Cdd:cd14908 473 ANYASRL---------YETYLPEKNQTHSENTRFEATSiqktkliFAVRHFAGQVQYTVeTTFCEKNKDEIP-------L 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 936 TSENvvinhLFQSklsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvt 1015
Cdd:cd14908 537 TADS-----LFES------------------------------------------------------------------- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1016 iASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1095
Cdd:cd14908 545 -GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLL 623
|
....*...
gi 1622884524 1096 DTFLREKK 1103
Cdd:cd14908 624 PLIPEVVL 631
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
416-1133 |
1.30e-93 |
|
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: 318.84 E-value: 1.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14929 2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY---KGKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRA-----MLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQqLTG 570
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESkkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM-LSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 571 ARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDG--------LSAEEKHGLHLnnlCAHRYLNQTMQDDVstgerslnrEKL 642
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGkkelrdllLVSANPSDFHF---CSCGAVAVESLDDA---------EEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 643 AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 722
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 723 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKM 802
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVL---DAKLSRQFF-IGILDITGFEILDYNSLEQLCINFTNEKL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 803 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSMESNFPKKLqslLESSNTNAV 882
Cdd:cd14929 382 QQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKL---FDNHFGKSV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 883 Y--SPLKDGngnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqTGSlvsay 960
Cdd:cd14929 458 HfqKPKPDK------KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIS-TDS----- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 961 psfkfrghksallskkmtaSSIIGENKNylelskllkKKGTSTFLqrlergdpvtIASQLRKSLTDIIGKLQKCTPHFIH 1040
Cdd:cd14929 526 -------------------AIQFGEKKR---------KKGASFQT----------VASLHKENLNKLMTNLKSTAPHFVR 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1041 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-ADTFLREK--KEHLAAERCRLVLQQ 1117
Cdd:cd14929 568 CINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILnPRTFPKSKfvSSRKAAEELLGSLEI 647
|
730
....*....|....*.
gi 1622884524 1118 CKLQgWQMGVRKVFLK 1133
Cdd:cd14929 648 DHTQ-YRFGITKVFFK 662
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
404-1171 |
1.21e-91 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 317.74 E-value: 1.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 404 DDLATLSELNDGSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQ 483
Cdd:PTZ00014 99 GDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDS--DKLPPHVFTTARRALEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 484 LFQEQRPQCFILSGERGSGKSEASKQIIRHLtcrAASSRAMLDSRF-KHVMC---ILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:PTZ00014 177 LHGVKKSQTIIVSGESGAGKTEATKQIMRYF---ASSKSGNMDLKIqNAIMAanpVLEAFGNAKTIRNNNSSRFGRFMQL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 560 QFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ-----DDVSTGE 634
Cdd:PTZ00014 254 QL-GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLdvpgiDDVKDFE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 635 RSLnreklavlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG---NSAFVSD--LQLLEQVAGMLQVSTDELA 709
Cdd:PTZ00014 333 EVM---------ESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltDAAAISDesLEVFNEACELLFLDYESLK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 710 SALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNE 789
Cdd:PTZ00014 404 KELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVF----IGMLDIFGFEVFKNNS 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 790 FEQLCVNMTNEKMH-HYINeVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMESNFPK 868
Cdd:PTZ00014 480 LEQLFINITNEMLQkNFVD-IVFERESKLYKDEGISTEELEYTSNES-VIDLLCGKGKSVLSILEDQCLAPGGTDEKFVS 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 869 KLQSLLESsntNAVYSPLK-DGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ 947
Cdd:PTZ00014 558 SCNTNLKN---NPKYKPAKvDSNKN---------FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFE 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 948 SKLSQTGSlvsaypsfkfrghksalLSKKMtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDI 1027
Cdd:PTZ00014 626 GVEVEKGK-----------------LAKGQ-------------------------------------LIGSQFLNQLDSL 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1028 IGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEHLA 1107
Cdd:PTZ00014 652 MSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYL-DLAVSNDSSLDP 730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884524 1108 AERCRLVLQQCKL--QGWQMGVRKVFLKYWHADQLNdlclQLQRKIITCQK--------VIRGFLARQHLLQKI 1171
Cdd:PTZ00014 731 KEKAEKLLERSGLpkDSYAIGKTMVFLKKDAAKELT----QIQREKLAAWEplvsvleaLILKIKKKRKVRKNI 800
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
416-1122 |
2.39e-89 |
|
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: 305.31 E-value: 2.39e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS--------LPPHLFSCVERAFHQ--- 483
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYLLSFEARSSStrnkgsdpMPPHIYQVAGEAYKAmml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 484 -LFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCI----------LEAFGHAKTTLNDLSSC 552
Cdd:cd14900 82 gLNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIaakvlqtnilLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 553 FIKYFELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGlSAEEKHGLHLnnlcahryLNQTMqddvst 632
Cdd:cd14900 162 FGKFIKLHF-TSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIG-ASEAARKRDM--------YRRVM------ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 633 gerslnreklavlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGN--SAFVSDL-----QLLEQVAGMLQVST 705
Cdd:cd14900 226 --------------DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrlGQLKSDLapssiWSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 706 DELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLD-IGILDIFGFEE 784
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHfIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 785 FQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMIWSMES 864
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQD-CVNLISQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 865 NFPKKLQSLLEsSNTNAVYSPLKDGNGnvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvinH 944
Cdd:cd14900 451 TLASKLYRACG-SHPRFSASRIQRARG---------LFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------D 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 945 LFQSKLsqtgslvsaypsfkfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpvtiasQLRKSL 1024
Cdd:cd14900 509 LFVYGL--------------------------------------------------------------------QFKEQL 520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1025 TDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLAdtflREKKE 1104
Cdd:cd14900 521 TTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLA----RAKNR 596
|
730
....*....|....*...
gi 1622884524 1105 HLAAERCRLVLQQCKLQG 1122
Cdd:cd14900 597 LLAKKQGTSLPDTDSDHG 614
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
416-1133 |
3.84e-89 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 306.14 E-value: 3.84e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY---KGIKRHEVPPHVFAITDSAYRNMLGDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASS-----------------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFE 558
Cdd:cd14911 79 TGESGAGKTENTKKVIQFLAYVAASKpkgsgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 559 LQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ-----DDVSTG 633
Cdd:cd14911 159 INF-DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLpvpgvDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 634 ERSLNreklavlkqALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALT 713
Cdd:cd14911 238 QATVK---------SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 714 TDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQL 793
Cdd:cd14911 309 TPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL---DRTKRQGASFIGILDMAGFEIFELNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 794 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSl 873
Cdd:cd14911 386 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDKLVS- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 874 LESSNTNAVYSPLKdgngnvalkdhGTA-FTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsq 952
Cdd:cd14911 464 AHSMHPKFMKTDFR-----------GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD---- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 953 tgslvsaypsfkfrghksallskkmtaSSIIGenknylelsKLLKKKGTSTFLQRLERGDPVTIASQLRKSLTDIIGKLQ 1032
Cdd:cd14911 529 ---------------------------AEIVG---------MAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLR 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1033 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT-----FLREKKEhla 1107
Cdd:cd14911 573 NTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNvipkgFMDGKKA--- 649
|
730 740
....*....|....*....|....*...
gi 1622884524 1108 aerCRLVLQQCKLQG--WQMGVRKVFLK 1133
Cdd:cd14911 650 ---CEKMIQALELDSnlYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
416-1133 |
6.93e-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: 305.40 E-value: 6.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY---RGKKRHEMPPHIYAISESAYRCMLQDREDQSILC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRAM--------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQ 567
Cdd:cd14920 79 TGESGAGKTENTKKVIQYLAHVASSHKGRkdhnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF-DVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 568 LTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ-----TMQDDvstgerslnREKL 642
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNgyipiPGQQD---------KDNF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 643 AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 722
Cdd:cd14920 229 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 723 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 802
Cdd:cd14920 309 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 803 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSMESNFPKKLQSllESSNTN 880
Cdd:cd14920 386 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 881 AVYSPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTG-SLVSA 959
Cdd:cd14920 464 KFQKPRQ-------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGlDQVTG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 960 YPSFKFrghKSALLSKKmtassiigenknylelskllkkkgtstflqrlerGDPVTIASQLRKSLTDIIGKLQKCTPHFI 1039
Cdd:cd14920 536 MTETAF---GSAYKTKK----------------------------------GMFRTVGQLYKESLTKLMATLRNTNPNFV 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1040 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA-----DTFLREKkehlaaERCRLV 1114
Cdd:cd14920 579 RCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpnaipKGFMDGK------QACERM 652
|
730 740
....*....|....*....|.
gi 1622884524 1115 LQQCKLQG--WQMGVRKVFLK 1133
Cdd:cd14920 653 IRALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
424-1133 |
1.10e-88 |
|
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: 304.22 E-value: 1.10e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 424 RFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGK 503
Cdd:cd14876 10 RYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPD--LTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 504 SEASKQIIRHLtcrAASSRAMLDSRF-KHVMC---ILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQLTGArIYTYLLE 579
Cdd:cd14876 88 TEATKQIMRYF---ASAKSGNMDLRIqTAIMAanpVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS-VVAFLLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 580 KSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQ-----DDVSTGERslnreklavLKQALNVVGF 654
Cdd:cd14876 164 KSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLdvpgiDDVADFEE---------VLESLKSMGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 655 SNLEVENLFVILAAILHLGDIRFTALTEG---NSAFVS--DLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 729
Cdd:cd14876 235 TEEQIDTVFSIVSGVLLLGNVKITGKTEQgvdDAAAISneSLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 730 IQIAEFFRDLLAKSLYSRLFSFLVNTMNScllSQDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINe 808
Cdd:cd14876 315 KDDAEMLKLSLAKAMYDKLFLWIIRNLNS---TIEPPGGFKNF-MGMLDIFGFEVFKNNSLEQLFINITNEMLQkNFID- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 809 VLFLHEQVECVQEGV-TMETAYSPGNQngVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESsntNAVYSPLK 887
Cdd:cd14876 390 IVFERESKLYKDEGIpTAELEYTSNAE--VIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKS---NGKFKPAK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 888 -DGNGNvalkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsaypsfkfr 966
Cdd:cd14876 465 vDSNIN---------FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG------------ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 967 ghksallskKMTASSIIGenknylelskllkkkgtstflqrlergdpvtiaSQLRKSLTDIIGKLQKCTPHFIHCIRPNN 1046
Cdd:cd14876 524 ---------KIAKGSLIG---------------------------------SQFLKQLESLMGLINSTEPHFIRCIKPNE 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1047 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLaDTFLREKKEHLAAERCRLVLQQCKL--QGWQ 1124
Cdd:cd14876 562 TKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL-DLGIANDKSLDPKVAALKLLESSGLseDEYA 640
|
....*....
gi 1622884524 1125 MGVRKVFLK 1133
Cdd:cd14876 641 IGKTMVFLK 649
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
416-1133 |
1.42e-88 |
|
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: 304.57 E-value: 1.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY---KGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRAM--------------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQF 561
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAIVAALGDGPgkkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 562 CErKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLN-NLCAHRYLNQ--TMQDDVSTGErsln 638
Cdd:cd14927 159 GP-TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQgvTTVDNMDDGE---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 639 reKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 718
Cdd:cd14927 234 --ELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 719 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMT 798
Cdd:cd14927 312 VGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFF----IGVLDIAGFEIFEFNSFEQLCINFT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 799 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLES 876
Cdd:cd14927 388 NEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACID-LIEKPLGILSILEEECMFPKASDASFKAKLydNHLGKS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 877 SNTNavySPLKDGNgnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTgsl 956
Cdd:cd14927 467 PNFQ---KPRPDKK-----RKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSD--- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 957 vSAYPsfkfrgHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpvTIASQLRK-SLTDIIGKLQKCT 1035
Cdd:cd14927 536 -STED------PKSGVKEKRKKAASF--------------------------------QTVSQLHKeNLNKLMTNLRATQ 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1036 PHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL------ADTFLREKKehlAAE 1109
Cdd:cd14927 577 PHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILnpsaipDDKFVDSRK---ATE 653
|
730 740
....*....|....*....|....
gi 1622884524 1110 RCRLVLQQCKLQgWQMGVRKVFLK 1133
Cdd:cd14927 654 KLLGSLDIDHTQ-YQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
416-1133 |
3.62e-88 |
|
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: 303.30 E-value: 3.62e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14909 2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMY---RGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASS--------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQ 567
Cdd:cd14909 79 TGESGAGKTENTKKVIAYFATVGASKktdeaaksKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP-TGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 568 LTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHL-NNLCAHRYLNQ--TMQDDVSTGErslnreKLAV 644
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQgkVTVPNVDDGE------EFSL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 645 LKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 724
Cdd:cd14909 232 TDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 725 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 804
Cdd:cd14909 312 TQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETL---DTQQKRQHF-IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 805 YINEVLFLHEQVECVQEGVtmETAYspgnqngvLDF---------FFQKPSGFLTLLDEESQMIWSMESNFPKKLQSL-L 874
Cdd:cd14909 388 FFNHHMFVLEQEEYKREGI--DWAF--------IDFgmdllacidLIEKPMGILSILEEESMFPKATDQTFSEKLTNThL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 875 ESSNTNAVYSPLKDGNgnvalkdHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTG 954
Cdd:cd14909 458 GKSAPFQKPKPPKPGQ-------QAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSG 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 955 SLVSAYPSfkfRGHKSALLSkkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKC 1034
Cdd:cd14909 531 GGEQAKGG---RGKKGGGFA----------------------------------------TVSSAYKEQLNSLMTTLRST 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1035 TPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLR-EKKEHLAAERCrl 1113
Cdd:cd14909 568 QPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQgEEDPKKAAEII-- 645
|
730 740
....*....|....*....|..
gi 1622884524 1114 vLQQCKL--QGWQMGVRKVFLK 1133
Cdd:cd14909 646 -LESIALdpDQYRLGHTKVFFR 666
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
415-1133 |
1.73e-86 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 298.47 E-value: 1.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDS--------RFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 566
Cdd:cd14921 78 CTGESGAGKTENTKKVIQYLAVVASSHKGKKDTsitgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 567 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLavlk 646
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETL---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 647 QALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 726
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 806
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 807 NEVLFLHEQVECVQEGV-------------TMETAYSPGNqngvldfffqkPSGFLTLLDEESQMIWSMESNFPKKLQSl 873
Cdd:cd14921 390 NHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKSFVEKLCT- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 874 lESSNTNAVYSPLKdgngnvaLKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQT 953
Cdd:cd14921 458 -EQGNHPKFQKPKQ-------LKDK-TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIV 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 954 GSLVSAypsfkfrghksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQK 1033
Cdd:cd14921 529 GLDQMA----------------KMTESSLPSASKT--------------------KKGMFRTVGQLYKEQLGKLMTTLRN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1034 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRL 1113
Cdd:cd14921 573 TTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACIL 651
|
730 740
....*....|....*....|..
gi 1622884524 1114 VLQQCKLQG--WQMGVRKVFLK 1133
Cdd:cd14921 652 MIKALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
416-1133 |
2.46e-86 |
|
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: 297.88 E-value: 2.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGN-NQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLF-QEQRPQCF 493
Cdd:cd14875 2 TLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDP--RLLPPHIWQVAHKAFNAIFvQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 494 ILSGERGSGKSEASKQII------RHLTCRAASSRAM---LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCER 564
Cdd:cd14875 80 VISGESGSGKTENAKMLIaylgqlSYMHSSNTSQRSIadkIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 565 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGL-HLNNLCAHRYLN--QTMQDDVSTGERSLNREK 641
Cdd:cd14875 160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNggNTFVRRGVDGKTLDDAHE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 642 LAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTAlTEGNSAFVSDLQLLEQVAGMLQVSTDELASALttdiqyfkg 721
Cdd:cd14875 240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFES-DQNDKAQIADETPFLTACRLLQLDPAKLRECF--------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 722 dmIIRRHT--IQI------AEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTldIGILDIFGFEEFQKNEFEQL 793
Cdd:cd14875 310 --LVKSKTslVTIlankteAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGCKY--IGLLDIFGFENFTRNSFEQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 794 CVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSl 873
Cdd:cd14875 386 CINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECV-NMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWD- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 874 lESSNTNAVYSPLKDGNGNvalkdhgtAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqt 953
Cdd:cd14875 464 -QWANKSPYFVLPKSTIPN--------QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIR---------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 954 gSLVSAYPSFKFRGHksallskkmtassiigenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQK 1033
Cdd:cd14875 525 -TLLSTEKGLARRKQ----------------------------------------------TVAIRFQRQLTDLRTELES 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1034 CTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFlSRY------KPLADTFlreKKEHLA 1107
Cdd:cd14875 558 TETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF-CRYfylimpRSTASLF---KQEKYS 633
|
730 740 750
....*....|....*....|....*....|.
gi 1622884524 1108 AERCRLVLQQCKLQGWQ-----MGVRKVFLK 1133
Cdd:cd14875 634 EAAKDFLAYYQRLYGWAkpnyaVGKTKVFLR 664
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
415-1133 |
1.15e-85 |
|
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: 295.78 E-value: 1.15e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMY---KGKKRTEMPPHLFSISDNAYHDMLMDRENQSML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTC------RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErKQQL 568
Cdd:cd14934 78 ITGESGAGKTENTKKVIQYFANiggtgkQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT-TGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 569 TGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHL-NNLCAHRYLNQ--TMQDDVSTGErslnreKLAVL 645
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQgvTVVDNMDDGE------ELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 646 KQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 725
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 726 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTL----DTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNtnavY 883
Cdd:cd14934 387 FNHHMFVLEQEEYKREGIEWVFIDFGLDLQACID-LLEKPMGIFSILEEQCVFPKATDATFKAALydNHLGKSSN----F 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 884 SPLKDGNGnvalKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSlvsaypsf 963
Cdd:cd14934 462 LKPKGGKG----KGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGS-------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 964 kfrghksallSKKMTASSIIgenknylelskllkkkgtstflqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIR 1043
Cdd:cd14934 530 ----------KKQKRGSSFM-------------------------------TVSNFYREQLNKLMTTLHSTAPHFVRCIV 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1044 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL-----ADTFLREKKehlAAErcrLVLQQC 1118
Cdd:cd14934 569 PNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLnpnviPQGFVDNKK---ASE---LLLGSI 642
|
730
....*....|....*..
gi 1622884524 1119 KLQ--GWQMGVRKVFLK 1133
Cdd:cd14934 643 DLDvnEYKIGHTKVFFR 659
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
415-1133 |
1.71e-84 |
|
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: 292.70 E-value: 1.71e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAAS------------SRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFc 562
Cdd:cd14932 78 CTGESGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 563 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLnqtmqddvSTGERSL----N 638
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFL--------SNGNVTIpgqqD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 639 REKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 718
Cdd:cd14932 229 KELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 719 FKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 798
Cdd:cd14932 309 VGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 799 NEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSMESNFPKKLQSllES 876
Cdd:cd14932 386 NEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQ--EQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 877 SNTNAVYSPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgsl 956
Cdd:cd14932 464 GNNPKFQKPKK-------LKDDAD-FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD-------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 957 vsaypsfkfrghksallskkmtASSIIGENKNYLELSKLLKKKGTSTFLQRlergdpvTIASQLRKSLTDIIGKLQKCTP 1036
Cdd:cd14932 528 ----------------------VDRIVGLDKVAGMGESLHGAFKTRKGMFR-------TVGQLYKEQLMNLMTTLRNTNP 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1037 HFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQ 1116
Cdd:cd14932 579 NFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMVK 657
|
730
....*....|....*....
gi 1622884524 1117 QCKLQG--WQMGVRKVFLK 1133
Cdd:cd14932 658 ALELDPnlYRIGQSKVFFR 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
416-1133 |
7.85e-84 |
|
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: 290.41 E-value: 7.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASS----------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERK 565
Cdd:cd14913 79 TGESGAGKTVNTKRVIQYFATIAATGdlakkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 566 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NREK 641
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITT-------NPYDYPFISQGEILVasidDAEE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 642 LAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 721
Cdd:cd14913 231 LLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 722 DMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEK 801
Cdd:cd14913 311 EYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL---DTKLPRQHF-IGVLDIAGFEIFEYNSLEQLCINFTNEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 802 MHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNt 879
Cdd:cd14913 387 LQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 880 navYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvsa 959
Cdd:cd14913 465 ---FQKPKVVKGRAE-----AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT----------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 960 ypsfkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFI 1039
Cdd:cd14913 526 -----FATADADSGKKKVAKKK-------------------GSSFQ---------TVSALFRENLNKLMSNLRTTHPHFV 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1040 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCK 1119
Cdd:cd14913 573 RCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASID 652
|
730
....*....|....*.
gi 1622884524 1120 LQ--GWQMGVRKVFLK 1133
Cdd:cd14913 653 IDhtQYKFGHTKVFFK 668
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
416-1133 |
4.71e-83 |
|
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: 287.41 E-value: 4.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGklcSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSR---SDNAPHIFSVADSAYQDMLHHEEPQHIIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLtCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLTGARIYT 575
Cdd:cd14882 79 SGESYSGKTTNARLLIKHL-CYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTF-GSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 576 YLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEK-HGLHLNNLCAHRYLnqtmQDDVSTGERSL---------NREKLAVL 645
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYL----RIPPEVPPSKLkyrrddpegNVERYKEF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 646 KQALNVVGFSNLEVENLFVILAAILHLGDIRFTaltEGN-SAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 724
Cdd:cd14882 233 EEILKDLDFNEEQLETVRKVLAAILNLGEIRFR---QNGgYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 725 IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQdeqRSM--QTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 802
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFP---RAVfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 803 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVlDFFFQKPSGFLTLLDEESQmiwSMESnfpkklqsllessnTNAV 882
Cdd:cd14882 387 QYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAV-DQLMTKPDGLFYIIDDASR---SCQD--------------QNYI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 883 YSPLKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLVSAYPS 962
Cdd:cd14882 449 MDRIKEKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--SQVRNMRTLAAT 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 963 FKFrghkSALLSKKMTAssiIGENknylelskllkKKGTstflqrlergdpvtiasqlrksltdiigklqkctpHFIHCI 1042
Cdd:cd14882 527 FRA----TSLELLKMLS---IGAN-----------SGGT-----------------------------------HFVRCI 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1043 RPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFlrEKKEHLAAERCRLVLQQCKLQG 1122
Cdd:cd14882 554 RSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDF--DETVEMTKDNCRLLLIRLKMEG 631
|
730
....*....|.
gi 1622884524 1123 WQMGVRKVFLK 1133
Cdd:cd14882 632 WAIGKTKVFLK 642
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
415-1133 |
3.78e-81 |
|
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: 282.75 E-value: 3.78e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASSRAM-----LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQQLT 569
Cdd:cd14919 78 CTGESGAGKTENTKKVIQYLAHVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 570 GARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKLavlkQAL 649
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETM----EAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 650 NVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 729
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 730 IQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 809
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 810 LFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQK--PSGFLTLLDEESQMIWSMESNFPKKlqsLLESSNTNAVYSPLK 887
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEK---VVQEQGTHPKFQKPK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 888 DgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAypsfkfrg 967
Cdd:cd14919 467 Q------LKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVA-------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 968 hksallskKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNS 1047
Cdd:cd14919 532 --------GMSETALPGAFKT--------------------RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHE 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1048 KLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQQCKLQG--WQM 1125
Cdd:cd14919 584 KKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRI 662
|
....*...
gi 1622884524 1126 GVRKVFLK 1133
Cdd:cd14919 663 GQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
415-1133 |
1.18e-80 |
|
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: 281.57 E-value: 1.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAAS------------SRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFc 562
Cdd:cd15896 78 CTGESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 563 ERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGERSLNREKL 642
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 643 avlkQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 722
Cdd:cd15896 237 ----EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 723 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 802
Cdd:cd15896 313 YVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 803 HHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSMESNFPKKLqsLLESSNTN 880
Cdd:cd15896 390 QQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKV--LQEQGTHP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 881 AVYSPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGslvsay 960
Cdd:cd15896 468 KFFKPKK-------LKDEAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVG------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 961 psfkfrghksalLSKKMTASSIIGENKNylelskllkkkgtstflqrlERGDPVTIASQLRKSLTDIIGKLQKCTPHFIH 1040
Cdd:cd15896 534 ------------LDKVSGMSEMPGAFKT--------------------RKGMFRTVGQLYKEQLSKLMATLRNTNPNFVR 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1041 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQQCKL 1120
Cdd:cd15896 582 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMIKSLEL 660
|
730
....*....|....*
gi 1622884524 1121 QG--WQMGVRKVFLK 1133
Cdd:cd15896 661 DPnlYRIGQSKVFFR 675
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
415-1092 |
2.99e-79 |
|
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: 278.52 E-value: 2.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLY-------FSSSGKLCSSLPPHLFSCVERAFHQLFQ 486
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqFGDRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 487 EQRPQCFILSGERGSGKSEASKQIIRH--LTCRAAS---------------SRAMLDSRFKHVMCILEAFGHAKTTLNDL 549
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYfaVHCGTGNnnltnsesisppaspSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 550 SSCFIKYFELQFCERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDG----LSAEEKHGLHLN-NLCAHRYLNQ 624
Cdd:cd14899 161 SSRFGKFIELRFRDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSgGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 625 TMQDDVSTGERslNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG--NSAFVSDLQLLEQVAG--- 699
Cdd:cd14899 241 SLCSKRRDGVK--DGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKgdDTVFADEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 700 -------MLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQ--------- 763
Cdd:cd14899 319 hftkaaeLLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 764 ----DEQRSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQnGVLD 839
Cdd:cd14899 399 sdvdDEEDATDF--IGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNR-ACLE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 840 FFFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTNAVYSplkdgngNVALKDHGTAFTIMHYAGRVMYDVVGAI 919
Cdd:cd14899 476 LFEHRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFR-------SAPLIQRTTQFVVAHYAGCVTYTIDGFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 920 EKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAYPSFKFRGHKSAllsKKMTASsiigenknylelskllkkk 999
Cdd:cd14899 549 AKNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRA---KSAIAA------------------- 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1000 gtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYP 1079
Cdd:cd14899 607 --------------VSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFP 672
|
730
....*....|...
gi 1622884524 1080 VRLSFSDFLSRYK 1092
Cdd:cd14899 673 VRLTHKQFLGRYR 685
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
416-1094 |
3.17e-79 |
|
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: 276.98 E-value: 3.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAA----------SSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCErK 565
Cdd:cd14917 79 TGESGAGKTVNTKRVIQYFAVIAAigdrskkdqtPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA-T 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 566 QQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NREK 641
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-------NPYDYAFISQGETTVasidDAEE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 642 LAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 721
Cdd:cd14917 231 LMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 722 DMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEK 801
Cdd:cd14917 311 EYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 802 MHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNT 879
Cdd:cd14917 387 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLfdNHLGKSNNF 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 880 NavysplKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklsqtgslvsa 959
Cdd:cd14917 466 Q------KPRNIKGKPEAH---FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN----------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 960 ypsfkFRGHKSALLSKKMTASSiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPHFI 1039
Cdd:cd14917 526 -----YAGADAPIEKGKGKAKK-------------------GSSFQ---------TVSALHRENLNKLMTNLRSTHPHFV 572
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884524 1040 HCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 1094
Cdd:cd14917 573 RCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
415-1133 |
6.09e-79 |
|
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: 276.21 E-value: 6.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 415 GSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY---RGKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASSRAM--------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 566
Cdd:cd14930 78 CTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 567 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLnqTMQDDVSTG-ERSLNREKLavl 645
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGqERELFQETL--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 646 kQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMII 725
Cdd:cd14930 232 -ESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 726 RRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd14930 311 KAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQ--KPSGFLTLLDEESQMIWSMESNFPKKLQSllESSNTNAVY 883
Cdd:cd14930 388 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQ--EQGGHPKFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 884 SPLKdgngnvaLKDHGTaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS-----KLSQTGSLVS 958
Cdd:cd14930 466 RPRH-------LRDQAD-FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGD 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 959 AYPSFKFRghksallskkmtassiigenknylelskllkkkgtstflqrleRGDPVTIASQLRKSLTDIIGKLQKCTPHF 1038
Cdd:cd14930 538 GPPGGRPR-------------------------------------------RGMFRTVGQLYKESLSRLMATLSNTNPSF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1039 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLrEKKEHLAAERCRLVLQQC 1118
Cdd:cd14930 575 VRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQAL 653
|
730
....*....|....*..
gi 1622884524 1119 KLQG--WQMGVRKVFLK 1133
Cdd:cd14930 654 ELDPnlYRVGQSKIFFR 670
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
421-1132 |
1.60e-77 |
|
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: 270.83 E-value: 1.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 421 IQKRFGNNQIYTFIGDILLLVNPYKELPiyssmvSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERG 500
Cdd:cd14881 7 LQARFYAKEFFTNVGPILLSVNPYRDVG------NPLTLTSTRS--SPLAPQLLKVVQEAVRQQSETGYPQAIILSGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 501 SGKSEASKQIIRHLTCRAA---SSRAmldsrFKHV---MCILEAFGHAKTTLNDLSSCFIKYFELQFCErkQQLTGARIY 574
Cdd:cd14881 79 SGKTYASMLLLRQLFDVAGggpETDA-----FKHLaaaFTVLRSLGSAKTATNSESSRIGHFIEVQVTD--GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 575 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAH--RYLNQtmqddvSTGERSLNREKLA--VLKQALN 650
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSPAnlRYLSH------GDTRQNEAEDAARfqAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 651 VVGFSNLEVENlfvILAAILHLGDIRFTALTEGNSAFVSDLQLlEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTI 730
Cdd:cd14881 226 ILGIPFLDVVR---VLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 731 QIAEFFRDLLAKSLYSRLFSFLVNTMNScLLSQDEQRSMQTLD--IGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 808
Cdd:cd14881 302 NMSNMTRDALAKALYCRTVATIVRRANS-LKRLGSTLGTHATDgfIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 809 VLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESnFPKKLQslLESSNTNAVYSPlkd 888
Cdd:cd14881 381 HIFKSSIESCRDEGIQCEVEVDYVDNVPCIDLISSLRTGLLSMLDVECSPRGTAES-YVAKIK--VQHRQNPRLFEA--- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 889 gngnvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtsenvvinhlfqsklSQTGslvsaypSFKFRGH 968
Cdd:cd14881 455 ------KPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY---------------KQNC-------NFGFATH 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 969 ksallskkmtassiigenknylelskllkkkgTSTFLQRLErgdpvtiasqlrksltDIIGKLQKCTPHFIHCIRPNNSK 1048
Cdd:cd14881 507 --------------------------------TQDFHTRLD----------------NLLRTLVHARPHFVRCIRSNTTE 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1049 LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLREKKEHLAAERCRLVLQQCKLQ------- 1121
Cdd:cd14881 539 TPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILQFLEAQppsklss 618
|
730
....*....|....
gi 1622884524 1122 ---GWQMGVRKVFL 1132
Cdd:cd14881 619 vstSWALGKRHIFL 632
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
416-1133 |
5.53e-77 |
|
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: 270.45 E-value: 5.53e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASS------------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcE 563
Cdd:cd14912 79 TGESGAGKTVNTKRVIQYFATIAVTGekkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 564 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NR 639
Cdd:cd14912 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITT-------NPYDYPFVSQGEISVasidDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 640 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 719
Cdd:cd14912 231 EELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 720 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTN 799
Cdd:cd14912 311 GNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 800 EKMHHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESS 877
Cdd:cd14912 387 EKLQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 878 NtnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSklSQTGSLV 957
Cdd:cd14912 466 N----FQKPKVVKGKAE-----AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSG--AQTAEGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 958 SAYPSFKFRGHKSAllskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPH 1037
Cdd:cd14912 535 SAGGGAKKGGKKKG------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPH 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1038 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT------FLREKKehlAAERC 1111
Cdd:cd14912 576 FVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegqFIDSKK---ASEKL 652
|
730 740
....*....|....*....|..
gi 1622884524 1112 RLVLQQCKLQgWQMGVRKVFLK 1133
Cdd:cd14912 653 LASIDIDHTQ-YKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
416-1101 |
6.44e-77 |
|
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: 270.39 E-value: 6.44e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY---RGKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAA-----------SSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 564
Cdd:cd14916 79 TGESGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 565 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NRE 640
Cdd:cd14916 158 TGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTN-------NPYDYAFVSQGEVSVasidDSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 641 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 720
Cdd:cd14916 231 ELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 721 GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNE 800
Cdd:cd14916 311 NEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 801 KMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFfQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSN 878
Cdd:cd14916 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLydNHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 879 TNavysplKDGNGNVALKDHgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSqtgslVS 958
Cdd:cd14916 466 FQ------KPRNVKGKQEAH---FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYAS-----AD 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 959 AYPSFKFRGHKSAllskkmtassiigenknylelskllkkkgTSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPHF 1038
Cdd:cd14916 532 TGDSGKGKGGKKK-----------------------------GSSFQ---------TVSALHRENLNKLMTNLKTTHPHF 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884524 1039 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1101
Cdd:cd14916 574 VRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 636
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
416-1101 |
1.41e-76 |
|
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: 269.29 E-value: 1.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASS------------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcE 563
Cdd:cd14910 79 TGESGAGKTVNTKRVIQYFATIAVTGekkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 564 RKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NR 639
Cdd:cd14910 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITT-------NPYDYAFVSQGEITVpsidDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 640 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 719
Cdd:cd14910 231 EELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 720 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTN 799
Cdd:cd14910 311 GNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 800 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESS 877
Cdd:cd14910 387 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 878 NtnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLV 957
Cdd:cd14910 466 N----FQKPKPAKGKVE-----AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 958 SAYPSFKFRGhksallskkmtassiigenknylelskllkkkgtSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPH 1037
Cdd:cd14910 537 GGKKGGKKKG----------------------------------SSFQ---------TVSALFRENLNKLMTNLRSTHPH 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884524 1038 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1101
Cdd:cd14910 574 FVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
416-1101 |
1.97e-75 |
|
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: 265.82 E-value: 1.97e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRA---------ASSRAM---LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCE 563
Cdd:cd14915 79 TGESGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 564 rKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NR 639
Cdd:cd14915 159 -TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITT-------NPYDFAFVSQGEITVpsidDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 640 EKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 719
Cdd:cd14915 231 EELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 720 KGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTN 799
Cdd:cd14915 311 GNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 800 EKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESS 877
Cdd:cd14915 387 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLyeQHLGKSN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 878 NtnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLfvmktsenvvinHLFQSKLSQTgslv 957
Cdd:cd14915 466 N----FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVV------------GLYQKSGMKT---- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 958 sayPSFKFRGHKSAllSKKMTASSIIGENKNylelskllkkkgtSTFLqrlergdpvTIASQLRKSLTDIIGKLQKCTPH 1037
Cdd:cd14915 521 ---LAFLFSGGQTA--EAEGGGGKKGGKKKG-------------SSFQ---------TVSALFRENLNKLMTNLRSTHPH 573
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884524 1038 FIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1101
Cdd:cd14915 574 FVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
421-1133 |
5.07e-75 |
|
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: 264.06 E-value: 5.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 421 IQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLC--SSLPPHLFSCVERAFHQLFQEQRPQCFILSG 497
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSRGfpSDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 498 ERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIYTYL 577
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL-LVGPDGGLKGGKITSYM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 578 LEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVSTGErslNREKLAVLKQALNVVgFSNL 657
Cdd:cd14886 166 LELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGID---DQKEFAPVRSQLEKL-FSKN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 658 EVENLFVILAAILHLGDIRFTALTEG---NSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAE 734
Cdd:cd14886 242 EIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 735 FFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVlFLH 813
Cdd:cd14886 322 VNIRAVAKDLYGALFELCVDTLNEIIQFDADARPW----IGILDIYGFEFFERNTYEQLLINYANERLQqYFINQV-FKS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 814 EQVECVQEGVTMETAYSPGNQNGVLdfFFQKPS-GFLTLLDEESQmiwsMESNFPKKLQSLLESSNTNAVYSPLKDGNGN 892
Cdd:cd14886 397 EIQEYEIEGIDHSMITFTDNSNVLA--VFDKPNlSIFSFLEEQCL----IQTGSSEKFTSSCKSKIKNNSFIPGKGSQCN 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 893 valkdhgtaFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINhlfqsklsqtgslvsaypsfkfrghksal 972
Cdd:cd14886 471 ---------FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN----------------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 973 lskkMTASSIIGENKNYLelskllkkkgtSTFLqrlergdpvtiASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDT 1052
Cdd:cd14886 513 ----KAFSDIPNEDGNMK-----------GKFL-----------GSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1053 FDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL---ADTFLREKKEHLAAERCRLVLQQCKLQGWQMGVRK 1129
Cdd:cd14886 567 YETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTK 646
|
....
gi 1622884524 1130 VFLK 1133
Cdd:cd14886 647 VFLR 650
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
417-1133 |
1.66e-74 |
|
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: 263.13 E-value: 1.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILS 496
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 497 GERGSGKSEASKQIIRHLTCRAASS----------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 566
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGekkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 567 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NREKL 642
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITT-------NPYDYAFVSQGEITVpsidDQEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 643 AVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 722
Cdd:cd14918 232 MATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 723 MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNEKM 802
Cdd:cd14918 312 YVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 803 HHYINEVLFLHEQVECVQEGVTMeTAYSPGNQNGVLDFFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSNtn 880
Cdd:cd14918 388 QQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLydQHLGKSAN-- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 881 avYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSqnllfvmktseNVVINHLFQSKLSQTGSLVSAY 960
Cdd:cd14918 465 --FQKPKVVKGKAE-----AHFSLIHYAGTVDYNITGWLDKNKDPLN-----------DTVVGLYQKSAMKTLASLFSTY 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 961 PSFKfrGHKSALLSKKMTASSIigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIH 1040
Cdd:cd14918 527 ASAE--ADSGAKKGAKKKGSSF-------------------------------QTVSALFRENLNKLMTNLRSTHPHFVR 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1041 CIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT------FLREKKehlAAERCRLV 1114
Cdd:cd14918 574 CIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASaipegqFIDSKK---ASEKLLAS 650
|
730
....*....|....*....
gi 1622884524 1115 LQQCKLQgWQMGVRKVFLK 1133
Cdd:cd14918 651 IDIDHTQ-YKFGHTKVFFK 668
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
416-1095 |
5.67e-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: 261.32 E-value: 5.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKlcSSLPPHLFSCVERAFHQLFQEQRP--QC 492
Cdd:cd14880 2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQP--QKLKPHIFTVGEQTYRNVKSLIEPvnQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 493 FILSGERGSGKSEASKQIIRHLTCRAASSRAM--------LDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcER 564
Cdd:cd14880 80 IVVSGESGAGKTWTSRCLMKFYAVVAASPTSWeshkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL-NR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 565 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTmqddvstgERSLNREKLAV 644
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP--------ERNLEEDCFEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 645 LKQALNVVGFSNLEVENLFVILAAILHLGDIRFTA---------LTEGNSAFVSDLQLLeqvagmLQVSTDELASALTT- 714
Cdd:cd14880 231 TREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADsedeaqpcqPMDDTKESVRTSALL------LKLPEDHLLETLQIr 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 715 DIQYFKGDMIIRRHTIQI-AEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDeqrSMQTLDIGILDIFGFEEFQKNEFEQL 793
Cdd:cd14880 305 TIRAGKQQQVFKKPCSRAeCDTRRDCLAKLIYARLFDWLVSVINSSICADT---DSWTTFIGLLDVYGFESFPENSLEQL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 794 CVNMTNEKM-HHYINEVLfLHEQVECVQEGVTMETAYSPGNQNgVLDFFFQKPSGFLTLLDEESQMiwsMESNFPKKLQS 872
Cdd:cd14880 382 CINYANEKLqQHFVAHYL-RAQQEEYAVEGLEWSFINYQDNQT-CLDLIEGSPISICSLINEECRL---NRPSSAAQLQT 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 873 LLESSNTNavySPLKdGNGNVALKdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKlsq 952
Cdd:cd14880 457 RIESALAG---NPCL-GHNKLSRE---PSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN--- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 953 tgslvsaypsfkfrghksallSKKMTASSIIGENknylelskllkkkgtstflqrleRGDPVTIASQLRKSLTDIIGKLQ 1032
Cdd:cd14880 527 ---------------------PEEKTQEEPSGQS-----------------------RAPVLTVVSKFKASLEQLLQVLH 562
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884524 1033 KCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA 1095
Cdd:cd14880 563 STTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLR 625
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
416-1101 |
1.13e-72 |
|
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: 257.69 E-value: 1.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY---RGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASS-----------RAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCEr 564
Cdd:cd14923 79 TGESGAGKTVNTKRVIQYFATIAVTGdkkkeqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 565 KQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNlcahrylNQTMQDDVSTGERSL----NRE 640
Cdd:cd14923 158 TGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIST-------NPFDFPFVSQGEVTVasidDSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 641 KLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFK 720
Cdd:cd14923 231 ELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 721 GDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqDEQRSMQTLdIGILDIFGFEEFQKNEFEQLCVNMTNE 800
Cdd:cd14923 311 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL---DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 801 KMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDfFFQKPSGFLTLLDEESQMIWSMESNFPKKL--QSLLESSN 878
Cdd:cd14923 387 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLydQHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 879 tnavYSPLKDGNGNVAlkdhgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFqsklsqtgslvS 958
Cdd:cd14923 466 ----FQKPKPAKGKAE-----AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-----------S 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 959 AYpsfkfrghksallskkmtASSIIGENknylelskllkkkGTSTFLQRLERGDPVTIASQLRKSLTDIIGKLQKCTPHF 1038
Cdd:cd14923 526 NY------------------AGAEAGDS-------------GGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHF 574
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884524 1039 IHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1101
Cdd:cd14923 575 VRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
416-1097 |
1.02e-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: 249.43 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKlcsslpPHLFSCVERAFHQLFQEQRpQCFIL 495
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE------PHVYDVAEASVQDLLVHGN-QTIVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASSRAmLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFcerKQQLTGARIYT 575
Cdd:cd14898 75 SGESGSGKTENAKLVIKYLVERTASTTS-IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF---DGKITGAKFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 576 YLLEKSRLVSQPLGQSNFLIFSLLmdglsaeekhglhlnnlCAHRYLNQTmQDDVSTGERSLNREKLAVLKQ-------A 648
Cdd:cd14898 151 YLLEKSRVTHHEKGERNFHIFYQF-----------------CASKRLNIK-NDFIDTSSTAGNKESIVQLSEkykmtcsA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 649 LNVVGFSNL-EVENLfviLAAILHLGDIRFTalTEGNSAFVSDlQLLEQVAGMLQVSTDELASALTT-DIQYfKGDMIIR 726
Cdd:cd14898 213 MKSLGIANFkSIEDC---LLGILYLGSIQFV--NDGILKLQRN-ESFTEFCKLHNIQEEDFEESLVKfSIQV-KGETIEV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEqrsmqtLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 806
Cdd:cd14898 286 FNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGE------RSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 807 NEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDffFQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLessntnavyspl 886
Cdd:cd14898 360 IKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRD--FEKPCGLMDLISEESFNAWGNVKNLLVKIKKYL------------ 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 887 kdgNGNVALKdHGTAFTIMHYAGRVMYDVVGAIEKNKDSlsqnllfvmktsenvvinhlfqsklsqtGSLvsaypsfkfR 966
Cdd:cd14898 426 ---NGFINTK-ARDKIKVSHYAGDVEYDLRDFLDKNREK----------------------------GQL---------L 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 967 GHKSALLSKKMTASSIIGENKNylelskllkkkgtstflqrlergdpvtiasqlrkSLTDIIGKLQKCTPHFIHCIRPNN 1046
Cdd:cd14898 465 IFKNLLINDEGSKEDLVKYFKD----------------------------------SMNKLLNSINETQAKYIKCIRPNE 510
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1622884524 1047 SKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADT 1097
Cdd:cd14898 511 ECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
428-1101 |
2.34e-70 |
|
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: 252.26 E-value: 2.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 428 NQIYTFIGDILLLVNPYKELPIYS-SMVSQLYFSSSgklcSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGKSEA 506
Cdd:cd14887 22 NCIYTYTGTLLIAVNPYRFFNLYDrQWISRFDTEAN----SRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTET 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 507 SKQIIRHLTC----RAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKqQLTGARIYTYLLEKSR 582
Cdd:cd14887 98 SKHVLTYLAAvsdrRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG-KLTRASVATYLLANER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 583 LVSQPLGQSNFLIFSllmdglsaeekhglhlnNLCAHRYLNQTMqdDVSTGERSLNREKLAVLKQALNVVGFSNLEVENL 662
Cdd:cd14887 177 VVRIPSDEFSFHIFY-----------------ALCNAAVAAATQ--KSSAGEGDPESTDLRRITAAMKTVGIGGGEQADI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 663 FVILAAILHLGDIRFTALTE--------------GNSAFVSDL-QLLE--------QVAGMLQVSTDELASALTTDIQYF 719
Cdd:cd14887 238 FKLLAAILHLGNVEFTTDQEpetskkrkltsvsvGCEETAADRsHSSEvkclssglKVTEASRKHLKTVARLLGLPPGVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 720 KGDMI-----IRR-------HTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL----------LSQDEQRSMQTLDIGIL 777
Cdd:cd14887 318 GEEMLrlalvSRSvretrsfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdSDEDTPSTTGTQTIGIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 778 DIFGFEEFQ---KNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVL-DFFFQKPSGFLTLLD 853
Cdd:cd14887 398 DLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSFPLaSTLTSSPSSTSPFSP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 854 EESQMIWSMESNFPKKLQSLLESSNTNAVYSPLKDGNGNV----------------------ALKDHGTAFTIMHYAGRV 911
Cdd:cd14887 478 TPSFRSSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSdlfyeklnkniinsakyknitpALSRENLEFTVSHFACDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 912 MYDVVGAIEKNKDSLSQNLlfvmktsenvvinhlfqsklsqtgslvsaypsfkfrghkSALLSKKMTASSIIGENKNyle 991
Cdd:cd14887 558 TYDARDFCRANREATSDEL---------------------------------------ERLFLACSTYTRLVGSKKN--- 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 992 lskllkkKGTSTFLQRLErgdpvTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMV 1071
Cdd:cd14887 596 -------SGVRAISSRRS-----TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLL 663
|
730 740 750
....*....|....*....|....*....|
gi 1622884524 1072 KIFRYGYPVRLSFSDFLSRYKPLADTFLRE 1101
Cdd:cd14887 664 RVMADGFPCRLPYVELWRRYETKLPMALRE 693
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
417-1094 |
2.90e-69 |
|
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: 246.71 E-value: 2.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgklcsslppHLFSCVERAFHQLFQ-EQRPQCFIL 495
Cdd:cd14874 3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC-------------HISGVAENALDRIKSmSSNAESIVF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTcrAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFceRKQQLTGARI-Y 574
Cdd:cd14874 70 GGESGSGKSYNAFQVFKYLT--SQPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY--KRNVLTGLNLkY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 575 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQ-----TMQDDVstgerslnrEKLAVLKQAL 649
Cdd:cd14874 146 TVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQgnsteNIQSDV---------NHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 650 NVVGFSNLEVENLFVILAAILHLGDIRFTAL----TEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQyfKGDMIi 725
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTKrnpnVEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSE--DGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 726 rrhTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdeQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHY 805
Cdd:cd14874 294 ---DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL-----KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 806 INEVLFLHEQVECVQEGVTMETAYSPGNQNG-VLDFFFQKPSGFLTLLDEESQmiwsmesnFPK-KLQSLLESSNTNAVY 883
Cdd:cd14874 366 FVKHSFHDQLVDYAKDGISVDYKVPNSIENGkTVELLFKKPYGLLPLLTDECK--------FPKgSHESYLEHCNLNHTD 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 884 splKDGNGNVALKDHgTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVsaypsf 963
Cdd:cd14874 438 ---RSSYGKARNKER-LEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMI------ 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 964 kfrghksallskkmtassiigenknylelskllkkkgtstflqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIR 1043
Cdd:cd14874 508 --------------------------------------------------VSQAQFILRGAQEIADKINGSHAHFVRCIK 537
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1622884524 1044 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPL 1094
Cdd:cd14874 538 SNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
416-1091 |
1.15e-65 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 237.30 E-value: 1.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGklcssLPPHLFSCVERAFHQLFQEQRPQCFI 494
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRG-----LPPHLFALAAKAISDMQDFRRDQLIF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 495 LSGERGSGKSEASKQIIRHLTCRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELqFCERKQQLTGARIY 574
Cdd:cd14905 77 IGGESGSGKSENTKIIIQYLLTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEM-FYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 575 TYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNQTMQDDVST--GERSLNReklavLKQALNVV 652
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDR-----LKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 653 GFSNLEVENLFVILAAILHLGDIRFtaLTEGNSAFVSDLQLLEQVAGMLQVSTDELASALTTDiqyfkgdmiiRRHTIQI 732
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTF--FQKNGKTEVKDRTLIESLSHNITFDSTKLENILISD----------RSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 733 AEFFRDLLAKSLYSRLFSFLVNTMNSCLlsqdeQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFL 812
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKL-----KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 813 HEQVECVQEGVTMETAYS-PGNQNGVldfffQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLESSNTnavysplkdgng 891
Cdd:cd14905 374 QEQREYQTERIPWMTPISfKDNEESV-----EMMEKIINLLDQESKNINSSDQIFLEKLQNFLSRHHL------------ 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 892 nvaLKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKtseNVVINHLFQS----KLSQTGSLVSAYPSFKFRG 967
Cdd:cd14905 437 ---FGKKPNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHK---NSITKYLFSRdgvfNINATVAELNQMFDAKNTA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 968 HKSALLSKK--MTASSIIGENKNYLELSKLLKKKGTSTFLQRLERGDPVTIASQLRKSLTDiigklQKCTPHFIHCIRPN 1045
Cdd:cd14905 511 KKSPLSIVKvlLSCGSNNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINN-----SNCDFHFIRCIKPN 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1622884524 1046 NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 1091
Cdd:cd14905 586 SKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRF 631
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
416-1092 |
1.33e-65 |
|
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: 237.11 E-value: 1.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSSMVSQLYFSSSGKLCSS----LPPHLFSCVERAFHQLFQEQRP 490
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAASaapfPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 491 QCFILSGERGSGKSEASKQIIRHLT-CRAASSRAMLDSRFKHVMCILEAFGHAKTTLNDLSSCFIKYFELQFCERKQQ-- 567
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHyIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENTqk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 568 ------LTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYL--------NQTMQDDVSTG 633
Cdd:cd14884 162 nmfngcFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLlnpdeshqKRSVKGTLRLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 634 ERSLNREKLAVLK---------QALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAgMLQVS 704
Cdd:cd14884 242 SDSLDPSEEEKAKdeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKAAAECLQIEEEDLENVIKYK-NIRVS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 705 TDelasalttdiqyfkgdmIIRRH-TIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMQTLD--------IG 775
Cdd:cd14884 321 HE-----------------VIRTErRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDiysineaiIS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 776 ILDIFGFEEFQKNEFEQLCVNMTNEKMH-HYINEVLFlHEQVECVQEGVTMETAYSPgNQNGVLDFffqkPSGFLTLLDE 854
Cdd:cd14884 384 ILDIYGFEELSGNDFDQLCINLANEKLNnYYINNEIE-KEKRIYARENIICCSDVAP-SYSDTLIF----IAKIFRRLDD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 855 ESQM-----------IWSMESNFPKKLQslLESSNTNAVYSPLKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNK 923
Cdd:cd14884 458 ITKLknqgqkktddhFFRYLLNNERQQQ--LEGKVSYGFVLNHDADGTAKKQNIKKNIFFIRHYAGLVTYRINNWIDKNS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 924 DSLSQNLLFVMKTSENVVINHlfqsklsqtgslvsaypsfkfrghksallskkmtasSIIGENKNYLelskllkkkgtst 1003
Cdd:cd14884 536 DKIETSIETLISCSSNRFLRE------------------------------------ANNGGNKGNF------------- 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1004 flqrlergdpVTIASQLRKSLTDIIGKLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLS 1083
Cdd:cd14884 567 ----------LSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
....*....
gi 1622884524 1084 FSDFLSRYK 1092
Cdd:cd14884 637 KKETAAALK 645
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
416-1133 |
6.14e-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: 229.50 E-value: 6.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfssSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFIL 495
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMF---KGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 496 SGERGSGKSEASKQIIRHLTCRAASS---------RAMLDsrfkhvmcILEAFGHAKTTLNDLSSCFIKYFELQFcERKQ 566
Cdd:cd01386 79 LGRSGSGKTTNCRHILEYLVTAAGSVggvlsveklNAALT--------VLEAFGNVRTALNGNATRFSQLFSLDF-DQAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 567 QLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLC--AHRYLNQTM-QDDVSTGERSLNRekla 643
Cdd:cd01386 150 QLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAesNSFGIVPLQkPEDKQKAAAAFSK---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 644 vLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAFVSDLQLLEQVAGMLQVSTDELASAL----------- 712
Cdd:cd01386 226 -LQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqq 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 713 -TTDIQYFKGDMIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQdeQRSMQTldIGILDIFGFE--EFQKNE 789
Cdd:cd01386 305 sTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSS--HHSTSS--ITIVDTPGFQnpAHSGSQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 790 ----FEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFFQKPS--------------GFLTL 851
Cdd:cd01386 381 rgatFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedrrGLLWL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 852 LDEESQMIWSMESNFPKKLQSLLESSNTNAVYSPLKDGngnvalkDHGTAFTIMHYAGR--VMYDVVGaieknkdslsqn 929
Cdd:cd01386 461 LDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRS-------EGPLQFVLGHLLGTnpVEYDVSG------------ 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 930 llFVMKTSENVvinhlfqSKLSQTGSLVSaypsfkfrghksallSKKMTAssiiGENKNYlelskllkkkgtstflqrle 1009
Cdd:cd01386 522 --WLKAAKENP-------SAQNATQLLQE---------------SQKETA----AVKRKS-------------------- 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1010 rgdpvtIASQLRKSLTDIIGKLQKCTPHFIHCIRPN------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG 1077
Cdd:cd01386 554 ------PCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkderstssPAAGDELLDVPLLRSQLRGSQLLDALRLYRQG 627
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884524 1078 YPVRLSFSDFLSRYKPLADTFLRE-------KKEHLAAERcrlVLQQCKLQ--GWQMGVRKVFLK 1133
Cdd:cd01386 628 FPDHMPLGEFRRRFQVLAPPLTKKlglnsevADERKAVEE---LLEELDLEksSYRIGLSQVFFR 689
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
417-1092 |
1.89e-59 |
|
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: 220.23 E-value: 1.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 417 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYFSSSGKL-------CSSLPPHLFSCVERAFHQLFQEQR 489
Cdd:cd14893 3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQTplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 490 PQCFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDS------------RFKHVMCILEAFGHAKTTLNDLSSCFIKYF 557
Cdd:cd14893 83 DQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSegasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 558 ELQFcERKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEE--KHGLHLNNLCAHRYLNQTMQDDVstGER 635
Cdd:cd14893 163 SVEF-SKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlRDSLEMNKCVNEFVMLKQADPLA--TNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 636 SLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEG-------NSAFVSDLQ--------LLEQVAGM 700
Cdd:cd14893 240 ALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGgksvggaNSTTVSDAQscalkdpaQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 701 LQVSTDELASALTTDiQYFKGD-----MIIRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCL---LSQDEQRSM--Q 770
Cdd:cd14893 320 LEVEPVVLDNYFRTR-QFFSKDgnktvSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggiFDRYEKSNIviN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 771 TLDIGILDIFGFEEF--QKNEFEQLCVNMTNEKMHH-YINEVL-----FLHEQVECVQEGVTMETAYS-PGNQNGVLDFF 841
Cdd:cd14893 399 SQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHfYVQNTLainfsFLEDESQQVENRLTVNSNVDiTSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 842 FQKPSGFLTLLDEESQMIWSMESNFPKKLQSLLE-----------SSNTNAVYSPLKDGNgnvalkdhgTAFTIMHYAGR 910
Cdd:cd14893 479 EDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEavgglsrpnmgADTTNEYLAPSKDWR---------LLFIVQHHCGK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 911 VMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLSQTGSLVSAyPSFKFRGHKSALLSKKMTASSiigENKNyl 990
Cdd:cd14893 550 VTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAA-KQTEERGSTSSKFRKSASSAR---ESKN-- 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 991 elskllkkKGTSTFLQRLERGDPVTIAsqlrksltdiigkLQKCTPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEM 1070
Cdd:cd14893 624 --------ITDSAATDVYNQADALLHA-------------LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVEL 682
|
730 740
....*....|....*....|..
gi 1622884524 1071 VKIFRYGYPVRLSFSDFLSRYK 1092
Cdd:cd14893 683 MQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
424-1133 |
9.73e-59 |
|
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: 215.65 E-value: 9.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 424 RFGNNQIYTFIGDILLLVNPYKELPIYSSmvsqlyfSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGK 503
Cdd:cd14937 10 RYKKNYIYTIAEPMLISINPYQVIDVDIN-------EYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGSGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 504 SEASKQIIRHLTCRAAS----SRAMLDSRFkhvmcILEAFGHAKTTLNDLSSCFIKYFELQFCERkQQLTGARIYTYLLE 579
Cdd:cd14937 83 TEASKLVIKYYLSGVKEdneiSNTLWDSNF-----ILEAFGNAKTLKNNNSSRYGKYIKIELDEY-QNIVSSSIEIFLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 580 KSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYL-NQTMQ----DDVSTGER---SLNREKLAVLKqalnv 651
Cdd:cd14937 157 NIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIvNKNVVipeiDDAKDFGNlmiSFDKMNMHDMK----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 652 vgfsnlevENLFVILAAILHLGDIRFTALTEGNSAFVSDL-----QLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 726
Cdd:cd14937 232 --------DDLFLTLSGLLLLGNVEYQEIEKGGKTNCSELdknnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 727 RHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNSCLLSQDEQRSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 806
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNY----IGILDIFGFEIFSKNSLEQLLINIANEEIHSIY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 807 NEVLFLHEQVECVQEGVTMETAYSPGNQNgVLDfffqkpsgfltLLDEESQMIWSMESNF--PKKLQSLLESSNTNAvYS 884
Cdd:cd14937 380 LYIVYEKETELYKAEDILIESVKYTTNES-IID-----------LLRGKTSIISILEDSClgPVKNDESIVSVYTNK-FS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 885 plKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSkLSQTGSLvsaypsfk 964
Cdd:cd14937 447 --KHEKYASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-VEVSESL-------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 965 frGHKSALLSKKMtassiigenknylelskllkkkgtstflqrlergdpvtiasqlrKSLTDIIGKLQKCTPHFIHCIRP 1044
Cdd:cd14937 516 --GRKNLITFKYL--------------------------------------------KNLNNIISYLKSTNIYFIKCIKP 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1045 NNSKLPDTFDNFYVSAQLQYIGVLEMVKI---FRYGYpvrlSFSDFLSRYKPL-----ADTFLREKkehlaaERCRLVLQ 1116
Cdd:cd14937 550 NENKEKNNFNQKKVFPQLFSLSIIETLNIsffFQYKY----TFDVFLSYFEYLdystsKDSSLTDK------EKVSMILQ 619
|
730
....*....|....*...
gi 1622884524 1117 Q-CKLQGWQMGVRKVFLK 1133
Cdd:cd14937 620 NtVDPDLYKVGKTMVFLK 637
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
45-314 |
3.93e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 165.51 E-value: 3.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 45 LKRLKHAKNPKVHFDLADMIQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDE 124
Cdd:COG0666 39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 125 DFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyldENGVDLtslrqmklqrpmsmltd 204
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA-------------NGNLEI----------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 205 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLV 284
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
|
250 260 270
....*....|....*....|....*....|
gi 1622884524 285 NCNEEKPSDIAASEFIEEMLLKAEIAWEEK 314
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
44-333 |
3.36e-42 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 157.04 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 44 FLKRLKHAKNPKVHFDLADMIQDAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQD 123
Cdd:COG0666 5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 124 EDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEgtesssilltyldENGVDLtslrqmklqrpmsmlt 203
Cdd:COG0666 85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY-------------NGNLEI---------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 204 dVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHL 283
Cdd:COG0666 136 -VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622884524 284 VNCNEEKPSDIAASEF---IEEMLLKAEIAWEEKMKEPLSVSTLAQEEPYEEI 333
Cdd:COG0666 215 KDNDGKTALDLAAENGnleIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
416-1132 |
1.18e-39 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 159.23 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 416 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSSMVSQLYfsssgkLCSSLPPHL----FSCVERAFHQLFQEQRPQ 491
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKY------KCIDCIEDLslneYHVVHNALKNLNELKRNQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 492 CFILSGERGSGKSEASKQIIRHLTCRAASSRAMLDSR-----------------------FKHVMCILEAFGHAKTTLND 548
Cdd:cd14938 76 SIIISGESGSGKSEIAKNIINFIAYQVKGSRRLPTNLndqeednihneentdyqfnmsemLKHVNVVMEAFGNAKTVKNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 549 LSSCFIKYFELQFceRKQQLTGARIYTYLLEKSRLVSQPLGQSNFLIFSLLMDGLSAEEKHGLHLNNLCAHRYLNqtmqD 628
Cdd:cd14938 156 NSSRFSKFCTIHI--ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLN----N 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 629 DVSTGERSLNREKLAVLKQALNVVGFSNLEVENLFVILAAILHLGDIRFTALTEGNSAF---------------VSDLQL 693
Cdd:cd14938 230 EKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLLmgknqcgqninyetiLSELEN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 694 LEQVAGMLQVSTDELASAL-----TTDIQYFKGDMI------IRRHTIQIAEFFRDLLAKSLYSRLFSFLVNTMNsCLLS 762
Cdd:cd14938 310 SEDIGLDENVKNLLLACKLlsfdiETFVKYFTTNYIfndsilIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN-EKCT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 763 QDEQRSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLHEQVECVQEGVTMETAYSPGNQNGVLDFFF 842
Cdd:cd14938 389 QLQNININTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 843 QKPSGFL-TLLDEESQMIWSMESNFpkkLQSLLESSNTNAVYSPLKDGNGNvalkdhGTAFTIMHYAGRVMYDVVGAIEK 921
Cdd:cd14938 469 GPTEGSLfSLLENVSTKTIFDKSNL---HSSIIRKFSRNSKYIKKDDITGN------KKTFVITHSCGDIIYNAENFVEK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 922 NKDSLSQNLLFVMKTSENVVINHLFQsklsqtgslvsaypSFKFRghksallskkmTASSIIGENKNYLELSKLlkkkgt 1001
Cdd:cd14938 540 NIDILTNRFIDMVKQSENEYMRQFCM--------------FYNYD-----------NSGNIVEEKRRYSIQSAL------ 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1002 STFLQRLERGDPVTIaSQLRKSLTDIIGKLQKCTPHFIHCIRPNNSK-LPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPV 1080
Cdd:cd14938 589 KLFKRRYDTKNQMAV-SLLRNNLTELEKLQETTFCHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPH 667
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1622884524 1081 RLSFSDFLSRYKpladtflreKKEHLAAERCRLVLQQCKL--QGWQMGVRKVFL 1132
Cdd:cd14938 668 KFTLNEFLSIFD---------IKNEDLKEKVEALIKSYQIsnYEWMIGNNMIFL 712
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
535-1101 |
2.60e-23 |
|
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: 107.91 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 535 ILEAFGHAKTTLNDLSSCFIKYFELQFC----ERKQQLTGARIYTYLLEKSRLVSQPLGQS------NFLIFSLLMDGLS 604
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVAfglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 605 AEE-----KHGLHLNNL-CA---------HRYLNQTMQDDvsTGERSLNREKLAVlkQALNVVGFSNLEVENLFVILAAI 669
Cdd:cd14894 335 AFPfmrllAKELHLDGIdCSaltylgrsdHKLAGFVSKED--TWKKDVERWQQVI--DGLDELNVSPDEQKTIFKVLSAV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 670 LHLGDIRFTALTEGNSAFVSD---LQLLEQVAGMLQV-STDELASALTTDIQYFKGDMIIRRHTIQIAEF--FRDLLAKS 743
Cdd:cd14894 411 LWLGNIELDYREVSGKLVMSStgaLNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVnhVRDTLARL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 744 LYSRLFSFLVNTMNSCL----LSQDEQRSMQTLD---------IGILDIFGFEEFQKNEFEQLCVNMTNEKMhhYINEvl 810
Cdd:cd14894 491 LYQLAFNYVVFVMNEATkmsaLSTDGNKHQMDSNasapeavslLKIVDVFGFEDLTHNSLDQLCINYLSEKL--YARE-- 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 811 flhEQVecvqegvtMETAYSP-------GNQNGVLdFFFQKPSGF------LTLLDEESQMIWSMESNFPKKLQSLLESS 877
Cdd:cd14894 567 ---EQV--------IAVAYSSrphltarDSEKDVL-FIYEHPLGVfasleeLTILHQSENMNAQQEEKRNKLFVRNIYDR 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 878 NTNAVYSP---LKDGNGNVALKDHGTAFTIMHYAGRVMYDVVGAIEKNKDSLSQNLLFVMKTSENvviNHLfqSKLSQTG 954
Cdd:cd14894 635 NSSRLPEPprvLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNS---SHF--CRMLNES 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 955 SLVSAYPSfkfrghksallskkmTASSIIGENKNylelskllKKKGTSTFLqrlergdpvtiaSQLRKSLTDIIGKLQKC 1034
Cdd:cd14894 710 SQLGWSPN---------------TNRSMLGSAES--------RLSGTKSFV------------GQFRSHVNVLTSQDDKN 754
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884524 1035 TPHFIHCIRPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG----YPVRLSFSDFLSRYKPLadtfLRE 1101
Cdd:cd14894 755 MPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSsssySAIDISKSTLLTRYGSL----LRE 821
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
72-304 |
1.23e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 102.82 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 72 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACAC-----DNPDIVLLLV 146
Cdd:PHA03100 14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 147 LAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLR-------QMKLQRPMSMLTDVKHFLSSGGNVNEKN 219
Cdd:PHA03100 94 EYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNsdgenllHLYLESNKIDLKILKLLIDKGVDINAKN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 220 degvtllhmacasgykeVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAASEF 299
Cdd:PHA03100 174 -----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
|
....*
gi 1622884524 300 IEEML 304
Cdd:PHA03100 237 NKEIF 241
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
67-280 |
1.29e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 102.82 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 67 AIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARY-----DNAFIAEILIDRGVNVNHQDEDFWTPMHIA-CACDN-P 139
Cdd:PHA03100 42 AKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAiSKKSNsY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 140 DIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLrqmklqrpmsmlTDVKHFLSSGGNVNEKN 219
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLIDKGVDINAK------------NRVNYLLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884524 220 DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQAN 280
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
441-559 |
5.28e-20 |
|
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: 88.94 E-value: 5.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 441 VNPYKELPIYSSmvSQLYFSSSGKLCSSLPPHLFSCVERAFHQLFQEQRPQCFILSGERGSGKSEASKQIIRHLTCRAAS 520
Cdd:cd01363 5 VNPFKELPIYRD--SKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFN 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622884524 521 SRAMLDSRFK---------------HVMCILEAFGHAKTTLNDLSSCFIKYFEL 559
Cdd:cd01363 83 GINKGETEGWvylteitvtledqilQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
76-279 |
2.20e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 91.66 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 76 VLRLLKEGADPHTLVSSGGSLLHLCAR--YDNAFIaEILIDRGVNVNHQDEDFWTPMHIACACD-NPDIVLLLVLAGANV 152
Cdd:PHA02876 290 VPKLLERGADVNAKNIKGETPLYLMAKngYDTENI-RTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANV 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 153 LLQDVNGNIPLDYAveGTESSSILLTYLDENGVDLTSLRQmKLQRPMSM-------LTDVKHFLSSGGNVNEKNDEGVTL 225
Cdd:PHA02876 369 NARDYCDKTPIHYA--AVRNNVVIINTLLDYGADIEALSQ-KIGTALHFalcgtnpYMSVKTLIDRGANVNSKNKDLSTP 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884524 226 LHMACASGYK-EVVSLILEHGGDLNIVDDQYWTPLHLAAKYgqANLVKLLLMHQA 279
Cdd:PHA02876 446 LHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGA 498
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
205-285 |
7.50e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 205 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHgGDLNIVDDQyWTPLHLAAKYGQANLVKLLLMHQANPHLV 284
Cdd:pfam12796 13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGADINVK 90
|
.
gi 1622884524 285 N 285
Cdd:pfam12796 91 D 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
104-291 |
9.91e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.85 E-value: 9.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 104 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVllQDVNGNIPLDYAVEGTESSSILLTYLDEN 183
Cdd:PHA02874 13 DIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADI--NHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 184 GVDLTSLRQMKLQRPMsmltdVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAA 263
Cdd:PHA02874 91 GVDTSILPIPCIEKDM-----IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
|
170 180
....*....|....*....|....*...
gi 1622884524 264 KYGQANLVKLLLMHQANPHLVNCNEEKP 291
Cdd:PHA02874 166 KHNFFDIIKLLLEKGAYANVKDNNGESP 193
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
67-156 |
1.39e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.92 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 67 AIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRgVNVNHQDEDfWTPMHIACACDNPDIVLLLV 146
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVKLLL 81
|
90
....*....|
gi 1622884524 147 LAGANVLLQD 156
Cdd:pfam12796 82 EKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
85-285 |
3.88e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.99 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 85 DPHTLVSSGGSLLHLCARYDNAFIAEI--LIDRGVNVNHQDEDFWTPMH--IACACDN-PDIVLLLVLAGANVLLQDVNG 159
Cdd:PHA03095 4 DESVDIIMEAALYDYLLNASNVTVEEVrrLLAAGADVNFRGEYGKTPLHlyLHYSSEKvKDIVRLLLEAGADVNAPERCG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 160 NIPLDYavegtesssilltYLdENGvdlTSLRQMKLqrpmsmltdvkhFLSSGGNVNEKNDEGVTLLHmACASGY---KE 236
Cdd:PHA03095 84 FTPLHL-------------YL-YNA---TTLDVIKL------------LIKAGADVNAKDKVGRTPLH-VYLSGFninPK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622884524 237 VVSLILEHGGDLNIVDDQYWTPLHLAAKYGQAN--LVKLLLMHQANPHLVN 285
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVD 184
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
75-284 |
5.13e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.60 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 75 EVLRLL-KEGADPHTLVSSGGSLLHLCARYDN--AFIAEILIDRGVNVNHQDEDFWTPMHI-----ACacdNPDIVLLLV 146
Cdd:PHA03095 98 DVIKLLiKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVllksrNA---NVELLRLLI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 147 LAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDLTSLRQMKLQRPMSMLT-------DVKHFLSSGGNVNEKN 219
Cdd:PHA03095 175 DAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgssckrsLVLPLLIAGISINARN 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884524 220 DEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLV 284
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
102-287 |
2.59e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 74.23 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 102 RYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLqdvngnIPLDyAVEGTESSSILLTYLD 181
Cdd:PHA02874 44 RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIP-CIEKDMIKTILDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 182 ENGVDLTSLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHL 261
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180
....*....|....*....|....*.
gi 1622884524 262 AAKYGQANLVKLLLMHQANPhLVNCN 287
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHI-MNKCK 221
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
74-291 |
5.79e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.52 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 74 KEVLRLLKEGADP-----------HTLVSSGGSL-------------------------LHLCARYDN-AFIAEILIDRG 116
Cdd:PHA03095 28 EEVRRLLAAGADVnfrgeygktplHLYLHYSSEKvkdivrllleagadvnapercgftpLHLYLYNATtLDVIKLLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 117 VNVNHQDEDFWTPMHIACA--CDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILLTYLDENGVDL------- 187
Cdd:PHA03095 108 ADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVyavddrf 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 188 -TSLRQMKL-----QRPMSMLTDvkhflsSGGNVNEKNDEGVTLLH-MACASGYKE-VVSLILEHGGDLNIVDDQYWTPL 259
Cdd:PHA03095 188 rSLLHHHLQsfkprARIVRELIR------AGCDPAATDMLGNTPLHsMATGSSCKRsLVLPLLIAGISINARNRYGQTPL 261
|
250 260 270
....*....|....*....|....*....|..
gi 1622884524 260 HLAAKYGQANLVKLLLMHQANPHLVNCNEEKP 291
Cdd:PHA03095 262 HYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
73-303 |
6.52e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 73.38 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 73 DKEVLRLLKE-GADPHTLV-SSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGA 150
Cdd:PHA02878 146 EAEITKLLLSyGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 151 NVLLQDVNGNIPLDYAVEGTESSSILltyldengvdltslrqmklqrpmsmltdvKHFLSSGGNVNEKND-EGVTLLHMA 229
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDIL-----------------------------KLLLEHGVDVNAKSYiLGLTALHSS 276
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884524 230 CASgyKEVVSLILEHGGDLNIVDDQYWTPLHLAAK-YGQANLVKLLLMHqanphlVNCNEEKPSDIAASE-FIEEM 303
Cdd:PHA02878 277 IKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILISN------ICLLKRIKPDIKNSEgFIDNM 344
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
226-277 |
2.25e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 2.25e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1622884524 226 LHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMH 277
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
97-252 |
2.39e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.37 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 97 LHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLvlaganvllqdvngnipLDYAvegtesssil 176
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-----------------LEHA---------- 53
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884524 177 ltyldengvdltslrqmklqrpmsmltdvkhflssggNVNEKnDEGVTLLHMACASGYKEVVSLILEHGGDLNIVD 252
Cdd:pfam12796 54 -------------------------------------DVNLK-DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
72-310 |
9.02e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.61 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 72 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGAN 151
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 152 VLLQDVNGNIPLDYAVEgtesssilltYLDengvdltslrqmklqrpmsmLTDVKHFLSSGGNVNEKNDEGVTLLHMACA 231
Cdd:PHA02874 183 ANVKDNNGESPLHNAAE----------YGD--------------------YACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 232 sgYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYG-QANLVKLLLMHQANPHLVNCNEEKPSDIAASEFIEEMLLKAEIA 310
Cdd:PHA02874 233 --HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIA 310
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
222-275 |
1.58e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.75 E-value: 1.58e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622884524 222 GVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLL 275
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
72-280 |
3.69e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 68.17 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 72 NDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDedfwtpMHIACACDNPDI--VLLLVLAG 149
Cdd:PHA02876 190 NAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND------LSLLKAIRNEDLetSLLLYDAG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 150 ANVLLQDVNGNIPLDYAVEgTESSSILLTYLDENGVDLTSlRQMKLQRPMSMLT-------DVKHFLSSGGNVNEKNDEG 222
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASQ-APSLSRLVPKLLERGADVNA-KNIKGETPLYLMAkngydteNIRTLIMLGADVNAADRLY 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884524 223 VTLLHMACA-SGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQAN 280
Cdd:PHA02876 342 ITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
104-296 |
1.76e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.86 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 104 DNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSI-------- 175
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkaiidnrs 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 176 ---------------------LLTYldENGVDLTSLRQMK-------LQRPmSMLTDVKHFLSSGGNVNEKNDEGVTLLH 227
Cdd:PHA02876 236 ninkndlsllkairnedletsLLLY--DAGFSVNSIDDCKntplhhaSQAP-SLSRLVPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884524 228 MACASGY-KEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQ-ANLVKLLLMHQANPHLVNCNEEKPSDIAA 296
Cdd:PHA02876 313 LMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAA 383
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1370-1647 |
1.72e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.42 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1370 RPGDARPPGAPGTAARVLTPGTPQCALPPatPPG--------DEDDGEPVYIEML--------------GHPARPDSPD- 1426
Cdd:PHA03247 2482 RPAEARFPFAAGAAPDPGGGGPPDPDAPP--APSrlapailpDEPVGEPVHPRMLtwirgleelasddaGDPPPPLPPAa 2559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1427 ----PGESVYEEMkcCLPDDGGPGAGSflRASPPllhGAPEDEAAGP-PGDMCDIP--PPFPNLLPHRPPllvfPPTPVT 1499
Cdd:PHA03247 2560 ppaaPDRSVPPPR--PAPRPSEPAVTS--RARRP---DAPPQSARPRaPVDDRGDPrgPAPPSPLPPDTH----APDPPP 2628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1500 CSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSP-------LSPQYSKSQKGDGDRPASPGLALFNGSGRASPPStpp 1572
Cdd:PHA03247 2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPrrarrlgRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPP--- 2705
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884524 1573 ppppgPPPAPFRPCAHLAFPPEPAPVSLGKAGPSTEAPKVHPKPNSA---PGAGSCSSFPKIPYSPVKAARVDARKAG 1647
Cdd:PHA03247 2706 -----PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGpatPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
97-295 |
2.20e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.20 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 97 LHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIAC-----------------------------ACDNPD------- 140
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdAFNNRNveifkii 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 141 ----------------------------IVLLLVLAGANVLLQDVN-GNIPLDYAVEG--TESSSILLTYLDE-NGVDLT 188
Cdd:PHA02878 121 ltnrykniqtidlvyidkkskddiieaeITKLLLSYGADINMKDRHkGNTALHYATENkdQRLTELLLSYGANvNIPDKT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 189 SLRQMKLQRPMSMLTDVKHFLSSGGNVNEKNDEGVTLLHMacASGY---KEVVSLILEHGGDLNIVDD-QYWTPLHLAAK 264
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI--SVGYckdYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278
|
250 260 270
....*....|....*....|....*....|.
gi 1622884524 265 YGQAnlVKLLLMHQANPHLVNCNEEKPSDIA 295
Cdd:PHA02878 279 SERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
14-261 |
6.08e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.04 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 14 GQRQRLVKRMRCEQI----KAYYEREKAFQKQEGFLKRL--------KHAKNPKVHfDLADMIQDAIIHH---NDKEVLR 78
Cdd:PLN03192 433 GEKERVVGTLGCGDIfgevGALCCRPQSFTFRTKTLSQLlrlktstlIEAMQTRQE-DNVVILKNFLQHHkelHDLNVGD 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 79 LLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILiDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVN 158
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 159 GNIPLDYAVEGTESSSILLTYL------DENGVDLTSLRQMKlqrpmSMLTDVKHFLSSGGNVNEKNDEGVTLLHMACAS 232
Cdd:PLN03192 591 GNTALWNAISAKHHKIFRILYHfasisdPHAAGDLLCTAAKR-----NDLTAMKELLKQGLNVDSEDHQGATALQVAMAE 665
|
250 260 270
....*....|....*....|....*....|
gi 1622884524 233 GYKEVVSLILEHGGDLNIVD-DQYWTPLHL 261
Cdd:PLN03192 666 DHVDMVRLLIMNGADVDKANtDDDFSPTEL 695
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
112-166 |
1.37e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 52.73 E-value: 1.37e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884524 112 LIDRG-VNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYA 166
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
205-282 |
1.77e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.53 E-value: 1.77e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884524 205 VKHFLSSGGNVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPH 282
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
66-287 |
2.43e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.46 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 66 DAIIHHNDKEVLRLLKEGADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIacACDNPDIVLLL 145
Cdd:PHA02875 8 DAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHD--AVEEGDVKAVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 146 VLAGANVLLQDV---NGNIPLDYAVEgtesssilltyldengvdLTSLRQMKLqrpmsmltdvkhFLSSGGNVNEKNDEG 222
Cdd:PHA02875 86 ELLDLGKFADDVfykDGMTPLHLATI------------------LKKLDIMKL------------LIARGADPDIPNTDK 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884524 223 VTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCN 287
Cdd:PHA02875 136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1333-1624 |
4.05e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.80 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1333 PRPHSDDYStmkkIPPRKPKRSPNTKLSGSYEEISGSRPGDARP--PGAPGTAARVLTPGTPqcaLPPATPPGDEDDGEP 1410
Cdd:PHA03247 2559 APPAAPDRS----VPPPRPAPRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRGPAPPSP---LPPDTHAPDPPPPSP 2631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1411 vyiemlghPARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLR-----ASPPLLHGAPED-------EAAGPPGDMCDIPP 1478
Cdd:PHA03247 2632 --------SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRrarrlGRAAQASSPPQRprrraarPTVGSLTSLADPPP 2703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1479 PFPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKSQKGDGDRPASPGLAL 1558
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL 2783
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884524 1559 FNGSGRA---------SPPSTPPPPPPGPPPAPFRPCAHLAFPPEPAPVSLGKAGPSTEAPkvhPKPNSAPGAGS 1624
Cdd:PHA03247 2784 TRPAVASlsesreslpSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG---PPPPSLPLGGS 2855
|
|
| NYAP_N |
pfam15439 |
Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter; NYAP_N is an N-terminal ... |
65-251 |
9.33e-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: 56.32 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 65 QDAIIHHNDKEvLRLLKEGADPHTLVSSGGSLLHL-----CARYDN---AFIAEILI--DRGVNVNHQDED--FWTPMHI 132
Cdd:pfam15439 7 LEKRRRQEEGI-KRSGEEVAGKVRDISSEGRHFRMgfmtmPASQDRlphPCAAGMSIrsQSLHSVGSGDEDgsLPSSRKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 133 ACACDNPDIVLLLVLAGANVLLQDVNGNIpldyaVEGTESSSILLTYLDENgVDLTSLRQMKLQR-PMSMLT-------- 203
Cdd:pfam15439 86 PPPKPKRDPSTKLSMSSEAVSAGLSAGAK-----ETPSETEALSKPRPHSD-EYSRKIPPPKPKRsPNTQLSgsfdeipa 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884524 204 ------DVKHFLSSGG---NVNEKNDE---------GVTLLHMACA----------SGYKEVVSLILEHGGDLNIV 251
Cdd:pfam15439 160 pyirphGLLQRASSSDgpsPAPLPDEEeepvyiemvGNVLRDFSPTtpdddpdqseAVYEEMKYPLPEDSGAANGP 235
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
92-260 |
1.51e-07 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 56.46 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 92 SGGSLLH--LCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDN--PDIVLLLVLAGANVLLQDVNGNIP-LDYA 166
Cdd:PHA02716 176 TGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPiMTYI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 167 VE----GTESSSILLTYLDENGVD-----LTSLRQMKLQRPMSMltdVKHFLSSGGNVNEKNDEGVTLLHMACASGY--K 235
Cdd:PHA02716 256 INidniNPEITNIYIESLDGNKVKnipmiLHSYITLARNIDISV---VYSFLQPGVKLHYKDSAGRTCLHQYILRHNisT 332
|
170 180
....*....|....*....|....*
gi 1622884524 236 EVVSLILEHGGDLNIVDDQYWTPLH 260
Cdd:PHA02716 333 DIIKLLHEYGNDLNEPDNIGNTVLH 357
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
93-146 |
2.45e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.20 E-value: 2.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622884524 93 GGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLV 146
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
214-262 |
3.36e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 3.36e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622884524 214 NVNEKNDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLA 262
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
130-297 |
3.79e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.61 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 130 MHIACACD-----NPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSILL-----TYLDENGVDLTSLRQMKLQRpm 199
Cdd:PHA02875 1 MDQVALCDailfgELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLlmkhgAIPDVKYPDIESELHDAVEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 200 SMLTDVKHFLSSGGNVNEK-NDEGVTLLHMACASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQ 278
Cdd:PHA02875 79 GDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
170
....*....|....*....
gi 1622884524 279 ANPHLVNCNEEKPSDIAAS 297
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAMA 177
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1325-1660 |
5.38e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 55.18 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1325 AANEALARPRPHSDDYSTMKKIPPRKPKRSPNTklsgsyeeiSGSRPGDARPPGAPGTAARvlTPGTPQCALPPATPPGD 1404
Cdd:PHA03307 133 DLSEMLRPVGSPGPPPAASPPAAGASPAAVASD---------AASSRQAALPLSSPEETAR--APSSPPAEPPPSTPPAA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1405 EDDGEPVYIEMLGHPARPDSPDPGESvyeemkcclpDDGGPGAGSFLRASPPllhgaPEDEAAGPPgDMCDIPPPFPNLL 1484
Cdd:PHA03307 202 ASPRPPRRSSPISASASSPAPAPGRS----------AADDAGASSSDSSSSE-----SSGCGWGPE-NECPLPRPAPITL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1485 PHRPPLLVFP-PTPVTCSPASDESPLTPLEVKKLPvletnlkypvQSEGSSPLSPQYSKSQKGDGDRPASPGLALFNGSG 1563
Cdd:PHA03307 266 PTRIWEASGWnGPSSRPGPASSSSSPRERSPSPSP----------SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSES 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1564 RASppstppppppgpppapfrpcahLAFPPEPAPVSLGKAGPSTEAPKVHPK---PNSAPGAGSCSSFPKIPYSPVKAAR 1640
Cdd:PHA03307 336 SRG----------------------AAVSPGPSPSRSPSPSRPPPPADPSSPrkrPRPSRAPSSPAASAGRPTRRRARAA 393
|
330 340
....*....|....*....|
gi 1622884524 1641 VDARKAGSSASPPAPYSPPS 1660
Cdd:PHA03307 394 VAGRARRRDATGRFPAGRPR 413
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1308-1647 |
7.05e-07 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.79 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1308 LSASYEAVSACLSAAREAANealaRPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPPGAPGTAArvl 1387
Cdd:PHA03307 44 VSDSAELAAVTVVAGAAACD----RFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDP--- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1388 TPGTPQCALPPATPPgdeddgePVYIEML------GHPARPDSPDPGESvyeemKCCLPDDGGPGAGSFLRASPPllhga 1461
Cdd:PHA03307 117 PPPTPPPASPPPSPA-------PDLSEMLrpvgspGPPPAASPPAAGAS-----PAAVASDAASSRQAALPLSSP----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1462 PEDEAAGPPGDMCDIPPPFPNLLPHRPPllvfPPTPVTCSPASDESPLTP--LEVKKLPVLETNLKYPVQSEGSSPL--- 1536
Cdd:PHA03307 180 EETARAPSSPPAEPPPSTPPAAASPRPP----RRSSPISASASSPAPAPGrsAADDAGASSSDSSSSESSGCGWGPEnec 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1537 -----SPQYSKSQKGDGDRPASPGLALFNGSGRASPPSTPPPPPPGPPPAPFRPCAH-------------LAFPPEPAPV 1598
Cdd:PHA03307 256 plprpAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPrasssssssressSSSTSSSSES 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622884524 1599 SLGKAGPSTEAPKVHPKPNSAPGAGSCSSFPKIPySPVKAARVDARKAG 1647
Cdd:PHA03307 336 SRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP-RPSRAPSSPAASAG 383
|
|
| GGN |
pfam15685 |
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ... |
1297-1638 |
7.81e-07 |
|
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.
Pssm-ID: 434857 [Multi-domain] Cd Length: 668 Bit Score: 54.00 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1297 PPKPKRDPNTRLSASYE-AVSACLSAAREAANEALARPRPHSDDYS-----TMKKIPPRKPKRSpntklSGSYEEISGSR 1370
Cdd:pfam15685 198 SATSPTDSQAKHIAEGKtAGGACGGAPPQAGEGEMARFAASESGLSllckvTFKSAAPLCPAAA-----SGPLAAKASLG 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1371 PGDARPPGAPGTA---ARVLTPG--TPQCALPPATPP-------GDEDDGEPVYiemlGHPARPDS-----PDPGESVYE 1433
Cdd:pfam15685 273 GGGGGGLFAASGAiscAEVLKQGplAPGAARPLGEVPraaleteGGEGDGEGCS----GGPAAPASharalPPPAYTTFP 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1434 EMKCCL----PDDG--------GPGAGSflrasppllhGAPEDEAAGPPGDMCDIPPP----FPNLLPHRP-PLLVFPPT 1496
Cdd:pfam15685 349 GSKPKFdwvsPPDGperhfrfnGAGGGI----------GAPRRRAAALSGPWGSPPPPpgkaHPIPGPRRPaPALLAPPM 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1497 PVTCSPASDESPLT-PLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKSQKGD--GDRPASPGlalfNGSGRASPpstppp 1573
Cdd:pfam15685 419 FIFPAPTNGEPVRPgPPAPQALLPRPPPPTPPATPPPVPPPIPQLPALQPMPlaAARPPTPR----PCPGHGES------ 488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884524 1574 pppgpppapfrpcahlAFPPEP-APVSLGKAGPSTEAPKVH--PKPNSAPGAGSCSSFPKIPySPVKA 1638
Cdd:pfam15685 489 ----------------ALAPAPtAPLPPALAADQAPAPALAaaPAPSPAPAPATADPLPPAP-APIKA 539
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1309-1524 |
8.16e-07 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 54.11 E-value: 8.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1309 SASYEAVSACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDA-RPPGAPGTAARVl 1387
Cdd:PRK12323 376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASArGPGGAPAPAPAP- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1388 tPGTPQCALPPAT----PPGDEDDGEPVYIEMLGHPAR-PDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPPLLHGAP 1462
Cdd:PRK12323 455 -AAAPAAAARPAAagprPVAAAAAAAPARAAPAAAPAPaDDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATAD 533
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622884524 1463 EDEAAGPPGDMcdiPPPFPNLLPHRPPLLVFPPTPvtcsPASDESPLTPLEVKKLPVLETNL 1524
Cdd:PRK12323 534 PDDAFETLAPA---PAAAPAPRAAAATEPVVAPRP----PRASASGLPDMFDGDWPALAARL 588
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
137-290 |
1.08e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.30 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 137 DNP--DIVLLLVLAGANVLLQDVNGNIPLdyavegtesSSILLTYLDENgvdltslrqmklqrpmSMLTDVKHFLSSGGN 214
Cdd:PHA02798 47 DSPstDIVKLFINLGANVNGLDNEYSTPL---------CTILSNIKDYK----------------HMLDIVKILIENGAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 215 VNEKNDEGVTLLHMACASGY---KEVVSLILEHGGDLNIVDDQYWTPLHLAAKYG---QANLVKLLLMHQANPHLVNcNE 288
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHN-NK 180
|
..
gi 1622884524 289 EK 290
Cdd:PHA02798 181 EK 182
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
241-295 |
2.85e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 2.85e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884524 241 ILEHGG-DLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIA 295
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1307-1638 |
4.63e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1307 RLSASYEAVSACLSAAREAANEALARPRPHSddysTMKKIP-PRKPKRSPNTKLSGSYEEISGSRPGDARPPGAPGTAAR 1385
Cdd:PHA03247 2684 RRRAARPTVGSLTSLADPPPPPPTPEPAPHA----LVSATPlPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1386 VLTPGTPQCALPPATPPGDEDDGEPVYIEMLGHPARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPPLLHGAPede 1465
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQP--- 2836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1466 AAGPPGdmcdiPPPFPNLLPhrPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKSQK 1545
Cdd:PHA03247 2837 TAPPPP-----PGPPPPSLP--LGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1546 gdgdRPASPGLALFNGSGRASPPSTPPPPPPGPPPAPFRPCAHLAFPPEPAPVS----LGKAGPS-TEAPKVHPKPNSAP 1620
Cdd:PHA03247 2910 ----QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVpqpwLGALVPGrVAVPRFRVPQPAPS 2985
|
330
....*....|....*...
gi 1622884524 1621 GAGSCSSFPKIPYSPVKA 1638
Cdd:PHA03247 2986 REAPASSTPPLTGHSLSR 3003
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
37-168 |
5.36e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 37 AFQKQEGFLKRLKHAKNPK-VHFDLADMIQDAIIHHNDK-EVLRLLKEGAD--PHTLVSSGG-----------SLLHLCA 101
Cdd:PTZ00322 12 AFAAQLFFGTEGSRKRRAKpISFERMAAIQEEIARIDTHlEALEATENKDAtpDHNLTTEEVidpvvahmltvELCQLAA 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622884524 102 RYDnAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVE 168
Cdd:PTZ00322 92 SGD-AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
48-265 |
1.98e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.22 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 48 LKHAKNPKVHF-DLADMIQDAIIHHNDKEVLRLLKEGADPHTLV-SSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDED 125
Cdd:PHA02875 55 MKHGAIPDVKYpDIESELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 126 FWTPMHIACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAVEGTESSSilltyldengvdltslrqmklqrpmsmltdV 205
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI------------------------------C 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884524 206 KHFLSSGGNVNEKNDEG-VTLLHMACASGYKEVVSLILEHGGDLNI---VDDQYWTPLHLAAKY 265
Cdd:PHA02875 185 KMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNImfmIEGEECTILDMICNM 248
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1348-1554 |
2.13e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 49.69 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1348 PRKPK--RSPNTKLSGSYEEisgSRPGDARPPGA--PGTAARVLTPGTPQCALPPATPPGDEDDGEPVYIEMLGHPARPD 1423
Cdd:PTZ00449 588 PKDPEepKKPKRPRSAQRPT---RPKSPKLPELLdiPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKIIKSPKPPKSPK 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1424 SP-DPG--ESVYE----------EMKCCLPDDggPGAGSFLRASPPLLHGAPEDEaagppgdmcdiPPPFPNLLPHRPPL 1490
Cdd:PTZ00449 665 PPfDPKfkEKFYDdyldaaakskETKTTVVLD--ESFESILKETLPETPGTPFTT-----------PRPLPPKLPRDEEF 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1491 LVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYP-------------VQSEGSSPLSPQ------YSKSQKGDGDRP 1551
Cdd:PTZ00449 732 PFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPlpdilaeefkeedIHAETGEPDEAMkrpdspSEHEDKPPGDHP 811
|
...
gi 1622884524 1552 ASP 1554
Cdd:PTZ00449 812 SLP 814
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
108-275 |
2.17e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 49.06 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 108 IAEILIDRGVNVNHQDEDFWTPM-----HIACACDNPDIVLLLVLAGANVLLQDVNGNIPLdYAV--EGTESSSILLTYL 180
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL-YCLlsNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 181 DENGVDLTSLRQMKlqrpmsmLTDVKHFLSSGGNVNekndegvtllhmacasgyKEVVSLILEHGGDLNIVDDQY-WTPL 259
Cdd:PHA02798 132 IENGADTTLLDKDG-------FTMLQVYLQSNHHID------------------IEIIKLLLEKGVDINTHNNKEkYDTL 186
|
170 180
....*....|....*....|
gi 1622884524 260 HLAAKYG----QANLVKLLL 275
Cdd:PHA02798 187 HCYFKYNidriDADILKLFV 206
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1333-1643 |
2.46e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 49.30 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1333 PRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYE----EISGSRPGDARPPGAPGTAARvltpgTPQCALPPATPPGdeddg 1408
Cdd:PHA03378 659 ITPYKPTWTQIGHIPYQPSPTGANTMLPIQWApgtmQPPPRAPTPMRPPAAPPGRAQ-----RPAAATGRARPPA----- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1409 epvyiemlGHPARPDSPDPGesvyeemkcclPDDGGPGAGSFLRASPPLLHGAPEDEAAGPPGDMCDIPPP--------F 1480
Cdd:PHA03378 729 --------AAPGRARPPAAA-----------PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPqappapqqR 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1481 PNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEvkklPVLETNLKYPVQSEGSSPLSPQYSKSQKGDGDRPaSPglalfn 1560
Cdd:PHA03378 790 PRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTK----QILRQLLTGGVKRGRPSLKKPAALERQAAAGPTP-SP------ 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1561 GSGRASPPSTppppppgpppapfrpcAHLAFPPEPAPVSL-GKAGPSTE--APKVHPKPNSAPG---AGSCSSFPKIPys 1634
Cdd:PHA03378 859 GSGTSDKIVQ----------------APVFYPPVLQPIQVmRQLGSVRAaaASTVTQAPTEYTGerrGVGPMHPTDIP-- 920
|
....*....
gi 1622884524 1635 PVKAARVDA 1643
Cdd:PHA03378 921 PSKRAKTDA 929
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
69-205 |
2.57e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 48.81 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 69 IHHNDKEVLRLLKE-GADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIACACDNPDIVLLLVL 147
Cdd:PHA02874 165 IKHNFFDIIKLLLEkGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINN 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622884524 148 AGANVllQDVNGNIPLDYAVEGTESSSILLTYL---------DENGVDLTSLrQMKLQRPMSMLTDV 205
Cdd:PHA02874 245 ASIND--QDIDGSTPLHHAINPPCDIDIIDILLyhkadisikDNKGENPIDT-AFKYINKDPVIKDI 308
|
|
| PHA03321 |
PHA03321 |
tegument protein VP11/12; Provisional |
1321-1511 |
3.40e-05 |
|
tegument protein VP11/12; Provisional
Pssm-ID: 223041 [Multi-domain] Cd Length: 694 Bit Score: 48.80 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1321 AAREAANEAlarPRPHSDDYSTMKKIPPRKPKRSPntklsgsyeeisgsRPGDARPPGAPGTAARVLTPGTPQcaLPPAT 1400
Cdd:PHA03321 486 AAPPPEPAA---APSPATYYTRMGGGPPRLPPRNR--------------ATETLRPDWGPPAAAPPEQMEDPY--LEPDD 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1401 PPGDEDDGEPVYIEmlGHPARPDSPDpGESVYEEMKcclpDDGGPGAGSF--LRASPPLLhGAPEDEAAGPPgdmcDIPP 1478
Cdd:PHA03321 547 DRFDRRDGAAAAAT--SHPREAPAPD-DDPIYEGVS----DSEEPVYEEIptPRVYQNPL-PRPMEGAGEPP----DLDA 614
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622884524 1479 PFPNLLPH--------RPPLLVFPPTPVTCSPASDESPLTP 1511
Cdd:PHA03321 615 PTSPWVEEenpiygwgDSPLFSPPPAARFPPPDPALSPEPP 655
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
256-285 |
4.28e-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: 42.28 E-value: 4.28e-05
10 20 30
....*....|....*....|....*....|.
gi 1622884524 256 WTPLHLAA-KYGQANLVKLLLMHQANPHLVN 285
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
61-167 |
4.65e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 48.10 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 61 ADMIQDAIIHH------NDKEVLR-LLKEGADPHTLVSSGGSLLHLCARYDNAFIAEI--LIDRGVNVNHQDEDFWTPMH 131
Cdd:PHA03095 183 VDDRFRSLLHHhlqsfkPRARIVReLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLH 262
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622884524 132 IACACDNPDIVLLLVLAGANVLLQDVNGNIPLDYAV 167
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
221-250 |
1.02e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 1.02e-04
10 20 30
....*....|....*....|....*....|
gi 1622884524 221 EGVTLLHMACASGYKEVVSLILEHGGDLNI 250
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
254-283 |
1.19e-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: 1.19e-04
10 20 30
....*....|....*....|....*....|
gi 1622884524 254 QYWTPLHLAAKYGQANLVKLLLMHQANPHL 283
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1308-1635 |
1.20e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 47.07 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1308 LSASYEAVSACLSAAREAANEALARPRPHSddystmkkiPPRKPKRSPNTKLSgSYEEISGSRPGDARPPGAPGTAARVL 1387
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSA---------PSVPPQGSPATSQP-PNQTQSTAAPHTLIQQTPTLHPQRLP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1388 TPGTPQCALPPATPPgDEDDGEPVYIEMLgHPARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPPLLhgaPEDEAA 1467
Cdd:pfam03154 244 SPHPPLQPMTQPPPP-SQVSPQPLPQPSL-HGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPG---PSPAAP 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1468 GPPGDMCDIPPPFPNLLPHRPPL-LVFPPTPVTCsPASDESPLTPleVKKLPVLETNlKYPVQSEGSSPLSPqysksqkg 1546
Cdd:pfam03154 319 GQSQQRIHTPPSQSQLQSQQPPReQPLPPAPLSM-PHIKPPPTTP--IPQLPNPQSH-KHPPHLSGPSPFQM-------- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1547 DGDRPASPGLALFngsgraSPPSTPPPPPPGPPPAPFRPCAHlAFPPEPAPVSLGKAGPSTEAPKV-HPKPNSAPGAGSC 1625
Cdd:pfam03154 387 NSNLPPPPALKPL------SSLSTHHPPSAHPPPLQLMPQSQ-QLPPPPAQPPVLTQSQSLPPPAAsHPPTSGLHQVPSQ 459
|
330
....*....|
gi 1622884524 1626 SSFPKIPYSP 1635
Cdd:pfam03154 460 SPFPQHPFVP 469
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
73-195 |
1.87e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.81 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 73 DKEVLRLL-KEGAD-PHTLVSSGGSLLHLCARYD---NAFIAEILIDRGVNVNHQDEDFWTPMHI-ACACD-NPDIVLLL 145
Cdd:PHA02859 65 NVEILKFLiENGADvNFKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLL 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622884524 146 VLAGANVLLQDVNGNIPLdYAVEGTESSSILLTYLDENGVDLTSLRQMKL 195
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNIL-YSYILFHSDKKIFDFLTSLGIDINETNKSGY 193
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
221-253 |
2.14e-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: 2.14e-04
10 20 30
....*....|....*....|....*....|....
gi 1622884524 221 EGVTLLHMACAS-GYKEVVSLILEHGGDLNIVDD 253
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1309-1595 |
2.30e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1309 SASYEAVSACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISG---SRPGDARPPGA-PGT-- 1382
Cdd:PHA03247 2800 SPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPPSRSPAAkPAApa 2879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1383 ---AARVLTPGTPQCALPPATPPgdeDDGEPvyiemlghPARPDSPDPGESVYEEMKCCLPDDGGPGAGsflRASPPLlh 1459
Cdd:PHA03247 2880 rppVRRLARPAVSRSTESFALPP---DQPER--------PPQPQAPPPPQPQPQPPPPPQPQPPPPPPP---RPQPPL-- 2943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1460 gAPEDEAAGPPGDMCDIPPP-FPNLLPHR---PPLLVFPPTPVTCSPASDESPLTPLEVKKL----------------PV 1519
Cdd:PHA03247 2944 -APTTDPAGAGEPSGAVPQPwLGALVPGRvavPRFRVPQPAPSREAPASSTPPLTGHSLSRVsswasslalheetdppPV 3022
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884524 1520 -LETNLKYPVQSEGSSPLSPQYSKSQKGDGDRP-ASPGlalfngsgrASPPSTPPPPPPGPPPAPFRPCAHLAFPPEP 1595
Cdd:PHA03247 3023 sLKQTLWPPDDTEDSDADSLFDSDSERSDLEALdPLPP---------EPHDPFAHEPDPATPEAGARESPSSQFGPPP 3091
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
221-250 |
2.43e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.93 E-value: 2.43e-04
10 20 30
....*....|....*....|....*....|
gi 1622884524 221 EGVTLLHMACASGYKEVVSLILEHGGDLNI 250
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1323-1640 |
2.72e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.21 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1323 REAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYeeisgsrPGDARPPGAPGTAARVLTPGTP---------- 1392
Cdd:PHA03378 433 KKAARTEQPRATPHSQAPTVVLHRPPTQPLEGPTGPLSVQA-------PLEPWQPLPHPQVTPVILHQPPaqgvqahgsm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1393 ----------------QCALPPATP-PGDEDDGEPVYIEMLGhpARPDSPDPGESVYEEMkccLPDDG-GP--------G 1446
Cdd:PHA03378 506 ldllekddedmeqrvmATLLPPSPPqPRAGRRAPCVYTEDLD--IESDEPASTEPVHDQL---LPAPGlGPlqiqpltsP 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1447 AGSFLRASPPLLHGAP-----EDEAAGPPGDMCDIPP---PFPNLLPHRP-PLLVFPPTPVTCSPASDESPLTPLEVKKL 1517
Cdd:PHA03378 581 TTSQLASSAPSYAQTPwpvphPSQTPEPPTTQSHIPEtsaPRQWPMPLRPiPMRPLRMQPITFNVLVFPTPHQPPQVEIT 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1518 PVLETNLKYPVQSEGSSPLSPQYSKSQKGDGDR----PASPGL----ALFNGSGRASPPSTPPPPPPGPPPAPFRPCAHL 1589
Cdd:PHA03378 661 PYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTmqppPRAPTPmrppAAPPGRAQRPAAATGRARPPAAAPGRARPPAAA 740
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622884524 1590 AFPPEPAPVSLGKAGPSTEAPKVHPKPNSAPGAGSCSSFPKIPYSPVKAAR 1640
Cdd:PHA03378 741 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPR 791
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
1346-1647 |
3.47e-04 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 45.44 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1346 IPPRKPKRSPNT---KLSGSYEEISGSRPGDARPPGAPGTAARvltPGTPQCALPPAT-PPGDEDDGEPVYIEMLGHPAR 1421
Cdd:COG5180 84 LDPAPPKSSPDTpeeQLGAPAGDLLVLPAAKTPELAAGALPAP---AAAAALPKAKVTrEATSASAGVALAAALLQRSDP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1422 PDSPDPGEsvyeemkccLPDDGGPGAGSFLR--ASPPLLHGAPEDEAAgppgdmcDIPPPfpnllPHRPPLLVFPPTPVT 1499
Cdd:COG5180 161 ILAKDPDG---------DSASTLPPPAEKLDkvLTEPRDALKDSPEKL-------DRPKV-----EVKDEAQEEPPDLTG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1500 CS-----PASDESPLTPLEvkklPVLETNLKYPVQSEG-SSPLSPQYSKSQKGDGDRPAS--PGL-ALFNGSGRASPPST 1570
Cdd:COG5180 220 GAdhprpEAASSPKVDPPS----TSEARSRPATVDAQPeMRPPADAKERRRAAIGDTPAAepPGLpVLEAGSEPQSDAPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1571 PPPPPPGPPPAPFRPcahlafPPEPAPVSLG---------KAGPSTEAPKVHPKPNSAPGAGSCSSFPKIPYSPVKAARV 1641
Cdd:COG5180 296 AETARPIDVKGVASA------PPATRPVRPPggardpgtpRPGQPTERPAGVPEAASDAGQPPSAYPPAEEAVPGKPLEQ 369
|
....*.
gi 1622884524 1642 DARKAG 1647
Cdd:COG5180 370 GAPRPG 375
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
223-295 |
5.66e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 5.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622884524 223 VTLLHMAcASGYKEVVSLILEHGGDLNIVDDQYWTPLHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIA 295
Cdd:PTZ00322 84 VELCQLA-ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
255-282 |
8.70e-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: 38.39 E-value: 8.70e-04
10 20
....*....|....*....|....*...
gi 1622884524 255 YWTPLHLAAKYGQANLVKLLLMHQANPH 282
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1316-1508 |
1.38e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1316 SACLSAAREAANEALARPRPHSDDYSTMKKIPPRKPKRSPNTKLSGSYEEISGSRPGDARPPGAPGTAARVLTPGTPQCA 1395
Cdd:PHA03307 227 SAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1396 LPPATPPGDEDDGEPvyiemlgHPARPDSPDPGESVyeemkcclpdDGGPGAGSflrasppllhGAPEDEAAGPPGDMCD 1475
Cdd:PHA03307 307 PAPSSPRASSSSSSS-------RESSSSSTSSSSES----------SRGAAVSP----------GPSPSRSPSPSRPPPP 359
|
170 180 190
....*....|....*....|....*....|...
gi 1622884524 1476 IPPPFPnllPHRPPLLVFPPTPVTcSPASDESP 1508
Cdd:PHA03307 360 ADPSSP---RKRPRPSRAPSSPAA-SAGRPTRR 388
|
|
| PHA03325 |
PHA03325 |
nuclear-egress-membrane-like protein; Provisional |
1371-1513 |
2.12e-03 |
|
nuclear-egress-membrane-like protein; Provisional
Pssm-ID: 223044 Cd Length: 418 Bit Score: 42.56 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1371 PGDARPPGAPGTAARVLTPGTPQCALPPATPPGDEDDGEPVyiemlgHPARPDSPDPGESVYEEMkcclpDDGGPGAGSF 1450
Cdd:PHA03325 282 AMRAAAGETADLADDDGSEHSDPEPLPASLPPPPVRRPRVK------HPEAGKEEPDGARNAEAK-----EPAQPATSTS 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1451 LRASPpllHGAPEDEAAGPPGDMC-------DIPPPFPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLE 1513
Cdd:PHA03325 351 SKGSS---SAQNKDSGSTGPGSSLaaassflEDDDFGSPPLDLTTSLRHMPSPSVTSAPEPPSIPLTYLS 417
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
1344-1554 |
2.61e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 42.61 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1344 KKIPPRKPKRS--PNTKLSGSYEEISGSRPGDARPPGAPGTAARVLTPGTPQCALPPATPP------------------- 1402
Cdd:PLN03209 326 QRVPPKESDAAdgPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYEDLKPPTSPiptppssspassksvdava 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1403 -GDEDDGEPVYIEMLGHP-----------ARPDSPdpgESVYEEMK-CCLPDDGGPGAGSFLRASPPLLHGAPEDEAAGP 1469
Cdd:PLN03209 406 kPAEPDVVPSPGSASNVPevepaqveakkTRPLSP---YARYEDLKpPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1470 PGDMCDIPPPFPNllPHRPPL----LVFPPTPVTCSPASDESPLTPLEVKKL--------PVLETNLKYPVQsegsSPLS 1537
Cdd:PLN03209 483 ATDAAAPPPANMR--PLSPYAvyddLKPPTSPSPAAPVGKVAPSSTNEVVKVgnsapptaLADEQHHAQPKP----RPLS 556
|
250
....*....|....*..
gi 1622884524 1538 PqYSKSQkgDGDRPASP 1554
Cdd:PLN03209 557 P-YTMYE--DLKPPTSP 570
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
1337-1526 |
2.83e-03 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 42.73 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1337 SDDYSTMKKipPRKPKRSPNT--KLSGSYEE------ISGSRPG--DARPPGA--PGTAARVLTPGT--PQCALPPATPP 1402
Cdd:PHA03377 520 TEEEESVTQ--PAKPHRKVQDgfQRSGRRQKratppkVSPSDRGppKASPPVMapPSTGPRVMATPStgPRDMAPPSTGP 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1403 GDE---DDGEPVYIEMLGHP--ARPDSPDPgeSVYEEM--KCCLPDDGGPGAGSF--LRAS--------PPLLHGAPEDE 1465
Cdd:PHA03377 598 RQQakcKDGPPASGPHEKQPpsSAPRDMAP--SVVRMFlrERLLEQSTGPKPKSFweMRAGrdgsgiqqEPSSRRQPATQ 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884524 1466 AAgppgdmcdipPPFPNLLphrPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKY 1526
Cdd:PHA03377 676 ST----------PPRPSWL---PSVFVLPSVDAGRAQPSEESHLSSMSPTQPISHEEQPRY 723
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
127-156 |
2.84e-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: 2.84e-03
10 20 30
....*....|....*....|....*....|.
gi 1622884524 127 WTPMHIACA-CDNPDIVLLLVLAGANVLLQD 156
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1335-1469 |
3.61e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.62 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1335 PHS-DDYSTMKKIPPRKP-----------KRSPNTKLSGSYEEISGSRPGDARPP--GAPGTAARVltPGTPQCALPPAT 1400
Cdd:PHA03247 362 PSSlEDLSAGRHHPKRASlptrkrrsarhAATPFARGPGGDDQTRPAAPVPASVPtpAPTPVPASA--PPPPATPLPSAE 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622884524 1401 PPGDEDDGEPVYiemlGHPARPDSPDPGESvyeemkcclPDDGGPGAGSFLRASPPllhgaPEDEAAGP 1469
Cdd:PHA03247 440 PGSDDGPAPPPE----RQPPAPATEPAPDD---------PDDATRKALDALRERRP-----PEPPGADL 490
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
214-288 |
3.75e-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: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 214 NVNEKNDEGVTLLHMAcASGYKEVVSLILEH-------GGDLNIVDDQYW-------TPLHLAAKYGQANLVKLLLMHQA 279
Cdd:TIGR00870 74 NLSCRGAVGDTLLHAI-SLEYVDAVEAILLHllaafrkSGPLELANDQYTseftpgiTALHLAAHRQNYEIVKLLLERGA 152
|
90
....*....|
gi 1622884524 280 NPHL-VNCNE 288
Cdd:TIGR00870 153 SVPArACGDF 162
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
1354-1540 |
3.77e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 42.12 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1354 SPNTKLSGSYEEISGSRPGDARPPGAPGTAARVLTPGTPQC-ALPPATP--PGDEDDGEP-----------VYIEMLGHP 1419
Cdd:PRK14086 96 APPPPHARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQdQLPTARPayPAYQQRPEPgawpraaddygWQQQRLGFP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1420 ARPDSPDPGESVYEEMKCCLPDDGGPGAGSFLRASPpllHGaPEDEAAGPPGDMCDIPPPFPNllPHRPPLLVFPPTPVT 1499
Cdd:PRK14086 176 PRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDY---DH-PRPDWDRPRRDRTDRPEPPPG--AGHVHRGGPGPPERD 249
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622884524 1500 CSPASDESPLTPLEVKKLPvlETNlkyPVQSEGSSPLSPQY 1540
Cdd:PRK14086 250 DAPVVPIRPSAPGPLAAQP--APA---PGPGEPTARLNPKY 285
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
79-133 |
3.92e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 3.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884524 79 LLKEG-ADPHTLVSSGGSLLHLCARYDNAFIAEILIDRGVNVNHQDEDFWTPMHIA 133
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
259-309 |
4.62e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 38.17 E-value: 4.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622884524 259 LHLAAKYGQANLVKLLLMHQANPHLVNCNEEKPSDIAAS----EFIEEMLLKAEI 309
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKnghlEIVKLLLEHADV 55
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
125-152 |
4.76e-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: 36.41 E-value: 4.76e-03
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
127-152 |
5.36e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.08 E-value: 5.36e-03
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
69-261 |
5.69e-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: 41.54 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 69 IHHNDKEVL-RLLK-EGADPHTLVSSGGSLLHLCARYDNAFIAEILID---RGVNVNHQDEDFW--TPMHIACACDNPDI 141
Cdd:cd22192 25 AKENDVQAIkKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDLYQgeTALHIAVVNQNLNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 142 VLLLVLAGANVLLQDVNGnipldyavegtesssillTYLdengvdltslrqmkLQRPMSMLTDVKHFLSsggnvneknde 221
Cdd:cd22192 105 VRELIARGADVVSPRATG------------------TFF--------------RPGPKNLIYYGEHPLS----------- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622884524 222 gvtllHMACAsGYKEVVSLILEHGGDLNIVDDQYWTPLHL 261
Cdd:cd22192 142 -----FAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1374-1646 |
6.56e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1374 ARPPGAPGTAARVLTPGTPQCALPPatpPGDEDDGEPVYIEMLGHPARPDSPDPGESVYEEmkcclpDDGGPGAGSFLRA 1453
Cdd:PHA03307 22 PRPPATPGDAADDLLSGSQGQLVSD---SAELAAVTVVAGAAACDRFEPPTGPPPGPGTEA------PANESRSTPTWSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1454 SPPLLHGAPEDEAAGPPGdmcdipppfpnllphRPPLLVFPPTPVTCSPASDESPLTPlevkklPVLETNLKYPVQSEGS 1533
Cdd:PHA03307 93 STLAPASPAREGSPTPPG---------------PSSPDPPPPTPPPASPPPSPAPDLS------EMLRPVGSPGPPPAAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884524 1534 SPLSPqySKSQKGDGDRPASPGLALFNGSGRASPPSTPPPPPpgpppapfrpcahlAFPPEPAPVSLGKAGPSTEAPKVH 1613
Cdd:PHA03307 152 PPAAG--ASPAAVASDAASSRQAALPLSSPEETARAPSSPPA--------------EPPPSTPPAAASPRPPRRSSPISA 215
|
250 260 270
....*....|....*....|....*....|...
gi 1622884524 1614 PKPNSAPGAGSCSSFPKIPYSPVKAARVDARKA 1646
Cdd:PHA03307 216 SASSPAPAPGRSAADDAGASSSDSSSSESSGCG 248
|
|
| |
